ENTRY EC 1.1.1.1 NAME alcohol dehydrogenase aldehyde reductase ADH alcohol dehydrogenase (NAD) aliphatic alcohol dehydrogenase ethanol dehydrogenase NAD-dependent alcohol dehydrogenase NAD-specific aromatic alcohol dehydrogenase NADH-alcohol dehydrogenase NADH-aldehyde dehydrogenase primary alcohol dehydrogenase yeast alcohol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME alcohol:NAD+ oxidoreductase REACTION an alcohol + NAD+ = an aldehyde or ketone + NADH + H+ SUBSTRATE alcohol NAD+ PRODUCT aldehyde ketone NADH H+ COMMENT A zinc protein. Acts on primary or secondary alcohols or hemi-acetals; the animal, but not the yeast, enzyme acts also on cyclic secondary alcohols. PATHWAY PATH: map00010 Glycolysis / Gluconeogenesis PATH: map00071 Fatty acid metabolism PATH: map00120 Bile acid biosynthesis PATH: map00350 Tyrosine metabolism PATH: map00561 Glycerolipid metabolism ORTHOLOG KO: K00001 alcohol dehydrogenase GENES HSA: 124(ADH1A) 125(ADH1B) 126(ADH1C) 127(ADH4) 128(ADH5) 130(ADH6) 131(ADH7) 137872(ADHFE1) MMU: 11522(Adh1) 11529(Adh7) 11532(Adh5) 26876(Adh4) RNO: 29646(Adh4) DME: CG32954-PA(CG32954) CG3425-PA(CG3425) CEL: D2063.1 H24K24.3a H24K24.3b K12G11.3 K12G11.4 Y38F1A.6 ATH: At1g22430(F12K8.22) At1g22440(F12K8.21) At1g32780(F6N18.16) At1g64710(F13O11.3) At1g77120(F22K20.19) At5g42250(K5J14.6) At5g43940(MRH10.4) At5g63620(MBK5.9) CME: CMS125C SCE: YBR145W(ADH5) YDL168W(SFA1) YGL256W(ADH4) YMR083W(ADH3) YMR303C(ADH2) YOL086C(ADH1) AGO: AAR084W(AAR084Wp) ABL033C(ABL033Cp) ACL148C(ACL148Cp) AER032W(AER032Wp) CAL: orf19.2394 orf19.2608(ADH5) orf19.2908 orf19.3997(ADH1) orf19.4504(ADH4) orf19.5113(ADH2) orf19.6816 orf19.7600(SFA1) SPO: SPAC5H10.06c SPCC13B11.01(adh) CHO: Chro.80199 ECO: b0356(frmA) b1241(adhE) b1478(adhP) b3589(yiaY) ECJ: JW0347(adhC) JW1228(adhE) JW1474(adhP) JW3562(yiaY) ECE: Z0456(adhC) Z2016(adhE) Z2232(adhP) Z5010(yiaY) ECS: ECs0411 ECs1741 ECs2082 ECs4466 ECC: c0465(adhC) c1705(adhE) c1911(adhP) c4410(yiaY) STY: STY1302(adh) STY1493(adhP) STY3830 STT: t1482(adhP) t1660(adh) t3575 STM: STM1567(adhP) STM1627 STM1749(adhE) STM4044 YPE: YPO1502 YPO2180(adhE) YPK: y2023(adhE) y2667(adhC) YPM: YP1392(adhC) YP1976(adhE) YPS: YPTB1517 YPTB2103(adhE) SFL: SF1240(adhE) SF1747(adhP) SF3627(yiaY) SFX: S1326(adhE) S1880(adhP) S4141(yiaY) ECA: ECA2326(adhE) ECA2714(adhC) ECA3950 PLU: plu1563 plu2496(adhE) plu4332(adhC) HIN: HI0185(adhC) PMU: PM1453(adh2) XFA: XF1746 XF2389 XFT: PD1406(yahK) XCC: XCC3389 XCC3475(adhC) XAC: XAC0652(adhC) XAC0734 XAC2826 VCH: VC2033 VVU: VV10344 VV13111 VV20019 VVY: VV0841 VV1175 VV2175 VVA0527 VPA: VP2121 VPA0071 VPA0566 PPR: PBPRA0784 PBPRA1103(adhE) PBPRA1480 PBPRA2519(yiaY) PAE: PA2119 PA2158 PA2188 PA3629(adhC) PA5427(adhA) PPU: PP1616 PP3839 PST: PSPTO1558(adhC) PSPTO4285(adhB) ACI: ACIAD1879(adhC) ACIAD1950 ACIAD2015 ACIAD2929 ACIAD3339(adhA) SON: SO1490(adhB) SO2054(adhC) SO2136(adhE) SOA0161 SOA0164 LPN: lpg2492 NME: NMB0546 NMB1304 NMB1395 NMA: NMA0725(adhA) NMA1518(adhC) CVI: CV0740(adhC) CV0808 CV1137(adhE) CV2051 CV2728 RSO: RS00473(adhA) RS00889 RS02044(adhC1) RS04838(adhC2) BMA: BMAA0132 BMAA0163 BMAA0709 BPS: BPSS1944(adhA) BPE: BP0777 BP2601 BP3751(adhI) BPA: BPP0339 BPP2723 BPP4251(adhI) BBR: BB0342 BB2775 BB4838(adhI) NEU: NE0620 NE0820 NE0907(adhC1) GSU: GSU0573 DVU: DVU2405 DVU2885 BBA: Bd0898(adhC) Bd2813(adh) DPS: DP0950 DP0951 DP1034 MLO: mlr0872 mlr1136 mlr1178 SME: SMa1156 SMa1296(adhA1) SMa2113(adhC2) SMb20170(fdh) SMc00105 SMc01270(adhC1) SMc04270 ATU: Atu0626(adhP) Atu1595 Atu1670(adhC) Atu2151(adh) ATC: AGR_C_1112 AGR_C_2931(adh4) AGR_C_3072 AGR_C_3897 BME: BMEI0925 BMEI1114 BMEI1746 BMEI1819 BMEII0553 BMEII0867 BMS: BR0203 BR0852 BR1061 BRA0734 BJA: bll4101 bll5655 bll7898 blr2780 blr3675 blr4874 blr6070 blr6215(adhC) RPA: RPA0374 RPA0656(badC) RPA1205 RPA1955 RPA2018 RPA3067 RPA3655 BHE: BH07430(adh) BQU: BQ05280(adh) CCR: CC2516 CC3029 BSU: BG11902(adhB) BG11941(gbsB) BG13553(yogA) BHA: BH1829(adhB) BAN: BA2222 BA2267 BA2647 BA3131(adhB) BA3566 BA4599 BAR: GBAA2222 GBAA2267 GBAA2647 GBAA3131(adhB) GBAA3566 GBAA4599 BAA: BA_2770 BA_3165 BA_3633 BA_4058 BA_5039 BAT: BAS2066 BAS2111 BAS2466 BAS2912 BAS3306 BAS4267 BCE: BC0802 BC2220 BC2660 BC3092 BC4365 BCA: BCE0198 BCE0742 BCE0877 BCE1099 BCE2252 BCE2296 BCE2677 BCE3145(adhB) BCE3521 BCE4453 BCZ: BTZK0168 BTZK0681 BTZK2005(gbsB) BTZK2048(adhB) BTZK2331(adhB) BTZK2390 BTZK2838(adhB) BTZK3221 BTZK4115 BTK: BT9727_0165 BT9727_2006(gbsB) BT9727_2050(adhB) BT9727_2367(adhB) BT9727_2429 BT9727_2881(adhB) BT9727_3273 BT9727_4104 BLI: BL00199 BL02473(adhB) BL02563(gbsB) BL05087 BLD: BLi03502 OIH: OB1376 OB2738 SAU: SA0143(adhE) SA0562(adh1) SAV: SAV0148(adhE) SAV0605(adh1) SAM: MW0123(adhE) MW0568(adh1) SAR: SAR0150(adhE) SAR0613(adhA) SAS: SAS0123 SAS0573 SEP: SE0375 SE0506 SE2098 LMO: lmo1634 LMF: LMOf2365_1656(adhE) LIN: lin1675 LLA: L13145(adhE) L190278(ypjA) L55758(adhA) SPY: SPy0044(adhA) SPy1111 SPM: spyM18_0043(adhE) spyM18_0045(adhP) spyM18_1073 SPG: SpyM3_0036(adh2) SpyM3_0037(adh1) SpyM3_0772 SPS: SPs0037 SPs0038 SPs0972 SPA: M6_Spy0088 M6_Spy0090 M6_Spy0832 M6_Spy0833 SPN: SP0285 SP1855 SP2026 SP2055 SP2157 SPR: spr0262(adhP) spr1670(adhB) spr1837(adhE) spr1866(adh) spr1963(adh2) SAG: SAG0053(adhE) SAG0054(adhP) SAG0428 SAG1637(adh) SAN: gbs0053 gbs0054 gbs1684 SMU: SMU.119(adh) SMU.148(adhE) SMU.1867c LPL: lp_1665(adh1) lp_2873(adh2) lp_3662(adhE) LJO: LJ1120 LJ1766 EFA: EF0900(adhE) EF1826 CAC: CAC3375 CAP0035(adhe) CAP0162(adhe1) CPE: CPE0449(adh) CPE2531(adhE) CTC: CTC01366 CTC01453 TTE: TTE0696(eutG) MPE: MYPE4620(gbsB) MTU: Rv0162c(adhE) Rv0761c(adhB) Rv1862(adhA) MTC: MT0786 MT1911 MBO: Mb0167c(adhE1) Mb0784c(adhB) Mb1557(adh) Mb1893(adhA) MLE: ML2053 MPA: MAP0595c(adhB) MAP1571(adhA_1) MAP1613c(adhA_2) MAP3596c(adhE) CGL: NCgl0219(Cgl0222) NCgl2449(Cgl2537) NCgl2709(Cgl2807) CEF: CE0053 CDI: DIP2114(adhA) SCO: SCO0199(SCJ12.11c) SCO5262(2SC7G11.24) SMA: SAV1141 SAV1357 SAV1393 SAV2980 SAV414(pteB) SAV5335 SAV7169 TWH: TW326(adh) TWS: TW445(adh) LXX: Lxx22610(adh) PAC: PPA0539 BLO: BL1090 BL1131(badC) BL1575(adh2) STH: STH2049 RBA: RB10805 RB13260(yhdH) RB4131(yjjN) RB5320 RB5856(adh) RB5948(adh) LIL: LA0296 LA0325 LA1616(adeH) LA2361 LA2629 LA3158 LIC: LIC10253 LIC10282 LIC10958 LIC11357 LIC11586 LIC12166 SYN: sll0990 SYC: syc1059_d TEL: tlr0227 GVI: gll4111 glr4425 ANA: all0879 all2810 all5334 TTH: TTC0097 TTC1572 AAE: aq_1240(adh2) aq_1362(adh1) TMA: TM0111 TM0920 MMP: MMP0802 MAC: MA2630(adh) MMA: MM2769 AFU: AF0024 AF0339 AF2019 AF2101 HAL: VNG1821G(adh4) HMA: pNG7022(adh1) pNG7032(adh10) pNG7101(adh8) pNG7103(adh7) pNG7278(adh12) pNG7289(adh6) pNG7314(adhC) pNG7351(adh13) rrnAC0012(adh11) rrnAC0191(adh3) rrnAC1300(adh9) rrnAC1402(adh4) rrnAC1975(adh5) rrnAC2172(adh14) rrnAC3506(adh2) TAC: Ta0832 Ta0833 Ta0841 TVO: TVG0387048 TVG0995648 TVG1348694 PTO: PTO0846 PTO1151 PTO1249 PHO: PH0743 PAB: PAB1511 PFU: PF0608 APE: APE1245 APE1557 APE1963 APE2239 SSO: SSO0472(adh-1) SSO0764(adh-2) SSO1646(adh-5) SSO2494(adh-8) SSO2536(adh-10) SSO2878(adh-13) STO: ST0038 ST0053 ST0075 ST0480 ST2056 ST2577 PAI: PAE1921 PAE2051 PAE2332 PAE2931 DISEASE MIM: 103735 Alcohol dehydrogenase 6 (aldehyde reductase) MIM: 103740 Alcohol dehydrogenase (class II), pi polypeptide MIM: 600086 Alcohol dehydrogenase-7 MOTIF PS: PS00059 G-H-E-x(2)-G-x(5)-[GA]-x(2)-[IVSAC] PS: PS00060 [GSW]-x-[LIVTSACD]-[GH]-x(2)-[GSAE]-[GSHYQ]-x-[LIVTP]- [GAST]-[GAS]-x(3)-[LIVMT]-x-[HNS]-[GA]-x-[GTAC] PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] PS: PS00913 [STALIV]-[LIVF]-x-[DE]-x(6,7)-P-x(4)-[ALIV]-x-[GST]- x(2)-D-[TAIVM]-[LIVMF]-x(4)-E STRUCTURES PDB: 1A4U 1A71 1A72 1ADB 1ADC 1ADF 1ADG 1AGN 1AXE 1AXG 1B14 1B15 1B16 1B2L 1BTO 1CDO 1D1S 1D1T 1DEH 1E3E 1E3I 1E3L 1EE2 1H2B 1HDX 1HDY 1HDZ 1HET 1HEU 1HF3 1HLD 1HSO 1HSZ 1HT0 1HTB 1JU9 1JVB 1LDE 1LDY 1LLU 1M6H 1M6W 1MA0 1MC5 1MG0 1MG5 1MGO 1MP0 1N8K 1N92 1NTO 1NVG 1O2D 1P1R 1QLH 1QLJ 1QV6 1QV7 1R37 1RJW 1TEH 1U3T 1U3U 1U3V 1U3W 1VJ0 2OHX 2OXI 3BTO 3HUD 5ADH 6ADH 7ADH REFERENCE 1 Branden, G.-I., Jornvall, H., Eklund, H. and Furugren, B. Alcohol dehydrogenase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic Press, New York, 1975, p. 103-190. 2 [PMID:320001] Jornvall, H. Differences between alcohol dehydrogenases. Structural properties and evolutionary aspects. Eur. J. Biochem. 72 (1977) 443-452. 3 Negelein, E. and Wulff, H.-J. Diphosphopyridinproteid ackohol, acetaldehyd. Biochem. Z. 293 (1937) 351-389. 4 Sund, H. and Theorell, H. Alcohol dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 25-83. 5 Theorell, H. Kinetics and equilibria in the liver alcohol dehydrogenase system. Adv. Enzymol. Relat. Subj. Biochem. 20 (1958) 31-49. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.1 ExPASy - ENZYME nomenclature database: 1.1.1.1 ERGO genome analysis and discovery system: 1.1.1.1 UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.1 BRENDA, the Enzyme Database: 1.1.1.1 CAS: 9031-72-5 /// ENTRY EC 1.1.1.2 NAME alcohol dehydrogenase (NADP+) aldehyde reductase (NADPH2) NADP-alcohol dehydrogenase NADP-aldehyde reductase NADP-dependent aldehyde reductase NADPH-aldehyde reductase NADPH-dependent aldehyde reductase nonspecific succinic semialdehyde reductase ALR 1 low-K(m) aldehyde reductase high-K(m) aldehyde reductase alcohol dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME alcohol:NADP+ oxidoreductase REACTION an alcohol + NADP+ = an aldehyde + NADPH + H+ SUBSTRATE alcohol NADP+ PRODUCT aldehyde NADPH H+ COMMENT A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. A-specific with respect to NADPH. PATHWAY PATH: map00010 Glycolysis / Gluconeogenesis PATH: map00561 Glycerolipid metabolism PATH: map00930 Caprolactam degradation ORTHOLOG KO: K00002 alcohol dehydrogenase (NADP+) GENES HSA: 10327(AKR1A1) MMU: 58810(Akr1a4) RNO: 78959(Akr1a1) CME: CMM296C CAL: orf19.5517(ADH6) orf19.6757(GCY1) orf19.6758(GCY2) XFA: XF1136 XF1727 XF1734 XFT: PD0423(adhP) XCC: XCC0029(yahK) XAC: XAC0031(yahK) PAE: PA2275 PPU: PP2426 PST: PSPTO2182 PSPTO2697 LPN: lpg0612 CVI: CV2051 RSO: RS01534 RS05494 BPS: BPSL0192(adhC) HPY: HP1104 HPJ: jhp1030 jhp1429 HHE: HH1166(cad) CJE: Cj1548c BBA: Bd0900(adhA) SME: SMc00680 ATU: Atu2022(adh) ATC: AGR_C_3663A BSU: BG12562(adhA) BLI: BL05196(adhA) OIH: OB0786 MPN: H03_orf351(adh) MPE: MYPE5230(adhA) MTU: Rv3045(adhC) MTC: MT3130 MBO: Mb3071(adhC) MLE: ML1730(adhA) MPA: MAP3093(adhC) CGL: NCgl0324(Cgl0331) CEF: CE0149 CE0338 SCO: SCO4945(2SCK31.05) SMA: SAV3314(adhA) PAC: PPA1072 LIL: LA3172 LIC: LIC10949(dkgA) SYN: slr0942 MAC: MA0403 MA1901(adh) HMA: pNG7101(adh8) DISEASE MIM: 103830 Aldo-keto reductase family 1, member A1 (aldehyde reductase) MOTIF PS: PS00059 G-H-E-x(2)-G-x(5)-[GA]-x(2)-[IVSAC] PS: PS00062 [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY] PS: PS00063 [LIVM]-[PAIV]-[KR]-[ST]-x(4)-R-x(2)-[GSTAEQK]-[NSL]- x(2)-[LIVMFA] PS: PS00798 G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGC]-[AS]-x(5)-E-x(2)- [LIVM]-G STRUCTURES PDB: 1AE4 1BXZ 1C9W 1CWN 1HQT 1JQB 1KEV 1NXQ 1P0C 1P0F 1PED 1UJM 1YKF 2ALR REFERENCE 1 [PMID:4402936] Bosron, W.F. and Prairie, R.L. Triphosphopyridine nucleotide-linked aldehyde reductase. I. Purification and properties of the enzyme from pig kidney cortex. J. Biol. Chem. 247 (1972) 4480-4485. 2 DeMoss, R. Triphosphopyridine nucleotide-specific ethanol dehydrogenase from Leuconostoc mesenteroides. Bacteriol. Proc. (1953) 81. 3 Reeves, R.E., Montalvo, F.E. and Lushbaugh, T.S. Nicotinamide-adenine dinucleotide phosphate-dependent alcohol dehydrogenase. Enzyme from Entamoeba histolytica and some enzyme inhibitors. Int. J. Biochem. 2 (1971) 55-64. 4 [PMID:4393513] Tabakoff, B. and Erwin, V.G. Purification and characterization of a reduced nicotinamide adenine dinucleotide phosphate-linked aldehyde reductase from brain. J. Biol. Chem. 245 (1970) 3263-3268. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.2 ExPASy - ENZYME nomenclature database: 1.1.1.2 ERGO genome analysis and discovery system: 1.1.1.2 BRENDA, the Enzyme Database: 1.1.1.2 CAS: 9028-12-0 /// ENTRY EC 1.1.1.3 NAME homoserine dehydrogenase HSDH HSD CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-homoserine:NAD(P)+ oxidoreductase REACTION L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ SUBSTRATE L-homoserine NAD+ NADP+ PRODUCT L-aspartate 4-semialdehyde NADH NADPH H+ COMMENT The yeast enzyme acts most rapidly with NAD+; the Neurospora enzyme with NADP+. The enzyme from Escherichia coli is a multi-functional protein, which also catalyses the reaction of EC 2.7.2.4 (aspartate kinase). PATHWAY PATH: map00260 Glycine, serine and threonine metabolism PATH: map00300 Lysine biosynthesis ORTHOLOG KO: K00003 homoserine dehydrogenase GENES ATH: At1g31230(F28K20.19) At4g19710(T16H5.70) CME: CMN129C SCE: YJR139C(HOM6) AGO: ABL080W(ABL080Wp) CAL: orf19.2951(HOM6) SPO: SPBC776.03 ECO: b0002(thrA) b3940(metL) ECJ: JW0001(thrA) JW3911(metL) ECE: Z0002(thrA) Z5495(metL) ECS: ECs0002 ECs4869 ECC: c0003(thrA) c4893(metL) STY: STY0002(thrA) STY3768(metL) STT: t0002(thrA) t3517(metL) STM: STM0002(thrA) STM4101(metL) YPE: YPO0116(metL) YPO0459(thrA) YPK: y0303(metL) y3718(thrA) YPM: YP0118(metL) YP3723(thrA) YPS: YPTB0106(metM) YPTB0602(thrA) SFL: SF0002(thrA) SF4018(metL) SFX: S0002(thrA) S3729(metL) ECA: ECA3891(thrA) ECA4251(metL) PLU: plu0563(thrA) plu4755(metL) BUC: BU194(thrA) BAS: BUsg188(thrA) BAB: bbp183(thrA) WBR: Wbr0162(thrA) BFL: Bfl111(thrA) HIN: HI0089(thrA) PMU: PM0113(thrA) XFA: XF2225 XFT: PD1273(lysC) XCC: XCC1800(metL) XAC: XAC1820(metL) VCH: VC2364 VC2684 VVU: VV10545 VV11365 VVY: VV0650 VV3007 VPA: VP0494 VP2764 PPR: PBPRA0262 PBPRA0552 PAE: PA3736(hom) PPU: PP0664 PP1470(hom) PST: PSPTO1480(hom) ACI: ACIAD0264(hom) SON: SO3415(thrA) SO4055(metL) MCA: MCA0597(hom) NME: NMB1228 NMA: NMA1395(hom) CVI: CV0996(metL) RSO: RS02849 BMA: BMA1385(hom) BPS: BPSL1477(hom) BPE: BP2784 BPA: BPP2479 BBR: BB1926 NEU: NE2369 HPY: HP0822(hom) HPJ: jhp0761 HHE: HH1750(hom) WSU: WS0450(hom) CJE: Cj0149c(hom) GSU: GSU1693(hom) DVU: DVU0890(hom) DPS: DP1732 MLO: mll0934 SME: SMc00293(thrA) ATU: Atu1588(hom) ATC: AGR_C_2919 BME: BMEI0725 BMS: BR1274(hom) BJA: blr4362(hom) RPA: RPA2504(hdh) BHE: BH10030(metM) CCR: CC1383 BSU: BG10460(hom) BHA: BH1253 BH1737 BH3422(hom) BAN: BA1968(hom-1) BA2608 BA5654(hom-2) BAR: GBAA1968(hom-1) GBAA2608 GBAA5654(hom-2) BAA: BA_0512 BA_2468 BA_3119 BAT: BAS1825 BAS2433 BAS5256 BCE: BC1964 BC2548 BC5404 BCA: BCE2051(hom) BCE2626 BCE5533(hom) BCZ: BTZK1782(hom) BTZK2354(hom) BTZK5102(hom) BTK: BT9727_1799(hom) BT9727_2388(hom) BT9727_5085(hom) BLI: BL02137(hom) OIH: OB0466 SAU: SA1164(dhoM) SAV: SAV1328(dhoM) SAM: MW1215(dhoM) SAR: SAR1338 SAS: SAS1268 SEP: SE1009 LMO: lmo2547(hom) LMF: LMOf2365_2520(hom) LIN: lin2691(hom) LLA: L0090(hom) SPN: SP1361 SPR: spr1219(hom) SAG: SAG1120(hom) SAN: gbs1187 SMU: SMU.965 LPL: lp_0571(hom2) lp_2535(hom1) EFA: EF2422(hom) CAC: CAC0998 CTC: CTC00886 CTC02355 TTE: TTE2620(thrA2) MTU: Rv1294(thrA) MTC: MT1333 MBO: Mb1326(thrA) MLE: ML1129(hom) MPA: MAP2468c(thrA) CGL: NCgl1136(Cgl1183) CEF: CE1289 CDI: DIP1036(thrA) SCO: SCO5354(SCBAC5H2.23) SMA: SAV2918(thrA) TWH: TW439(thrA) TWS: TW329(hom) LXX: Lxx06870(thrA) PAC: PPA1258 BLO: BL1274(thrA) STH: STH2739 RBA: RB8510(hom) LIL: LA3638(thrA) LIC: LIC10571(hom) BTH: BT2403 SYN: sll0455(thrA) SYW: SYNW0711(thrA) SYC: syc2003_c(thrA) TEL: tll0277(thrA) GVI: gll4295(thrA) ANA: all4120(thrA) PMA: Pro1150(thrA) PMM: PMM1051(thrA) PMT: PMT1143(thrA) CTE: CT2030 DRA: DR1278 TTH: TTC0115 AAE: aq_1812(thrA) TMA: TM0547 MJA: MJ1602(hom) MMP: MMP1702(hom) MAC: MA2572 MMA: MM2713 MTH: MTH1232 MTH417 MKA: MK1554(thrA) AFU: AF0935(hom) HAL: VNG2650G(hom) HMA: rrnAC2408(hom) TAC: Ta1179 TVO: TVG0375766 PTO: PTO1417 PHO: PH1075 PAB: PAB0610(hom) PFU: PF1104 APE: APE1144 SSO: SSO0657(thrA) STO: ST1519 PAI: PAE2868 MOTIF PS: PS00324 [LIVM]-x-K-[FY]-G-G-[ST]-[SC]-[LIVM] PS: PS01042 A-x(3)-G-[LIVMFY]-[STAG]-x(2,3)-[DNS]-P-x(2)-D-[LIVM]- x-G-x-D-x(3)-K STRUCTURES PDB: 1EBF 1EBU 1Q7G 1TVE REFERENCE 1 Black, S. and Wright, N.G. Homoserine dehydrogenase. J. Biol. Chem. 213 (1955) 51-60. 2 [PMID:4551091] Starnes, W.L., Munk, P., Maul, S.B., Cunningham, G.N., Cox, D.J. and Shive, W. Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex. Biochemistry 11 (1972) 677-687. 3 [PMID:4562990] Veron, M., Falcoz-Kelly, F. and Cohen, G.N. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain. Eur. J. Biochem. 28 (1972) 520-527. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.3 ExPASy - ENZYME nomenclature database: 1.1.1.3 ERGO genome analysis and discovery system: 1.1.1.3 BRENDA, the Enzyme Database: 1.1.1.3 CAS: 9028-13-1 /// ENTRY EC 1.1.1.4 NAME (R,R)-butanediol dehydrogenase butyleneglycol dehydrogenase D-butanediol dehydrogenase D-(-)-butanediol dehydrogenase butylene glycol dehydrogenase diacetyl (acetoin) reductase D-aminopropanol dehydrogenase 1-amino-2-propanol dehydrogenase 2,3-butanediol dehydrogenase D-1-amino-2-propanol dehydrogenase (R)-diacetyl reductase (R)-2,3-butanediol dehydrogenase D-1-amino-2-propanol:NAD+ oxidoreductase 1-amino-2-propanol oxidoreductase aminopropanol oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R,R)-butane-2,3-diol:NAD+ oxidoreductase REACTION (R,R)-butane-2,3-diol + NAD+ = (R)-acetoin + NADH + H+ SUBSTRATE (R,R)-butane-2,3-diol NAD+ PRODUCT (R)-acetoin NADH H+ COMMENT Also converts diacetyl into acetoin with NADH as reductant. PATHWAY PATH: map00650 Butanoate metabolism ORTHOLOG KO: K00004 (R,R)-butanediol dehydrogenase GENES ATH: At5g06580(F15M7.11) CAL: orf19.5288(YAL60) orf19.769 ACI: ACIAD1021 SME: SMc01455(dld) ATU: Atu2053 ATC: AGR_C_3718 BCE: BC0668 BCA: BCE3248(gutB) SPA: M6_Spy0555 REFERENCE 1 Strecker, H.J. and Harary, I. Bacterial butylene glycol dehydrogenase and diacetyl reductase. J. Biol. Chem. 211 (1954) 263-270. 2 Taylor, M.B. and Juni, E. Stereoisomeric specificities of 2,3-butanediol dehydrogenase. Biochim. Biophys. Acta 39 (1960) 448-457. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.4 ExPASy - ENZYME nomenclature database: 1.1.1.4 ERGO genome analysis and discovery system: 1.1.1.4 BRENDA, the Enzyme Database: 1.1.1.4 CAS: 37250-09-2 /// ENTRY EC 1.1.1.5 NAME acetoin dehydrogenase diacetyl reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME acetoin:NAD+ oxidoreductase REACTION acetoin + NAD+ = diacetyl + NADH + H+ SUBSTRATE acetoin NAD+ PRODUCT diacetyl NADH H+ COMMENT NADP+ also acts as acceptor. PATHWAY PATH: map00650 Butanoate metabolism ORTHOLOG KO: K03366 acetoin dehydrogenase GENES RNO: 171408(glb) ECA: ECA0310(budC) ACI: ACIAD1022(budC) BLD: BLi02066 SAU: SA0122(butA) SAV: SAV0126(butA) SAM: MW0100(butA) SAR: SAR0129 SAS: SAS0101 SEP: SE2225 LLA: L118271(butA) SPA: M6_Spy0555 SMU: SMU.1322(budC) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] STRUCTURES PDB: 1GEG REFERENCE 1 [PMID:4152609] Diez, V., Burgos, J. and Martin, R. Pigeon liver diacetyl reductase: purification and some properties. Biochim. Biophys. Acta 350 (1974) 253-262. 2 Strecker, H.J. and Harary, I. Bacterial butylene glycol dehydrogenase and diacetyl reductase. J. Biol. Chem. 211 (1954) 263-270. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.5 ExPASy - ENZYME nomenclature database: 1.1.1.5 ERGO genome analysis and discovery system: 1.1.1.5 BRENDA, the Enzyme Database: 1.1.1.5 CAS: 9028-49-3 /// ENTRY EC 1.1.1.6 NAME glycerol dehydrogenase glycerin dehydrogenase NAD-linked glycerol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME glycerol:NAD+ 2-oxidoreductase REACTION glycerol + NAD+ = glycerone + NADH + H+ SUBSTRATE glycerol NAD+ PRODUCT glycerone NADH H+ COMMENT Also acts on propane-1,2-diol. PATHWAY PATH: map00561 Glycerolipid metabolism ORTHOLOG KO: K00005 glycerol dehydrogenase GENES SPO: SPAC13F5.03c ECO: b3945(gldA) ECJ: JW3917(gldA) ECE: Z5500(gldA) ECS: ECs4874 ECC: c4904(gldA) STY: STY3759(gldA) STT: t3509(gldA) STM: STM3529 STM4108(gldA) ECA: ECA0846(gldA) ECA1523 PLU: plu4115(gldA) VVY: VV0158 VPA: VP0363 SME: SMc02038(gldA) BLI: BL03089 BLD: BLi00828 OIH: OB0323 OB3328 SEP: SE0235 SPY: SPy2047(gldA) SPM: spyM18_2108(gldA) SPG: SpyM3_1747(gldA) SPS: SPs1745 SPA: M6_Spy1741 SPN: SP0253 SPR: spr0234(gldA) SAG: SAG0333(gldA) SAG2046 SAN: gbs0321 gbs2002 SMU: SMU.1309c SMU.495(gldA) EFA: EF1358 CPE: CPE0099(gldA) CTC: CTC00596 CDI: DIP1893 STH: STH1267 SYN: slr1167(gldA) SYW: SYNW0939 SYC: syc1815_d(gldA) syc2433_d(gldA) TEL: tll2051(gldA) GVI: gll1456 ANA: alr2764 PMA: Pro1108(gldA) PMM: PMM1087(gldA) PMT: PMT1062(gldA) TMA: TM0423 HAL: VNG6270G(gldA) HMA: rrnAC0175(gldA) MOTIF PS: PS00060 [GSW]-x-[LIVTSACD]-[GH]-x(2)-[GSAE]-[GSHYQ]-x-[LIVTP]- [GAST]-[GAS]-x(3)-[LIVMT]-x-[HNS]-[GA]-x-[GTAC] PS: PS00913 [STALIV]-[LIVF]-x-[DE]-x(6,7)-P-x(4)-[ALIV]-x-[GST]- x(2)-D-[TAIVM]-[LIVMF]-x(4)-E STRUCTURES PDB: 1JPU 1JQ5 1JQA REFERENCE 1 Asnis, R.E. and Brodie, A.F. A glycerol dehydrogenase from Escherichia coli. J. Biol. Chem. 203 (1953) 153-159. 2 Burton, R.M. and Kaplan, N.O. A DPN specific glycerol dehydrogenase from Aerobacter aerogenes. J. Am. Chem. Soc. 75 (1953) 1005-1007. 3 Lin, E.C.C. and Magasanik, B. The activation of glycerol dehydrogenase from Aerobacter aerogenes by monovalent cations. J. Biol. Chem. 235 (1960) 1820-1823. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.6 ExPASy - ENZYME nomenclature database: 1.1.1.6 ERGO genome analysis and discovery system: 1.1.1.6 BRENDA, the Enzyme Database: 1.1.1.6 CAS: 9028-14-2 /// ENTRY EC 1.1.1.7 NAME propanediol-phosphate dehydrogenase PDP dehydrogenase 1,2-propanediol-1-phosphate:NAD+ oxidoreductase propanediol phosphate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME propane-1,2-diol-1-phosphate:NAD+ oxidoreductase REACTION propane-1,2-diol 1-phosphate + NAD+ = hydroxyacetone phosphate + NADH + H+ SUBSTRATE propane-1,2-diol 1-phosphate NAD+ PRODUCT hydroxyacetone phosphate NADH H+ REFERENCE 1 Sellinger, O.Z. and Miller, O.N. The metabolism of acetol phosphate. II. 1,2-Propanediol-1-phosphate dehydrogenase. J. Biol. Chem. 234 (1959) 1641-1646. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.7 ExPASy - ENZYME nomenclature database: 1.1.1.7 ERGO genome analysis and discovery system: 1.1.1.7 BRENDA, the Enzyme Database: 1.1.1.7 CAS: 9028-15-3 /// ENTRY EC 1.1.1.8 NAME glycerol-3-phosphate dehydrogenase (NAD+) alpha-glycerol phosphate dehydrogenase (NAD) alpha-glycerophosphate dehydrogenase (NAD) glycerol 1-phosphate dehydrogenase glycerol phosphate dehydrogenase (NAD) glycerophosphate dehydrogenase (NAD) hydroglycerophosphate dehydrogenase L-alpha-glycerol phosphate dehydrogenase L-alpha-glycerophosphate dehydrogenase L-glycerol phosphate dehydrogenase L-glycerophosphate dehydrogenase NAD-alpha-glycerophosphate dehydrogenase NAD-dependent glycerol phosphate dehydrogenase NAD-dependent glycerol-3-phosphate dehydrogenase NAD-L-glycerol-3-phosphate dehydrogenase NAD-linked glycerol 3-phosphate dehydrogenase NADH-dihydroxyacetone phosphate reductase glycerol-3-phosphate dehydrogenase (NAD) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase REACTION sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+ SUBSTRATE sn-glycerol 3-phosphate NAD+ PRODUCT glycerone phosphate NADH H+ COMMENT Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity). PATHWAY PATH: map00561 Glycerolipid metabolism ORTHOLOG KO: K00006 glycerol-3-phosphate dehydrogenase (NAD+) GENES HSA: 2819(GPD1) MMU: 14555(Gpd1) RNO: 60666(Gpd3) DME: CG3215-PA(CG3215) CG9042-PA(CG9042) CG9042-PB(CG9042) CG9042-PC(CG9042) CEL: F47G4.3 K11H3.1a ATH: At5g40610(MNF13.130) CME: CMD113C SCE: YDL022W(GPD1) YOL059W(GPD2) AGO: ADR311C(ADR311Cp) CAL: orf19.1756(GPD2) orf19.691(GPD1) SPO: SPAC23D3.04c(gpd2) SPBC215.05(gpd1) ECU: ECU05_0270 PFA: PF11_0157 PFL0780w CHO: Chro.20028 WOL: WD0731(gpsA) DISEASE MIM: 138420 Glycerol-3-phosphate dehydrogenase, soluble MOTIF PS: PS00957 G-[ATIV]-[LIVMYC]-K-[DN]-[LIVM]-[LIVMFY]-[GA]-x-[GA]-x- G-[LIVMF]-x(2)-[SGA]-[LIVM]-x-[LIVMFYW]-G-x-N STRUCTURES PDB: 1EVY 1EVZ 1JDJ 1M66 1M67 1N1E 1N1G REFERENCE 1 Baranowski, T. alpha-Glycerophosphate dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 85-96. 2 [PMID:4307630] Brosemer, R.W. and Kuhn, R.W. Comparative structural properties of honeybee and rabbit alpha-glycerophosphate dehydrogenases. Biochemistry 8 (1969) 2095-2105. 3 [PMID:4389388] Kito, M. and Pizer, L.I. Purification and regulatory properties of the biosynthetic L-glycerol 3-phosphate dehydrogenase from Escherichia coli. J. Biol. Chem. 244 (1969) 3316-3323. 4 [PMID:4340553] O'Brien, S.J. and MacIntyre, R.J. The alpha-glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects. Biochem. Genet. 7 (1972) 141-161. 5 [PMID:4200180] Warkentin, K.L. and Fondy, T.P. Isolation and characterization of cytoplasmic L-glycerol-3-phosphate dehydrogenase from rabbit-renal-adipose tissue and its comparison with the skeletal-muscle enzyme. Eur. J. Biochem. 36 (1973) 97-109. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.8 ExPASy - ENZYME nomenclature database: 1.1.1.8 ERGO genome analysis and discovery system: 1.1.1.8 BRENDA, the Enzyme Database: 1.1.1.8 CAS: 9075-65-4 /// ENTRY EC 1.1.1.9 NAME D-xylulose reductase NAD-dependent xylitol dehydrogenase xylitol dehydrogenase erythritol dehydrogenase 2,3-cis-polyol(DPN) dehydrogenase (C3-5) pentitol-DPN dehydrogenase xylitol-2-dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME xylitol:NAD+ 2-oxidoreductase (D-xylulose-forming) REACTION xylitol + NAD+ = D-xylulose + NADH + H+ SUBSTRATE xylitol NAD+ PRODUCT D-xylulose NADH H+ COMMENT Also acts as an L-erythrulose reductase. PATHWAY PATH: map00040 Pentose and glucuronate interconversions ORTHOLOG KO: K05351 D-xylulose reductase MOTIF PS: PS00059 G-H-E-x(2)-G-x(5)-[GA]-x(2)-[IVSAC] REFERENCE 1 Chiang, C. and Knight, S.G. A new pathway of pentose metabolism. Biochem. Biophys. Res. Commun. 3 (1960) 554-559. 2 Hickman, J. and Ashwell, G. A sensitive and stereospecific enzymatic assay for xylulose. J. Biol. Chem. 234 (1959) 758-761. 3 Jakoby, W.B. and Fredericks, J. Erythritol dehydrogenase from Aerobacter aerogenes. Biochim. Biophys. Acta 48 (1961) 26-32. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.9 ExPASy - ENZYME nomenclature database: 1.1.1.9 ERGO genome analysis and discovery system: 1.1.1.9 BRENDA, the Enzyme Database: 1.1.1.9 CAS: 9028-16-4 /// ENTRY EC 1.1.1.10 NAME L-xylulose reductase xylitol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME xylitol:NADP+ 4-oxidoreductase (L-xylulose-forming) REACTION xylitol + NADP+ = L-xylulose + NADPH + H+ SUBSTRATE xylitol NADP+ PRODUCT L-xylulose NADPH H+ PATHWAY PATH: map00040 Pentose and glucuronate interconversions ORTHOLOG KO: K03331 L-xylulose reductase GENES RNO: 171408(glb) STRUCTURES PDB: 1PR9 REFERENCE 1 [PMID:2981816] Doten, R.C. and Mortlock, R.P. Characterization of xylitol-utilizing mutants of Erwinia uredovora. J. Bacteriol. 161 (1985) 529-533. 2 Hickman, J. and Ashwell, G. A sensitive and stereospecific enzymatic assay for xylulose. J. Biol. Chem. 234 (1959) 758-761. 3 Hollmann, S. and Touster, O. The L-xylulose-xylitol enzyme and other polyol dehydrogenases of guinea pig liver mitochondria. J. Biol. Chem. 225 (1957) 87-102. 4 Touster, O., Reynolds, V.H. and Hutcheson, R.M. The reduction of L-xylulose to xylitol by guinea pig liver mitochondria. J. Biol. Chem. 221 (1956) 697-709. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.10 ExPASy - ENZYME nomenclature database: 1.1.1.10 ERGO genome analysis and discovery system: 1.1.1.10 BRENDA, the Enzyme Database: 1.1.1.10 CAS: 9028-17-5 /// ENTRY EC 1.1.1.11 NAME D-arabinitol 4-dehydrogenase D-arabitol dehydrogenase arabitol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-arabinitol:NAD+ 4-oxidoreductase REACTION D-arabinitol + NAD+ = D-xylulose + NADH + H+ SUBSTRATE D-arabinitol NAD+ PRODUCT D-xylulose NADH H+ PATHWAY PATH: map00040 Pentose and glucuronate interconversions PATH: map00051 Fructose and mannose metabolism ORTHOLOG KO: K00007 D-arabinitol 4-dehydrogenase GENES YPE: YPO2325(dalD) YPK: y2008 YPM: YP2112(dalD) YPS: YPTB2244(dalD) RSO: RS01475(dalD) BPS: BPSL0840(dalD) REFERENCE 1 Lin, E.C.C. An inducible D-arabitol dehydrogenase from Aerobacter aerogenes. J. Biol. Chem. 236 (1961) 31-36. 2 Wood, W.A., McDonough, M.J. and Jacobs, L.B. Ribitol and D-arabitol utilization by Aerobacter aerogenes. J. Biol. Chem. 236 (1961) 2190-2195. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.11 ExPASy - ENZYME nomenclature database: 1.1.1.11 ERGO genome analysis and discovery system: 1.1.1.11 BRENDA, the Enzyme Database: 1.1.1.11 CAS: 9028-18-6 /// ENTRY EC 1.1.1.12 NAME L-arabinitol 4-dehydrogenase pentitol-DPN dehydrogenase L-arabitol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming) REACTION L-arabinitol + NAD+ = L-xylulose + NADH + H+ SUBSTRATE L-arabinitol NAD+ PRODUCT L-xylulose NADH H+ PATHWAY PATH: map00040 Pentose and glucuronate interconversions REFERENCE 1 Chiang, C. and Knight, S.G. A new pathway of pentose metabolism. Biochem. Biophys. Res. Commun. 3 (1960) 554-559. 2 Chiang, C. and Knight, S.G. L-Arabinose metabolism by cell-free extracts of Penicillium chrysogenum. Biochim. Biophys. Acta 46 (1961) 271-278. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.12 ExPASy - ENZYME nomenclature database: 1.1.1.12 ERGO genome analysis and discovery system: 1.1.1.12 BRENDA, the Enzyme Database: 1.1.1.12 CAS: 9028-19-7 /// ENTRY EC 1.1.1.13 NAME L-arabinitol 2-dehydrogenase L-arabinitol dehydrogenase (ribulose-forming) L-arabinitol (ribulose-forming) dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-arabinitol:NAD+ 2-oxidoreductase (L-ribulose-forming) REACTION L-arabinitol + NAD+ = L-ribulose + NADH + H+ SUBSTRATE L-arabinitol NAD+ PRODUCT L-ribulose NADH H+ PATHWAY PATH: map00040 Pentose and glucuronate interconversions REFERENCE 1 Chiang, C. and Knight, S.G. L-Arabinose metabolism by cell-free extracts of Penicillium chrysogenum. Biochim. Biophys. Acta 46 (1961) 271-278. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.13 ExPASy - ENZYME nomenclature database: 1.1.1.13 ERGO genome analysis and discovery system: 1.1.1.13 BRENDA, the Enzyme Database: 1.1.1.13 CAS: 9028-20-0 /// ENTRY EC 1.1.1.14 NAME L-iditol 2-dehydrogenase polyol dehydrogenase sorbitol dehydrogenase L-iditol:NAD+ 5-oxidoreductase L-iditol (sorbitol) dehydrogenase glucitol dehydrogenase L-iditol:NAD oxidoreductase NAD+-dependent sorbitol dehydrogenase NAD-dependent sorbitol dehydrogenase NAD-sorbitol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-iditol:NAD+ 2-oxidoreductase REACTION L-iditol + NAD+ = L-sorbose + NADH + H+ SUBSTRATE L-iditol NAD+ PRODUCT L-sorbose NADH H+ COMMENT Also acts on D-glucitol (giving D-fructose) and other closely related sugar alcohols. PATHWAY PATH: map00051 Fructose and mannose metabolism ORTHOLOG KO: K00008 L-iditol 2-dehydrogenase GENES HSA: 6652(SORD) MMU: 20322(Sdh1) RNO: 24788(Sord) DME: CG1982-PA(CG1982) CG4649-PA(CG4649) CEL: R04B5.5 R04B5.6 ATH: At5g51970(MSG15.7) CME: CMA009C SCE: YDL246C YJR159W(SOR1) AGO: ABR229C(ABR229Cp) CAL: orf19.7676(SOR1) SPO: SPBC1773.05c(tms1) YPE: YPO2502(gutB) YPK: y1686 YPM: YP2317 YPS: YPTB2538(gutB) PAE: PA4153 PPU: PP0552(adh) PST: PSPTO0363(polS) RSO: RS01456(polS) BPS: BPSL0826 MLO: mll4921 mlr3340 SME: SMc01500(smoS) ATU: Atu3164 ATC: AGR_L_3292 BJA: bll5566 BSU: BG10177(gutB) BHA: BH0187(gutB) BH0189 BCZ: BTZK0739(gutB) OIH: OB2750 OB2752 OB3238 OB3258 SAU: SA0239 SA0240 SAV: SAV0248 SAV0250 SAM: MW0224 MW0226 SAR: SAR0243 SAR0245 SAS: SAS0224 SAS0226 LMO: lmo0506 lmo2663 lmo2664 LMF: LMOf2365_0535 LMOf2365_2643 LMOf2365_2644 LIN: lin0506 lin2812 lin2813 LPL: lp_3545(gutB) PAC: PPA0918 RBA: RB3488 TDE: TDE0075 TEL: tll0970 tlr1436 GVI: glr0369 glr0940 ANA: alr2335 alr5117 SSO: SSO3237 STO: ST2341 DISEASE MIM: 182500 Sorbitol dehydrogenase MOTIF PS: PS00059 G-H-E-x(2)-G-x(5)-[GA]-x(2)-[IVSAC] PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] STRUCTURES PDB: 1K2W 1PL6 1PL7 1PL8 REFERENCE 1 Bailey, J.P., Renz, C. and McGuinness, E.T. Sorbitol dehydrogenase from horse liver: purification, characterization and comparative properties. Comp. Biochem. Physiol. 69B (1981) 909-914. 2 [PMID:6852349] Burnell, J.N. and Holmes, R.S. Purification and properties of sorbitol dehydrogenase from mouse liver. Int. J. Biochem. 15 (1983) 507-511. 3 [PMID:667078] Leissing, N. and McGuinness, E.T. Rapid affinity purification and properties of rat liver sorbitol dehydrogenase. Biochim. Biophys. Acta 524 (1978) 254-261. 4 Negm, F.B. and Loescher, W.H. Detection and characterization of sorbitol dehydrogenase from apple callus tissue. Plant Physiol. 64 (1979) 69-73. 5 [PMID:6870831] O'Brien, M.M., Schofield, P.J. and Edwards, M.R. Polyol-pathway enzymes of human brain. Partial purification and properties of sorbitol dehydrogenase. Biochem. J. 211 (1983) 81-90. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.14 ExPASy - ENZYME nomenclature database: 1.1.1.14 ERGO genome analysis and discovery system: 1.1.1.14 BRENDA, the Enzyme Database: 1.1.1.14 CAS: 9028-21-1 /// ENTRY EC 1.1.1.15 NAME D-iditol 2-dehydrogenase D-sorbitol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-iditol:NAD+ 2-oxidoreductase REACTION D-iditol + NAD+ = D-sorbose + NADH + H+ SUBSTRATE D-iditol NAD+ PRODUCT D-sorbose NADH H+ COMMENT Also converts xylitol into L-xylulose and L-glucitol into L-fructose. PATHWAY PATH: map00040 Pentose and glucuronate interconversions PATH: map00051 Fructose and mannose metabolism REFERENCE 1 Shaw, D.R.D. Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol dehydrogenase. Biochem. J. 64 (1956) 394-405. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.15 ExPASy - ENZYME nomenclature database: 1.1.1.15 ERGO genome analysis and discovery system: 1.1.1.15 BRENDA, the Enzyme Database: 1.1.1.15 CAS: 9028-22-2 /// ENTRY EC 1.1.1.16 NAME galactitol 2-dehydrogenase dulcitol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME galactitol:NAD+ 2-oxidoreductase REACTION galactitol + NAD+ = D-tagatose + NADH + H+ SUBSTRATE galactitol NAD+ PRODUCT D-tagatose NADH H+ COMMENT Also converts other alditols containing an L-threo-configuration adjacent to a primary alcohol group into the corresponding sugars. PATHWAY PATH: map00052 Galactose metabolism REFERENCE 1 Shaw, D.R.D. Polyol dehydrogenases 3. Galactitol dehydrogenase and D-iditol dehydrogenase. Biochem. J. 64 (1956) 394-405. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.16 ExPASy - ENZYME nomenclature database: 1.1.1.16 ERGO genome analysis and discovery system: 1.1.1.16 BRENDA, the Enzyme Database: 1.1.1.16 CAS: 9028-23-3 /// ENTRY EC 1.1.1.17 NAME mannitol-1-phosphate 5-dehydrogenase hexose reductase mannitol 1-phosphate dehydrogenase D-mannitol-1-phosphate dehydrogenase fructose 6-phosphate reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-mannitol-1-phosphate:NAD+ 5-oxidoreductase REACTION D-mannitol 1-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+ SUBSTRATE D-mannitol 1-phosphate NAD+ PRODUCT D-fructose 6-phosphate NADH H+ PATHWAY PATH: map00051 Fructose and mannose metabolism ORTHOLOG KO: K00009 mannitol-1-phosphate 5-dehydrogenase GENES ECO: b3600(mtlD) ECJ: JW3574(mtlD) ECE: Z5024(mtlD) ECS: ECs4476 ECC: c4417(mtlD) STY: STY4110(mtlD) STT: t3833(mtlD) STM: STM3686(mtlD) YPE: YPO4067(mtlD) YPK: y4086(mtlD) YPM: YP3978(mtlD2) YPS: YPTB3919(mtlD) SFL: SF3634(mtlD) SFX: S4134(mtlD) ECA: ECA0088(mtlD) BUC: BU571(mtlD) BAS: BUsg551(mtlD) BAB: bbp516(mtlD) PMU: PM1062(mtlD) MSU: MS0410(mtlD) VCH: VCA1046 VVU: VV10639 VVY: VV0504 VPA: VP0369 PPR: PBPRB0362 BSU: BG11216(mtlD) BHA: BH3851(mtlD) BLI: BL02815(mtlD) OIH: OB2600 SAU: SA1963(mtlD) SAV: SAV2159(mtlD) SAM: MW2085(mtlD) SAR: SAR2247(mtlD) SAS: SAS2060 LLA: L33416(mtlD) SPN: SP0397 SPR: spr0359(mtlD) SMU: SMU.1182(mtlD) LPL: lp_0233(mtlD) EFA: EF0413(mtlD) CAC: CAC0157(MtlD) TTE: TTE0342(mtlD) MPN: E09_orf364(mtlD) MPU: MYPU_7500(mtlD) MMY: MSC_0017(mtlD) MHY: mhp568(mtlD) LXX: Lxx00800(mtlD) MOTIF PS: PS00974 [LIVMY]-x-[FS]-x(2)-[STAGCV]-x-V-D-R-[IV]-x-[PS] REFERENCE 1 Marmur, J. and Hotchkiss, R.D. Mannitol metabolism, a transferable property of pneumococcus. J. Biol. Chem. 214 (1955) 383-396. 2 Wolfe, J.B. and Kaplan, N.O. Hexose phosphate and hexose reductase. A. D-Mannitol-1-phosphate dehydrogenase from E. coli. Methods Enzymol. 1 (1955) 346-348. 3 Wolfe, J.B. and Kaplan, N.O. D-Mannitol 1-phosphate dehydrogenase from Escherichia coli. J. Biol. Chem. 218 (1956) 849-869. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.17 ExPASy - ENZYME nomenclature database: 1.1.1.17 ERGO genome analysis and discovery system: 1.1.1.17 BRENDA, the Enzyme Database: 1.1.1.17 CAS: 9028-24-4 /// ENTRY EC 1.1.1.18 NAME inositol 2-dehydrogenase myo-inositol 2-dehydrogenase myo-inositol:NAD+ oxidoreductase inositol dehydrogenase myo-inositol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME myo-inositol:NAD+ 2-oxidoreductase REACTION myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ SUBSTRATE myo-inositol NAD+ PRODUCT 2,4,6/3,5-pentahydroxycyclohexanone NADH H+ PATHWAY PATH: map00031 Inositol metabolism PATH: map00562 Inositol phosphate metabolism ORTHOLOG KO: K00010 myo-inositol 2-dehydrogenase GENES CME: CMF086C CMR475C CAL: orf19.6899 STM: STM4425 YPS: YPTB1073 ECA: ECA1458(idhA) PLU: plu1804 PPR: PBPRB0470 PST: PSPTO3047 PSPTO3494(iolG) RSO: RS02754(iolG) MLO: mll1000 mll4991 SME: SMb20899(idhA) ATU: Atu4012(idhA) Atu4554(iolG) ATC: AGR_L_1682 AGR_L_628 BME: BMEI0661 BMEII0574 BMEII0938 BMS: BRA0711(idhA) CCR: CC1296 BSU: BG10669(iolG) BHA: BH2220 BH2316(iolG) BLI: BL00240(idh) LPL: lp_3605(iolG1) lp_3606(iolG2) lp_3608(iolG3) lp_3612(iolG4) CPE: CPE0093 CTC: CTC00511 CTC00513 CGL: NCgl0161(Cgl0164) NCgl2029(Cgl2110) NCgl2957(Cgl3062) SCO: SCO6984(SC8F11.10c) SCO7254(SC5H1.38) SMA: SAV1234(iolG) SAV7188 LXX: Lxx24320 PAC: PPA0136 PPA0463 PPA0466 PPA0469 RBA: RB3338(idh) MMA: MM1153 MTH: MTH875 REFERENCE 1 [PMID:5905122] Berman, T. and Magasanik, B. The pathway of myo-inositol degradation in Aerobacter aerogenes. Dehydrogenation and dehydration. J. Biol. Chem. 241 (1966) 800-806. 2 Larner, J., Jackson, W.T., Graves, D.J. and Stamner, J.R. Inositol dehydrogenase from Aerobacter aerogenes. Arch. Biochem. Biophys. 60 (1956) 352-363. 3 [PMID:4351258] Vidal-Lieria, M. and van Uden, N. Inositol dehydrogenase from the yeast Cryptococcus melibiosum. Biochim. Biophys. Acta 293 (1973) 295-303. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.18 ExPASy - ENZYME nomenclature database: 1.1.1.18 ERGO genome analysis and discovery system: 1.1.1.18 BRENDA, the Enzyme Database: 1.1.1.18 CAS: 9028-25-5 /// ENTRY EC 1.1.1.19 NAME L-glucuronate reductase aldehyde reductase L-hexonate:NADP dehydrogenase TPN-L-gulonate dehydrogenase aldehyde reductase II NADP-L-gulonate dehydrogenase D-glucuronate dehydrogenase D-glucuronate reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-gulonate:NADP+ 6-oxidoreductase REACTION L-gulonate + NADP+ = D-glucuronate + NADPH + H+ SUBSTRATE L-gulonate NADP+ PRODUCT D-glucuronate NADPH H+ COMMENT Also reduces D-galacturonate. May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)]. PATHWAY PATH: map00040 Pentose and glucuronate interconversions PATH: map00053 Ascorbate and aldarate metabolism REFERENCE 1 Sivak, A. and Hoffmann-Ostenhof, O. Enzymes of meso-inositol catabolism in the yeast Schwanniomyces occidentalis. Biochim. Biophys. Acta 53 (1961) 426-428. 2 von Wartburg, J.P. and Wermoth, B. Aldehyde reductase. In: Jakoby, W.B. (Ed.), Enzymatic Basis of Detoxication, vol. 1, Academic Press, New York, 1980, p. 249-260. 3 York, J.L., Grollman, A.P. and Bublitz, C. TPN-L-gulonate dehydrogenase. Biochim. Biophys. Acta 47 (1961) 298-306. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.19 ExPASy - ENZYME nomenclature database: 1.1.1.19 ERGO genome analysis and discovery system: 1.1.1.19 BRENDA, the Enzyme Database: 1.1.1.19 CAS: 9028-29-9 /// ENTRY EC 1.1.1.20 NAME glucuronolactone reductase GRase gulonolactone dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-gulono-1,4-lactone:NADP+ 1-oxidoreductase REACTION L-gulono-1,4-lactone + NADP+ = D-glucurono-3,6-lactone + NADPH + H+ SUBSTRATE L-gulono-1,4-lactone NADP+ PRODUCT D-glucurono-3,6-lactone NADPH H+ PATHWAY PATH: map00053 Ascorbate and aldarate metabolism GENES BPS: BPSL2727(xdhB) BPSL2728(xdhA) REFERENCE 1 Suzuki, K., Mano, Y. and Shimazono, N. Conversion of L-gulonolactone to L-ascorbic acid; properties of the microsomal enzyme in rat liver. J. Biochem. (Tokyo) 48 (1960) 313-315. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.20 ExPASy - ENZYME nomenclature database: 1.1.1.20 ERGO genome analysis and discovery system: 1.1.1.20 BRENDA, the Enzyme Database: 1.1.1.20 CAS: 9028-30-2 /// ENTRY EC 1.1.1.21 NAME aldehyde reductase aldose reductase polyol dehydrogenase (NADP+) ALR2 alditol:NADP oxidoreductase alditol:NADP+ 1-oxidoreductase NADPH-aldopentose reductase NADPH-aldose reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME alditol:NAD(P)+ 1-oxidoreductase REACTION alditol + NAD(P)+ = aldose + NAD(P)H + H+ SUBSTRATE alditol NAD+ NADP+ PRODUCT aldose NADH NADPH H+ COMMENT Has wide specificity. PATHWAY PATH: map00040 Pentose and glucuronate interconversions PATH: map00051 Fructose and mannose metabolism PATH: map00052 Galactose metabolism PATH: map00561 Glycerolipid metabolism PATH: map00620 Pyruvate metabolism ORTHOLOG KO: K00011 aldehyde reductase GENES HSA: 231(AKR1B1) MMU: 11677(Akr1b3) 11997(Akr1b7) 14187(Akr1b8) RNO: 24192(Aldr1) DME: CG6084-PA(CG6084) CG6084-PB(CG6084) SCE: YHR104W(GRE3) CAL: orf19.1340 orf19.2172(ARA1) orf19.7260 YPS: YPTB2971 SFL: SF0192(yafB) ACI: ACIAD3616(alrA) CVI: CV0701 RPA: RPA3161(yafB) RPA4297 BBU: BB0528 MOTIF PS: PS00062 [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY] PS: PS00063 [LIVM]-[PAIV]-[KR]-[ST]-x(4)-R-x(2)-[GSTAEQK]-[NSL]- x(2)-[LIVMFA] PS: PS00798 G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGC]-[AS]-x(5)-E-x(2)- [LIVM]-G STRUCTURES PDB: 1ABN 1ADS 1AH0 1AH3 1AH4 1AZ1 1AZ2 1DLA 1EF3 1EKO 1EL3 1IEI 1JEZ 1K8C 1MAR 1MI3 1PWL 1PWM 1R38 1T40 1T41 1US0 1X96 1X97 1X98 2ACQ 2ACR 2ACS 2ACU REFERENCE 1 [PMID:4216364] Attwood, M.A. and Doughty, C.C. Purification and properties of calf liver aldose reductase. Biochim. Biophys. Acta 370 (1974) 358-368. 2 [PMID:36151] Boghosian, R.A. and McGuinness, E.T. Affinity purification and properties of porcine brain aldose reductase. Biochim. Biophys. Acta 567 (1979) 278-286. 3 Hers, H.G. L'Aldose-reductase. Biochim. Biophys. Acta 37 (1960) 120-126. 4 [PMID:4381350] Scher, B.M. and Horecker, B.L. Pentose metabolism in Candida. 3. The triphosphopyridine nucleotide-specific polyol dehydrogenase of Candida utilis. Arch. Biochem. Biophys. 116 (1966) 117-128. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.21 ExPASy - ENZYME nomenclature database: 1.1.1.21 ERGO genome analysis and discovery system: 1.1.1.21 BRENDA, the Enzyme Database: 1.1.1.21 CAS: 9028-31-3 /// ENTRY EC 1.1.1.22 NAME UDP-glucose 6-dehydrogenase UDP-glucose dehydrogenase uridine diphosphoglucose dehydrogenase UDPG dehydrogenase UDPG:NAD oxidoreductase UDP-alpha-D-glucose:NAD oxidoreductase UDP-glucose:NAD+ oxidoreductase uridine diphosphate glucose dehydrogenase UDP-D-glucose dehydrogenase uridine diphosphate D-glucose dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME UDP-glucose:NAD+ 6-oxidoreductase REACTION UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH + 2 H+ SUBSTRATE UDP-glucose NAD+ H2O PRODUCT UDP-glucuronate NADH H+ COMMENT Also acts on UDP-2-deoxyglucose. PATHWAY PATH: map00040 Pentose and glucuronate interconversions PATH: map00500 Starch and sucrose metabolism PATH: map00520 Nucleotide sugars metabolism ORTHOLOG KO: K00012 UDPglucose 6-dehydrogenase GENES HSA: 7358(UGDH) MMU: 22235(Ugdh) RNO: 83472(Ugdh) DME: CG10072-PA(CG10072) CEL: F29F11.1 ATH: At1g26570(T1K7.6) At3g29360(MUO10.18) At5g15490(T20K14.100) At5g39320(K3K3.170) CME: CMB031C CMT471C CHO: Chro.80111 ECO: b2028(ugd) ECJ: JW2010(ugd) ECE: Z3190(ugd) ECS: ECs2829 ECC: c2555(ugd) STY: STY2289(ugd) STT: t0793(ugd) STM: STM2080(udg) YPE: YPO2174 YPK: y2147 YPM: YP1973(ugd) YPS: YPTB2100 ECA: ECA3147(ugd) PLU: plu2500 WBR: Wbr0397(ugd) PMU: PM0776 XFA: XF1606 XFT: PD1167(ugd) XCC: XCC1503(ugd) XAC: XAC1551(ugd) XAC3581(ugd) VCH: VCA0780 VVU: VV10774 VVY: VV0365 VPA: VP0236 PPR: PBPRA2675(ugd) PAE: PA2022 PA3559 PPU: PP2926 PST: PSPTO2891 PSPTO5585 ACI: ACIAD0072(ugd) ACIAD0087 ACIAD0100 SON: SO4687(ugd) CBU: CBU0680 CBU0846(ugd) MCA: MCA2487(ugd) CVI: CV3041(ugd) CV4129(udg) RSO: RS04502(ugd) BMA: BMA0423(ugd) BPS: BPSS1833(udg2) BPE: BP3728(rkpK) BPA: BPP4227(rkpK) BBR: BB4815(rkpK) NEU: NE1343(udg) HHE: HH0644(kfiD) WSU: WS0583 CJE: Cj1441c(kfiD) GSU: GSU1816(ugd) DVU: DVU1907(ugd) DPS: DP0014 DPPB70 RPR: RP779(udg) RTY: RT0766(udg) RCO: RC1212(udg) WOL: WD0620 MLO: mlr5265 SME: SMc02641(rkpK) ATU: Atu4149(ugdH) ATC: AGR_L_1413 BME: BMEII0727 BMS: BRA0545(ugd) BJA: bll8129(ugdH) blr2383(ugdH) RPA: RPA4018 CCR: CC2379 CC2382 BSU: BG12691(tuaD) BHA: BH3708 BAN: BA5434(ugd) BAR: GBAA5434(ugd) GBAA_pXO1_0130(ugd) BAA: BA_0287 BXA0130(ugd) BAT: BAS5049 BCE: BC5202 BCA: BCE5308(ugd) BCE5385(ugd) BCZ: BTZK4894(ugd) BTK: BT9727_4879(ugd) BLI: BL03352(tuaD) OIH: OB2884 OB2929 SPY: SPy0542 SPy2201(hasB) SPM: spyM18_0608 spyM18_2237(hasB) SPG: SpyM3_0385 SpyM3_1852(hasB) SPS: SPs1468 SPs1848 SPA: M6_Spy0483 M6_Spy1870 SPR: spr0139(ugd) spr0318(cps2K) CPE: CPE0494 MMO: MMOB6010(udgA) MTU: Rv0322(udgA) MTC: MT0337 MBO: Mb0330(udgA) MPA: MAP3825(udgA) CGL: NCgl0351(Cgl0360) NCgl2750(Cgl2847) CEF: CE2662 CDI: DIP2141 SCO: SCO3052(SCBAC19G2.07) SMA: SAV5025(udgA) LXX: Lxx03520(udgA) PAC: PPA0593 STH: STH785 RBA: RB1784(ugdH) PCU: pc1695(rkpK) LIL: LA1459 LIC: LIC12294(ugd) BTH: BT0379 BT0599 BT0829 BT1341 PGI: PG1143 SYN: slr1299 SYW: SYNW0199(Ugd) SYC: syc0570_d(ugd) TEL: tll0664 GVI: gll0969 gll1798 gll2180 gll3719 glr1062 ANA: alr0658 PMA: Pro1312(ugd) PMM: PMM1261(ugd) PMT: PMT1904(ugd) CTE: CT1177 AAE: aq_024(nsd) MJA: MJ1054 MAC: MA4457 MMA: MM1132 AFU: AF0302(ugd-1) AF0596(ugd-2) HAL: VNG0046G(ugd) HMA: rrnAC3239(ugd2) PAB: PAB0770(ugd) PFU: PF0771 PF1355 SSO: SSO0810(ugd) DISEASE MIM: 603370 UDP-glucose dehydrogenase STRUCTURES PDB: 1DLI 1DLJ REFERENCE 1 [PMID:1091296] Druzhinina, T.N., Kusov, Y.Y., Shibaev, V.N., Kochetkov, N.K., Biely, P., Kucar, S. and Bauer, S. Uridine diphosphate 2-deoxyglucose. Chemical synthesis, enzymic oxidation and epimerization. Biochim. Biophys. Acta 381 (1975) 301-307. 2 Maxwell, E.S., Kalckar, H.M. and Strominger, J.L. Some properties of uridine diphosphoglucose dehydrogenase. Arch. Biochem. Biophys. 65 (1956) 2-10. 3 Strominger, J.L. and Mapson, L.W. Uridine diphosphoglucose dehydrogenase of pea seedlings. Biochem. J. 66 (1957) 567-572. 4 Strominger, J.L., Maxwell, E.S., Axelrod, J. and Kalckar, H.M. Enzymatic formation of uridine diphosphogluconic acid. J. Biol. Chem. 224 (1957) 79-90. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.22 ExPASy - ENZYME nomenclature database: 1.1.1.22 ERGO genome analysis and discovery system: 1.1.1.22 BRENDA, the Enzyme Database: 1.1.1.22 CAS: 9028-26-6 /// ENTRY EC 1.1.1.23 NAME histidinol dehydrogenase L-histidinol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-histidinol:NAD+ oxidoreductase REACTION L-histidinol + 2 NAD+ = L-histidine + 2 NADH + 2 H+ SUBSTRATE L-histidinol NAD+ PRODUCT L-histidine NADH H+ COMMENT Also oxidizes L-histidinal. The Neurospora enzyme also catalyses the reactions of EC 3.5.4.19 (phosphoribosyl-AMP cyclohydrolase) and EC 3.6.1.31 (phosphoribosyl-ATP diphosphatase). PATHWAY PATH: map00340 Histidine metabolism ORTHOLOG KO: K00013 histidinol dehydrogenase GENES CME: CMQ082C SCE: YCL030C(HIS4) AGO: AFR703W(AFR703Wp) CAL: orf19.5639(HIS4) SPO: SPBC1711.13(his2) ECO: b2020(hisD) ECJ: JW2002(hisD) ECE: Z3182(hisD) ECS: ECs2821 ECC: c2547(hisD) STY: STY2281(hisD) STT: t0801(hisD) STM: STM2072(hisD) YPE: YPO1548(hisD) YPK: y2621(hisD) YPM: YP1437(hisD) YPS: YPTB1561(hisD) SFL: SF2082(hisD) SFX: S2203(hisD) ECA: ECA2583(hisD) PLU: plu1569(hisD) BUC: BU100(hisD) BAS: BUsg093(hisD) BAB: bbp094(hisD) BFL: Bfl463(hisD) HIN: HI0469(hisD) PMU: PM1198(hisD) XFA: XF2219 XFT: PD1267(hisD) XCC: XCC1809(hisD) XAC: XAC1829(hisD) VCH: VC1133 VVU: VV12919 VVY: VV1351 VPA: VP1138 PPR: PBPRA1091 PAE: PA4448(hisD) PPU: PP0966(hisD) PST: PSPTO4438(hisD) ACI: ACIAD0663(hisD) SON: SO2073(hisD) LPN: lpg1199 MCA: MCA1963(hisD) NME: NMB1581 NMA: NMA1770(hisD) CVI: CV0611(hisD) RSO: RS00134(hisD) BMA: BMA2714(hisD) BPS: BPSL3139(hisD) BPE: BP3768(hisD) BPA: BPP4267(hisD) BBR: BB4854(hisD) NEU: NE0872(hisD) HHE: HH1721(hisD) WSU: WS1587(hisD) CJE: Cj1598(hisD) GSU: GSU3100(hisD) DVU: DVU0796(hisD) DPS: DP1282 MLO: mll6456 mlr6649 mlr7107 SME: SMa0398(hisD2) SMc02307(hisD1) ATU: Atu0537(hisD) ATC: AGR_C_948 BME: BMEI1668 BMS: BR0252(hisD) BJA: blr1256(hisD) RPA: RPA4531(hisD) CCR: CC2346 BSU: BG12599(hisD) BHA: BH3582(hisD) BAN: BA1426(hisD) BAR: GBAA1426(hisD) BAA: BA_1946 BAT: BAS1317 BCE: BC1406 BCA: BCE1526(hisD) BCZ: BTZK1291(hisD) BTK: BT9727_1290(hisD) BLI: BL03408(hisD) OIH: OB0551 SAU: SA2470 SAV: SAV2678 SAM: MW2597 SAR: SAR2760(hisD) SAS: SAS2563 SEP: SE0272 LMO: lmo0567(hisD) LMF: LMOf2365_0596(hisD) LIN: lin0576(hisD) LLA: L0067(hisD) SMU: SMU.1270(hisD) LPL: lp_2559(hisD) CAC: CAC0937(hisD) TTE: TTE2138(hisD) MTU: Rv1599(hisD) MTC: MT1635 MBO: Mb1625(hisD) MLE: ML1257(hisD) MPA: MAP1293(hisD) CGL: NCgl2021(Cgl2102) CEF: CE2003(hisD) CDI: DIP1566(hisD) SCO: SCO2054(SC4G6.23c) SMA: SAV6153(hisD) LXX: Lxx15120(hisD) PAC: PPA1152 BLO: BL1295(hisD) STH: STH2837(hisD) RBA: RB1584(hisD) LIL: LA2515(hisD) LIC: LIC11453(hisD) BTH: BT0201 SYN: slr0682(hisD) slr1848(hisD) SYW: SYNW0610(hisD) SYC: syc2504_c(hisD) TEL: tll2252(hisD) GVI: gll1324(hisD) ANA: all1591(hisD) alr3056(hisD) PMA: Pro1643(hisD) PMM: PMM1488(hisD) PMT: PMT1510(hisD) CTE: CT0546(hisD) DRA: DR2140 TTH: TTC0370 AAE: aq_782(hisD) TMA: TM1041 MJA: MJ1456(hisD) MMP: MMP0968(hisD) MAC: MA3201(hisD) MMA: MM0424 MTH: MTH225 MKA: MK0711(hisD) AFU: AF0212(hisD) HAL: VNG1444G(hisD) HMA: rrnAC0272(hisD) PTO: PTO1336 PFU: PF1659 SSO: SSO0599(hisD) STO: ST1464 PAI: PAE0988(hisD) MOTIF PS: PS00611 I-D-x(2)-A-G-P-[ST]-E-[LIVS]-[LIVMA](3)-[AC]-x(3)-A- x(4)-[LIVM]-[AV]-[SACL]-[DE]-[LIVMFC]-[LIVM]-[SA]-x(2)- E-H STRUCTURES PDB: 1K75 1KAE 1KAH 1KAR REFERENCE 1 Adams, E. Enzymatic synthesis of histidine from histidinol. J. Biol. Chem. 209 (1954) 829-846. 2 Adams, E. L-Histidinal, a biosynthetic precursor of histidine. J. Biol. Chem. 217 (1955) 325-344. 3 [PMID:4872177] Loper, J.C. Histidinol dehydrogenase from Salmonella typhimurium. Crystallization and composition studies. J. Biol. Chem. 243 (1968) 3264-3272. 4 [PMID:4872176] Yourno, J. and Ino, I. Purification and crystallization of histidinol dehydrogenase from Salmonella typhimurium LT-2. J. Biol. Chem. 243 (1968) 3273-3276. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.23 ExPASy - ENZYME nomenclature database: 1.1.1.23 ERGO genome analysis and discovery system: 1.1.1.23 BRENDA, the Enzyme Database: 1.1.1.23 CAS: 9028-27-7 /// ENTRY EC 1.1.1.24 NAME quinate dehydrogenase quinic dehydrogenase quinate:NAD oxidoreductase quinate 5-dehydrogenase quinate:NAD+ 5-oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-quinate:NAD+ 3-oxidoreductase REACTION quinate + NAD+ = 3-dehydroquinate + NADH + H+ SUBSTRATE quinate NAD+ PRODUCT 3-dehydroquinate NADH H+ COMMENT The enzyme is specific for quinate as substrate; phenylpyruvate, phenylalanine, cinnamate and shikimate will not act as substrates. NAD+ cannot be replaced by NADP+. PATHWAY PATH: map00400 Phenylalanine, tyrosine and tryptophan biosynthesis REFERENCE 1 Gamborg, O.L. Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures. Biochim. Biophys. Acta 128 (1966) 483-491. 2 Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268-280. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.24 ExPASy - ENZYME nomenclature database: 1.1.1.24 ERGO genome analysis and discovery system: 1.1.1.24 BRENDA, the Enzyme Database: 1.1.1.24 CAS: 9028-28-8 /// ENTRY EC 1.1.1.25 NAME shikimate dehydrogenase dehydroshikimic reductase shikimate oxidoreductase shikimate:NADP+ oxidoreductase 5-dehydroshikimate reductase shikimate 5-dehydrogenase 5-dehydroshikimic reductase DHS reductase shikimate:NADP+ 5-oxidoreductase AroE CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME shikimate:NADP+ 3-oxidoreductase REACTION shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ SUBSTRATE shikimate NADP+ PRODUCT 3-dehydroshikimate NADPH H+ COMMENT NAD+ cannot replace NADP+ [3]. In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase [4]. PATHWAY PATH: map00400 Phenylalanine, tyrosine and tryptophan biosynthesis ORTHOLOG KO: K00014 shikimate 5-dehydrogenase GENES CME: CMK269C SCE: YDR127W(ARO1) AGO: AGR066W(AGR066Wp) CAL: orf19.4704(ARO1) SPO: SPAC1834.02(aro1) ECO: b1692(ydiB) b3281(aroE) ECJ: JW3242(aroE) ECE: Z4652(aroE) ECS: ECs4147 ECC: c4042(aroE) STY: STY3924 STY4396(aroE) STT: t3664 t4103(aroE) STM: STM3401(aroE) STM3859 YPE: YPO0246(aroE) YPO1610 YPK: y1769 y4028(aroE) YPM: YP0245(aroE1) YP2244(aroE2) YPS: YPTB2454 YPTB3660(aroE) SFL: SF3313(aroE) SFX: S3537(aroE) ECA: ECA3995(aroE) PLU: plu4691(aroE) BUC: BU493(aroE) BAS: BUsg474(aroE) BAB: bbp437(aroE) BFL: Bfl221(aroE) HIN: HI0607 HI0655(aroE) HDU: HD0415(aroE) PMU: PM1271(aroE) PM1429 MSU: MS0133(aroE) XFA: XF0624 XFT: PD1532(aroE) XCC: XCC3953(aroE) XAC: XAC4034(aroE) VCH: VC0056 VVU: VV11057 VVY: VV3215 VPA: VP3033 PPR: PBPRA3571 PAE: PA0025(aroE) PA0244 PPU: PP0074(aroE-1) PP2406 PP2608 PP3002(aroE-2) PP3768 PST: PSPTO0169(aroE) PSPTO2348 PSPTO2685 ACI: ACIAD0418(aroE) SON: SO0040(aroE) CBU: CBU0010(aroE) LPN: lpg2808(aroE) MCA: MCA2794(aroE) NME: NMB0358 NMA: NMA2129(aroE) CVI: CV3587(aroE) RSO: RS00070(aroE1) RS02060(aroE2) BMA: BMA2494(aroE) BPS: BPSL2976(aroE) BPSS0341(aroE) BPE: BP3004(aroE) BPA: BPP3924(aroE) BBR: BB4397(aroE) NEU: NE1627(aroE1) HPY: HP1249(aroE) HPJ: jhp1170 HHE: HH1247(aroE) WSU: WS2168(aroE) CJE: Cj0405(aroE) GSU: GSU1490(aroE) DVU: DVU0115(aroE) BBA: Bd1508(aroE) DPS: DP3012 MLO: mlr4492 SME: SMb20037(aroE2) SMc02791(aroE1) ATU: Atu0003(aroE) Atu4295(aroE) Atu4532(aroE) ATC: AGR_C_3 AGR_L_1139 AGR_L_673 BME: BMEI2058 BMEII0871 BMS: BR2069(aroE) BJA: bll1059(aroE) bll3660 bll6391(aroE) bll6392 bll7412(aroE) blr2257(aroE) blr3543 blr3858 RPA: RPA4325(aroE) BHE: BH00030(aroE) BQU: BQ00030(aroE) CCR: CC0003 BSU: BG11522(aroD) BHA: BH1324(aroD) BAN: BA4561(aroE) BAR: GBAA4561(aroE) BAA: BA_5005 BAT: BAS4232 BCE: BC4331 BCA: BCE4415(aroE) BCZ: BTZK4080(aroE) BTK: BT9727_4070(aroE) BLI: BL02079(aroD) OIH: OB1987 SAU: SA1424(aroE) SAV: SAV1596(aroE) SAM: MW1547(aroE) SAR: SAR1673(aroE) SAS: SAS1533 SEP: SE1282 LMO: lmo0490 lmo1490 lmo2236 LMF: LMOf2365_0520(aroE-1) LMOf2365_1509(aroE-2) LMOf2365_2269 LIN: lin0493 lin1525 lin2338 LLA: L0061(aroE) SPY: SPy0534(aroE.2) SPy1584(aroE) SPM: spyM18_0600(aroD) spyM18_1592(aroE) SPG: SpyM3_0378(aroE.2) SpyM3_1284(aroE.1) SPS: SPs0577 SPs1475 SPA: M6_Spy0475 M6_Spy1321 SPN: SP1376 SPR: spr1234(aroE) SAG: SAG1680(aroE) SAN: gbs1724 SMU: SMU.778(aroE) LPL: lp_1084(aroD1) lp_3494(aroD2) lp_3498(aroD3) lp_3499(aroD4) EFA: EF1561(aroE) CAC: CAC0897(aro) CPE: CPE0700(aroE) CTC: CTC01117 TTE: TTE1261(aroE) MTU: Rv2552c(aroE) MTC: MT2629 MBO: Mb2582c(aroE) MLE: ML0515(aroE) MPA: MAP1080(aroE) CGL: NCgl0409(Cgl0424) NCgl1087(Cgl1132) NCgl1567(Cgl1629) CEF: CE0443(aroE) CE1194 CE1745 CDI: DIP1006 DIP1347 SCO: SCO1498(SC9C5.22c,) SMA: SAV1777(aroE2) SAV6853(aroE1) TWH: TW373(aroE) TWS: TW396(aroE) LXX: Lxx00310(aroE) Lxx10940(aroE) PAC: PPA1181 BLO: BL0704(aroE) STH: STH1952 FNU: FN0044 FN0045 RBA: RB6488 CTR: CT370(aroE) CMU: TC0649 CPN: CPn1035 CPA: CP0817 CPJ: CPj1035(aroE) CPT: CpB1075 CCA: CCA00727(aroE) LIL: LA0638(aroE) LIC: LIC12949(aroE) BTH: BT4215 PGI: PG0978(aroE) SYN: slr1559(aroE) SYW: SYNW2509(aroE) SYC: syc1637_d(aroE) TEL: tll0590(aroE) GVI: gll3278(aroE) ANA: alr2057(aroK) PMA: Pro1872(aroE) PMM: PMM1705(aroE) PMT: PMT2257(aroE) CTE: CT1809(aroE) DRA: DR0077 DR1173 TTH: TTC0688 AAE: aq_901(aroE) TMA: TM0346 MJA: MJ1084(aroE) MMP: MMP0936(aroE) MAC: MA4594(aroE) MMA: MM1274 MTH: MTH242 MKA: MK0117(aroE) AFU: AF2327(aroE) HAL: VNG0382G(aroE) HMA: rrnAC0707(aroE) TAC: Ta0284 TVO: TVG1385100 PTO: PTO0600 PAB: PAB0300(aroE) PFU: PF1693 APE: APE0574 SSO: SSO0306(aroE) STO: ST2273 PAI: PAE1913(aroE) MOTIF PS: PS00104 [LIVF]-x(2)-[GANQK]-[NLG]-[SA]-[GA]-[TAI]-[STAGV]-x-R- x-[LIVMFYAT]-x-[GSTAP] PS: PS00885 [KR]-x-[KH]-E-[CST]-[DNE]-R-[LIVM]-x-[GSTAV]-[LIVMCT]- x(3)-[LIVMF]-x(2)-[LIVMFCGAN]-G PS: PS01028 D-[LIVM]-[DE]-[LIVMN]-x(18,20)-[LIVM](2)-x-[SC]-[NHY]- H-[DN] PS: PS01128 [KR]-x(2)-E-x(3)-[LIVMF]-x(8,12)-[LIVMF](2)-[SA]-x- G(3)-x-[LIVMFG] STRUCTURES PDB: 1NPD 1NVT 1NYT 1O9B 1P74 1P77 1VI2 REFERENCE 1 [PMID:13686342] Balinsky, D. and Davies, D.D. Aromatic biosynthesis in higher plants. 1. Preparation and properties of dehydroshikimic reductase. Biochem. J. 80 (1961) 292-296. 2 [PMID:13208693] Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268-280. 3 [PMID:14367339] Yaniv, H. and Gilvarg, C. Aromatic biosynthesis. XIV. 5-Dehydroshikimic reductase. J. Biol. Chem. 213 (1955) 787-795. 4 [PMID:3883995] Chaudhuri, S. and Coggins, J.R. The purification of shikimate dehydrogenase from Escherichia coli. Biochem. J. 226 (1985) 217-223. 5 [PMID:3277621] Anton, I.A. and Coggins, J.R. Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. Biochem. J. 249 (1988) 319-326. 6 [PMID:12837789] Ye, S., Von Delft, F., Brooun, A., Knuth, M.W., Swanson, R.V. and McRee, D.E. The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. J. Bacteriol. 185 (2003) 4144-4151. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.25 ExPASy - ENZYME nomenclature database: 1.1.1.25 ERGO genome analysis and discovery system: 1.1.1.25 BRENDA, the Enzyme Database: 1.1.1.25 CAS: 9026-87-3 /// ENTRY EC 1.1.1.26 NAME glyoxylate reductase NADH-glyoxylate reductase glyoxylic acid reductase NADH-dependent glyoxylate reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME glycolate:NAD+ oxidoreductase REACTION glycolate + NAD+ = glyoxylate + NADH + H+ SUBSTRATE glycolate NAD+ PRODUCT glyoxylate NADH H+ COMMENT Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate. PATHWAY PATH: map00630 Glyoxylate and dicarboxylate metabolism ORTHOLOG KO: K00015 glyoxylate reductase GENES HSA: 9380(GRHPR) CME: CMQ289C PHO: PH0597 PAB: PAB2374(gdh-like) PFU: PF0319 APE: APE1831 REFERENCE 1 Zelitch, I. Oxidation and reduction of glycolic and glyoxylic acids in plants. II. Glyoxylic acid reductase. J. Biol. Chem. 201 (1953) 719-726. 2 Zelitch, I. The isolation and action of crystalline glyoxylic acid reductase from tobacco leaves. J. Biol. Chem. 216 (1955) 553-575. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.26 ExPASy - ENZYME nomenclature database: 1.1.1.26 ERGO genome analysis and discovery system: 1.1.1.26 BRENDA, the Enzyme Database: 1.1.1.26 CAS: 9028-32-4 /// ENTRY EC 1.1.1.27 NAME L-lactate dehydrogenase lactic acid dehydrogenase L(+)-nLDH L-(+)-lactate dehydrogenase L-lactic dehydrogenase L-lactic acid dehydrogenase lactate dehydrogenase lactate dehydrogenase NAD-dependent lactic dehydrogenase NAD-lactate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S)-lactate:NAD+ oxidoreductase REACTION (S)-lactate + NAD+ = pyruvate + NADH + H+ SUBSTRATE (S)-lactate NAD+ PRODUCT pyruvate NADH H+ COMMENT Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme. PATHWAY PATH: map00010 Glycolysis / Gluconeogenesis PATH: map00272 Cysteine metabolism PATH: map00620 Pyruvate metabolism PATH: map00640 Propanoate metabolism ORTHOLOG KO: K00016 L-lactate dehydrogenase GENES HSA: 3939(LDHA) 3945(LDHB) 3948(LDHC) 92483(LDHAL6B) MMU: 16828(Ldh1) 16832(Ldh2) 16833(Ldh3) RNO: 24533(Ldha) 24534(Ldhb) 29634(Ldhc) DRE: 30496(ldha) DME: CG10160-PA(CG10160) CG13334-PA(CG13334) CEL: F13D12.2(ldh-1) ATH: At4g17260(FCAALL.172) CME: CMA145C CMC188C CMI306C CMJ002C CMK006C SPO: SPAC186.08c PFA: PF13_0141 PF13_0144 VVU: VV21457 VVY: VVA0276 VPA: VPA0147 BPE: BP0379(ldh) BPA: BPP4051(ldh) BBR: BB4524(ldh) BB4684 HHE: HH1571(mdh) CJE: Cj1167(ldh) DVU: DVU0600(ldh) BSU: BG19003(ldh) BHA: BH3937(lctE) BAN: BA1923(ldh-1) BA5125(ldh-2) BA5240(ldh-3) BAR: GBAA1923(ldh-1) GBAA5125(ldh-2) GBAA5240(ldh-3) BAA: BA_0106 BA_2427 BAT: BAS1784 BAS4762 BAS4869 BCE: BC1924 BC4870 BC4996 BCA: BCE2007(ldh) BCE5032(ldh) BCE5135(ldh) BCZ: BTZK1741(ldh) BTZK4624(ldhP) BTZK4723(ldhB) BTK: BT9727_1763(ldh) BT9727_4600(ldhP) BT9727_4708(ldhB) BLI: BL01703(ldh) OIH: OB3279 SAU: SA0232(lctE) SA2395 SAV: SAV0241(lctE) SAV2602 SAM: MW0217(lctE) MW2521 SAR: SAR0234(ldh1) SAR2680(ldh2) SAS: SAS0217 SAS2487 SEP: SE2145 LMO: lmo0210(ldh) lmo1534 lmo1667 LMF: LMOf2365_0221(ldh-1) LMOf2365_1553(ldh-2) LMOf2365_1691 LIN: lin0242(ldh) lin1569 lin1775 LLA: L0017(ldh) L0018(ldhB) L142159(ldhX) SPY: SPy1151(ldh) SPM: spyM18_1111(ldh) SPG: SpyM3_0809(ldh) SPS: SPs1008 SPA: M6_Spy0869 SPN: SP1220 SPR: spr1100(ldh) SAG: SAG0128 SAG0959(ldh) SAN: gbs0126 gbs0947 SMU: SMU.1115(ldh) LPL: lp_0537(ldhL1) lp_1101(ldhL2) lp_2150 lp_2349(hicD3) LJO: LJ0274 LJ1403 EFA: EF0255(ldh-1) EF0641(ldh-2) CAC: CAC0267 CAC3552 CPE: CPE0103(ldh) CTC: CTC01998 MGE: MG460(ldh) MPN: K05_orf312(ldh) MPU: MYPU_7590(ldh) MPE: MYPE9640 MGA: MGA_0746(mdh) MMY: MSC_0532(ldh) MMO: MMOB0410(ldh) MHY: mhp245(ictD) mhp469(ldh) MFL: Mfl596 CGL: NCgl2810(Cgl2911) CEF: CE2753 CDI: DIP0427 DIP2255(ldh) SMA: SAV339(ldhA) PAC: PPA0012 PPA0887 PPA1952 BLO: BL0710(ldh1) BL1308(ldh2) FNU: FN1169 RBA: RB2566(ldh) RB856(ldh) BBU: BB0087(ldh) TDE: TDE0351(ldh) LIL: LA1488 LIC: LIC12268 GVI: gll3324 DRA: DR2364 TTH: TTC0748 TMA: TM1867 DISEASE MIM: 150000 Lactate dehydrogenase A MIM: 150100 Lactate dehydrogenase B MIM: 150150 Lactate dehydrogenase C MOTIF PS: PS00064 [LIVMA]-G-[EQ]-H-G-[DN]-[ST] STRUCTURES PDB: 1A5Z 1CEQ 1CET 1EZ4 1HYE 1HYG 1HYH 1I0Z 1I10 1LDB 1LDG 1LDM 1LDN 1LLC 1LLD 1LTH 1OC4 1PZE 1PZF 1PZG 1PZH 1T24 1T25 1T26 1T2C 1T2D 1T2E 1T2F 1Y6J 2LDB 2LDX 3LDH 5LDH 6LDH 8LDH 9LDB 9LDT REFERENCE 1 Dennis, D. and Kaplan, N.O. D and L-lactic acid dehydrogenase in Lactobacillus plantarum. J. Biol. Chem. 235 (1960) 810-818. 2 [PMID:4146647] Everse, J. and Kaplan, N.O. Lactate dehydrogenases: structure and function. Adv. Enzymol. Relat. Subj. Biochem. 37 (1973) 61-133. 3 Holbrook, J.J., Liljas, A., Steindel, S.J. and Rossmann, M.G. Lactate dehydrogenase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic Press, New York, 1975, p. 191-292. 4 [PMID:114469] Schar, H.-P. and Zuber, H. Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. I) Isolation and characterization of lactate dehydrogenases from thermophilic and mesophilic bacilli. Hoppe-Seyler's Z. Physiol. Chem. 360 (1979) 795-807. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.27 ExPASy - ENZYME nomenclature database: 1.1.1.27 ERGO genome analysis and discovery system: 1.1.1.27 BRENDA, the Enzyme Database: 1.1.1.27 CAS: 9001-60-9 /// ENTRY EC 1.1.1.28 NAME D-lactate dehydrogenase lactic acid dehydrogenase D-specific lactic dehydrogenase D-(-)-lactate dehydrogenase (NAD) D-lactic acid dehydrogenase D-lactic dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-lactate:NAD+ oxidoreductase REACTION (R)-lactate + NAD+ = pyruvate + NADH + H+ SUBSTRATE (R)-lactate NAD+ PRODUCT pyruvate NADH H+ PATHWAY PATH: map00620 Pyruvate metabolism ORTHOLOG KO: K00017 D-lactate dehydrogenase KO: K03777 D-lactate dehydrogenase KO: K03778 D-lactate dehydrogenase GENES HSA: 197257(LDHD) ECO: b1380(ldhA) b2133(dld) ECJ: JW1375(ldhA) JW2121(dld) ECE: Z2329(ldhA) Z3382(dld) ECS: ECs2002 ECs3020 ECC: c1827(ldhA) c2664(dld) STY: STY1422(ldhA) STY2397(dld) STT: t0688(dld) t1550(ldhA) STM: STM1647(ldhA) STM2167(dld) YPE: YPO1177(dld) YPO2329(ldhA) YPK: y2004(ldhA) y3012(dld) YPM: YP0960(dld) YP2115(ldhA1) YPS: YPTB1218(dld) YPTB2248(ldhA) SFL: SF1814(ldhA) SF2218(dld) SFX: S1459(ldhA) S2347(dld) ECA: ECA2000(ldhA) ECA3181(dld) PLU: plu2145(ldhA) plu2848(dld) HIN: HI0085 HI1649(dld) XFA: XF0347 XFT: PD1708 XCC: XCC0708(dld) XAC: XAC0762(dld) VCH: VCA0192 VVU: VV12200 VVY: VV2174 VPA: VPA0144 VPA1005 PPR: PBPRA1210 PBPRA2224 PAE: PA0927(ldhA) PPU: PP1649(ldhA) ACI: ACIAD0109(dld) SON: SO0968(ldhA) NME: NMB0997 NMB1685 NMA: NMA1205(dld) NMA1944(ldhA) RSO: RS00472(ldhA) BMA: BMA2050(ldhA) BPS: BPSL2734(ldhA) BPE: BP0651(dld) BBR: BB4787(dld) NEU: NE0899(ldhA) NE1009 ATU: Atu3870(ldhA) ATC: AGR_L_1952 BME: BMEII0185 SAU: SA2312(ddh) SA2346 SAV: SAV2524(ddh) SAV2559 SAM: MW2444(ddh) MW2480 SAR: SAR2605(ddh) SAR2640 SAS: SAS2410 SAS2445 SEP: SE2074 SE2121 SPY: SPy1170(ddh) SAG: SAG0695(ldhA) SAN: gbs0668 LPL: lp_2057(ldhD) LJO: LJ0045 EFA: EF2295 CAC: CAC1543 CAC2691 CPE: CPE0530(ldhD) CTC: CTC01840 MPE: MYPE2650 MMY: MSC_0034(ldh) CGL: NCgl0865(Cgl0901) SCO: SCO2118(SCE10.12c) SCO3594(SC66T3.05) FNU: FN0511 RBA: RB8859(ldhA) TPA: TP0037 BTH: BT1575 SYN: slr1556(ddh) SYC: syc0206_d TEL: tlr0711 ANA: alr0058 PMA: Pro1755(dld) AAE: aq_1769(dld1) aq_727(ldhA) PAI: PAE2035 DISEASE MIM: 607490 D-lactate dehydrogenase MOTIF PS: PS00065 [LIVMA]-[AG]-[IVT]-[LIVMFY]-[AG]-x-G-[NHKRQGSAC]-[LIV]- G-x(13,14)-[LIVMFT]-x(2)-[FYWCTH]-[DNSTK] PS: PS00670 [LIVMFYWA]-[LIVFYWC]-x(2)-[SAC]-[DNQHR]-[IVFA]-[LIVF]- x-[LIVF]-[HNI]-x-P-x(4)-[STN]-x(2)-[LIVMF]-x-[GSDN] PS: PS00671 [LMFATC]-[KPQ]-x-[GSTDN]-x-[LIVMFYWR]-[LIVMFYW](2)-N-x- [STAGC]-R-[GP]-x-[LIVH]-[LIVMC]-[DNV] STRUCTURES PDB: 1F0X 1J49 1J4A 2DLD REFERENCE 1 Dennis, D. and Kaplan, N.O. D and L-lactic acid dehydrogenase in Lactobacillus plantarum. J. Biol. Chem. 235 (1960) 810-818. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.28 ExPASy - ENZYME nomenclature database: 1.1.1.28 ERGO genome analysis and discovery system: 1.1.1.28 BRENDA, the Enzyme Database: 1.1.1.28 CAS: 9028-36-8 /// ENTRY EC 1.1.1.29 NAME glycerate dehydrogenase D-glycerate dehydrogenase hydroxypyruvate reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-glycerate:NAD+ oxidoreductase REACTION (R)-glycerate + NAD+ = hydroxypyruvate + NADH + H+ SUBSTRATE (R)-glycerate NAD+ PRODUCT hydroxypyruvate NADH H+ PATHWAY PATH: map00260 Glycine, serine and threonine metabolism PATH: map00630 Glyoxylate and dicarboxylate metabolism ORTHOLOG KO: K00018 glycerate dehydrogenase GENES ECA: ECA2721(hprA) PAE: PA4626(hprA) PPU: PP0762(hprA) ACI: ACIAD1301 ACIAD3278(hprA) SON: SO3631(hprA) NME: NMB0029 NMA: NMA0274 CVI: CV3789 NEU: NE0101(hprA) GSU: GSU1672(hprA) DVU: DVU1412 BJA: bll2918 CAC: CAC2945 RBA: RB6394 TDE: TDE1616(hprA) BTH: BT1207 PGI: PG1190(hprA) TTH: TTC0124 MMP: MMP0870 MOTIF PS: PS00065 [LIVMA]-[AG]-[IVT]-[LIVMFY]-[AG]-x-G-[NHKRQGSAC]-[LIV]- G-x(13,14)-[LIVMFT]-x(2)-[FYWCTH]-[DNSTK] PS: PS00670 [LIVMFYWA]-[LIVFYWC]-x(2)-[SAC]-[DNQHR]-[IVFA]-[LIVF]- x-[LIVF]-[HNI]-x-P-x(4)-[STN]-x(2)-[LIVMF]-x-[GSDN] PS: PS00671 [LMFATC]-[KPQ]-x-[GSTDN]-x-[LIVMFYWR]-[LIVMFYW](2)-N-x- [STAGC]-R-[GP]-x-[LIVH]-[LIVMC]-[DNV] STRUCTURES PDB: 1GDH REFERENCE 1 [PMID:13522707] Holzer, H. and Holldorf, A. Isolation of a D-glycerate dehydrogenase, its properties, and its use for the optical determination of hydroxypyruvate in the presence of pyruvate. Biochem. Z. 329 (1957) 292-312 (in German). 2 [PMID:13163046] Stafford, H.A., Magaldi, A. and Vennesland, B. The enzymatic reduction of hydroxypyruvic acid to D-glyceric acid in higher plants. J. Biol. Chem. 207 (1954) 621-629. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.29 ExPASy - ENZYME nomenclature database: 1.1.1.29 ERGO genome analysis and discovery system: 1.1.1.29 BRENDA, the Enzyme Database: 1.1.1.29 CAS: 9028-37-9 /// ENTRY EC 1.1.1.30 NAME 3-hydroxybutyrate dehydrogenase NAD-beta-hydroxybutyrate dehydrogenase hydroxybutyrate oxidoreductase beta-hydroxybutyrate dehydrogenase D-beta-hydroxybutyrate dehydrogenase D-3-hydroxybutyrate dehydrogenase D-(-)-3-hydroxybutyrate dehydrogenase beta-hydroxybutyric acid dehydrogenase 3-D-hydroxybutyrate dehydrogenase beta-hydroxybutyric dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-3-hydroxybutanoate:NAD+ oxidoreductase REACTION (R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+ SUBSTRATE (R)-3-hydroxybutanoate NAD+ PRODUCT acetoacetate NADH H+ COMMENT Also oxidizes other 3-hydroxymonocarboxylic acids. PATHWAY PATH: map00072 Synthesis and degradation of ketone bodies PATH: map00650 Butanoate metabolism ORTHOLOG KO: K00019 3-hydroxybutyrate dehydrogenase GENES HSA: 622(BDH) RNO: 117099(Bdh) DME: CG13377-PA(CG13377) XCC: XCC2162(hbdH1) XAC: XAC2045(hbdH1) PAE: PA2003(bdhA) PPU: PP3073(bdhA) ACI: ACIAD2509(bdhA) LPN: lpg2316(bdhA) CVI: CV0695(bdhA) RSO: RS05259 BMA: BMAA0017(bdhA-1) BMAA0876(bdhA-2) BPE: BP0229 BP2454 BPA: BPP3441 BPP3638 BBR: BB3891 BB4073 MLO: mll3632 mlr2400 SME: SMb21010(bdhA) ATU: Atu2308(bdhA) Atu4131 ATC: AGR_C_4198 AGR_L_1444 BME: BMEI0268 BMEII1090 BMS: BR1779 BJA: blr1488(bdhA) blr7029(bdhA) RPA: RPA4206 CCR: CC3384 BSU: BG11155(bdh) BAN: BA4249 BAR: GBAA4249 BAA: BA_4708 BAT: BAS3941 BCE: BC4030 BCA: BCE4084 BCZ: BTZK3788 BTK: BT9727_3773 OIH: OB2631 SPY: SPy1640 SPM: spyM18_1649 SPG: SpyM3_1381 SpyM3_1382 SPS: SPs0480 SPs0481 SPA: M6_Spy1393 CEF: CE2393 SCO: SCO1012(2SCG2.25c) SMA: SAV1420 TTH: TTC0333 MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] REFERENCE 1 [PMID:4291491] Bergmeyer, H.-U., Gawehn, K., Klotzsch, H., Krebs, H.A. and Williamson, D.H. Purification and properties of crystalline 3-hydroxybutyrate dehydrogenase from Rhodopseudomonas spheroides. Biochem. J. 102 (1967) 423-431. 2 [PMID:4954074] Delafield, F.P., Cooksey, K.E. and Doudoroff, M. beta-Hydroxybutyric dehydrogenase and dimer hydrolase of Pseudomonas lemoignei. J. Biol. Chem. 240 (1965) 4023-4028. 3 Lehninger, A.L., Sudduth, H.C. and Wise, J.B. D-beta-Hydroxybutyric dehydrogenase of mitochondria. J. Biol. Chem. 235 (1960) 2450-2455. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.30 ExPASy - ENZYME nomenclature database: 1.1.1.30 ERGO genome analysis and discovery system: 1.1.1.30 BRENDA, the Enzyme Database: 1.1.1.30 CAS: 9028-38-0 /// ENTRY EC 1.1.1.31 NAME 3-hydroxyisobutyrate dehydrogenase beta-hydroxyisobutyrate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3-hydroxy-2-methylpropanoate:NAD+ oxidoreductase REACTION 3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+ SUBSTRATE 3-hydroxy-2-methylpropanoate NAD+ PRODUCT 2-methyl-3-oxopropanoate NADH H+ PATHWAY PATH: map00280 Valine, leucine and isoleucine degradation ORTHOLOG KO: K00020 3-hydroxyisobutyrate dehydrogenase GENES HSA: 11112(HIBADH) MMU: 58875(Hibadh) DME: CG15093-PA(CG15093) CG15093-PC(CG15093) CG4747-PA(CG4747) CEL: B0250.5 ATH: At3g25530(MWL2.23) At4g20930(T13K14.90) At4g29120(F19B15.150) CAL: orf19.5565 STM: STM2918(ygbJ) HIN: HI1010 PMU: PM1366 XCC: XCC1264(mmsB) XAC: XAC1316(mmsB) VCH: VCA0007 VVU: VV20489 VV21637 VVY: VVA0448 VVA1038 VPA: VPA0625 VPA1118 VPA1419 PPR: PBPRB1107 PAE: PA0743 PA1576 PA3312 PA3569(mmsB) PPU: PP1143 PP4666(mmsB) PST: PSPTO0783(mmsB) PSPTO5060 ACI: ACIAD0032 ACIAD1605(mmsB) ACIAD2316 ACIAD3074 SON: SO1682(mmsB) SO2771(garR) CBU: CBU0926(mmsB) LPN: lpg0128 NME: NMB1584 NMA: NMA1773 CVI: CV2081(mmsB) CV3944 RSO: RS05573(mmsB) BPS: BPSS0620(mmsB) BPE: BP1447(mmsB) BP3053 BPA: BPP0881 BPP1554(mmsB) BPP3779 BBR: BB0653 BB0974 BB1031 BB2632(mmsB) BB4224 HPJ: jhp0585 GSU: GSU1372 GSU1451 MLO: mlr0552 mlr1203 mlr2606 SME: SMb20668 SMb20751 SMc00133 ATU: Atu4129(mmsB) ATC: AGR_L_1448 BME: BMEI0688 BMEI1024 BMS: BR0950 BR1314(mmsB) BJA: bll3740 bll6323 blr3957 RPA: RPA1973 RPA3446 CCR: CC1354 CC1574 BSU: BG12914(yfjR) BG13328(ykwC) BHA: BH2634 BAN: BA2353(garR) BAR: GBAA2353(garR) BAA: BA_4720 BA_4721 BAT: BAS2192 BAS3952 BAS3953 BCE: BC2289 BC4042 BCZ: BTZK2115(garR) BTZK3799 BTK: BT9727_2129(garR) BT9727_3784 BLI: BL00292(ykwC) BL03574 OIH: OB0581 OB0815 LMO: lmo1005 LMF: LMOf2365_1026 LIN: lin1004 LLA: L81616(ywjF) LPL: lp_2548(hibD) EFA: EF2889(glxR) CAC: CAC3342 CPE: CPE0393 MPE: MYPE3160 MTU: Rv0751c(mmsB) Rv0770 MTC: MT0775 MT0794 MBO: Mb0773c(mmsB) Mb0793 MPA: MAP0604 MAP4213c(mmsB) SCO: SCO0907(SCM1.40c) SMA: SAV1542 STH: STH938 RBA: RB13140(mmsB) RB3816 TDE: TDE1000 LIL: LA2054 LIC: LIC11860(mmsB) SYN: slr0229(mmsB) SYW: SYNW2430 SYC: syc2237_d(mmsB) GVI: glr3759 ANA: alr3358 PMA: Pro1229(mmsB) PMT: PMT2105 DRA: DR0499 TTH: TTC1749 AAE: aq_038(hibD) MAC: MA0614 TAC: Ta0161 TVO: TVG0242719 PFU: PF0716 APE: APE0756 SSO: SSO0974 SSO1560 STO: ST0619 PAI: PAE1145 MOTIF PS: PS00895 [LIVMFY](2)-G-L-G-x-[MQ]-G-x(2)-[MA]-[SAV]-x-[SNHR] REFERENCE 1 Robinson, W.G. and Coon, M.J. Purification and properties of beta-hydroxyisobutyric dehydrogenase. J. Biol. Chem. 225 (1957) 511-521. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.31 ExPASy - ENZYME nomenclature database: 1.1.1.31 ERGO genome analysis and discovery system: 1.1.1.31 BRENDA, the Enzyme Database: 1.1.1.31 CAS: 9028-39-1 /// ENTRY EC 1.1.1.32 NAME mevaldate reductase mevalonic dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-mevalonate:NAD+ oxidoreductase REACTION (R)-mevalonate + NAD+ = mevaldate + NADH + H+ SUBSTRATE (R)-mevalonate NAD+ PRODUCT mevaldate NADH H+ REFERENCE 1 Schlesinger, M.J. and Coon, M.J. Reduction of mevaldic acid to mevalonic acid by a partial purified enzyme from liver. J. Biol. Chem. 236 (1961) 2421-2424. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.32 ExPASy - ENZYME nomenclature database: 1.1.1.32 ERGO genome analysis and discovery system: 1.1.1.32 BRENDA, the Enzyme Database: 1.1.1.32 CAS: 9028-33-5 /// ENTRY EC 1.1.1.33 NAME mevaldate reductase (NADPH) mevaldate (reduced nicotinamide adenine dinucleotide phosphate) $reductase mevaldate reductase (NADPH2) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-mevalonate:NADP+ oxidoreductase REACTION (R)-mevalonate + NADP+ = mevaldate + NADPH + H+ SUBSTRATE (R)-mevalonate NADP+ PRODUCT mevaldate NADPH H+ COMMENT May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)]. REFERENCE 1 Coon, M.J., Kupiecki, F.P., Dekker, E.E., Schlesinger, M.J. and del Campillo, A. The enzymic synthesis of branched-chain acids. In: Wolstenholme, G.E.W. and O'Connor, M. (Eds.), CIBA Symposium on the Biosynthesis of Terpenes and Sterols, Churchill, London, 1959, p. 62-74. 2 von Wartburg, J.P. and Wermoth, B. Aldehyde reductase. In: Jakoby, W.B. (Ed.), Enzymatic Basis of Detoxication, vol. 1, Academic Press, New York, 1980, p. 249-260. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.33 ExPASy - ENZYME nomenclature database: 1.1.1.33 ERGO genome analysis and discovery system: 1.1.1.33 BRENDA, the Enzyme Database: 1.1.1.33 CAS: 9028-34-6 /// ENTRY EC 1.1.1.34 NAME hydroxymethylglutaryl-CoA reductase (NADPH) hydroxymethylglutaryl coenzyme A reductase (reduced nicotinamide $adenine dinucleotide phosphate) 3-hydroxy-3-methylglutaryl-CoA reductase beta-hydroxy-beta-methylglutaryl coenzyme A reductase hydroxymethylglutaryl CoA reductase (NADPH) S-3-hydroxy-3-methylglutaryl-CoA reductase NADPH-hydroxymethylglutaryl-CoA reductase HMGCoA reductase-mevalonate:NADP-oxidoreductase (acetylating-CoA) 3-hydroxy-3-methylglutaryl CoA reductase (NADPH) hydroxymethylglutaryl-CoA reductase (NADPH2) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-mevalonate:NADP+ oxidoreductase (CoA-acylating) REACTION (R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ SUBSTRATE (R)-mevalonate CoA NADP+ PRODUCT (S)-3-hydroxy-3-methylglutaryl-CoA NADPH H+ COMMENT The enzyme is inactivated by EC 2.7.1.109 {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and reactivated by EC 3.1.3.47 {[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase}. PATHWAY PATH: map00100 Biosynthesis of steroids ORTHOLOG KO: K00021 3-hydroxy-3-methylglutaryl-CoA reductase GENES HSA: 3156(HMGCR) RNO: 25675(Hmgcr) DME: CG10367-PA(CG10367) CEL: F08F8.2 ATH: At1g76490(F14G6.9) At2g17370(F5J6.1) SCE: YLR450W(HMG2) YML075C(HMG1) AGO: AER152W(AER152Wp) SPO: SPCC162.09c(hmg1) ECU: ECU10_1720 VCH: VCA0723 VVU: VV20117 VVY: VVA0625 VPA: VPA0968 CBU: CBU0030 CBU0610 LPN: lpg2052 CVI: CV1806 OIH: OB0224 SAU: SA2333(mvaA) SAV: SAV2545(mvaA) SAM: MW2466(mvaA) SEP: SE2109 LMO: lmo0825 LMF: LMOf2365_0844 LIN: lin0821 LLA: L10433(mvaA) SPY: SPy0880(mvaS.1) SPM: spyM18_0941(mvaS1) SPG: SpyM3_0599(mvaS.1) SPS: SPs1254 SPA: M6_Spy0703 SPN: SP1726 SPR: spr1570(mvaA) SAG: SAG1317 SAN: gbs1387 SMU: SMU.942(mvaA) LPL: lp_0447(mvaA) LJO: LJ1608 EFA: EF1364 BBU: BB0685(mvaA) MJA: MJ0705(hmgA) MMP: MMP0087(hmgA) MAC: MA3073(hmgA) MMA: MM0335 MTH: MTH562 MKA: MK0355(HMG1) AFU: AF1736(mvaA) HAL: VNG1875G(mvaA) HMA: rrnAC3412(mvaA) TAC: Ta0406 TVO: TVG1221182 PTO: PTO1143 PHO: PH1805 PAB: PAB2106(mvaA) PFU: PF1848 APE: APE1869 SSO: SSO0531 STO: ST1352 PAI: PAE2182 DISEASE MIM: 142910 3-hydroxy-3-methylglutaryl-Coenzyme A reductase; MOTIF PS: PS00066 [RKH]-x(6)-D-x-M-G-x-N-x-[LIVMA] PS: PS00318 [LIVM]-G-x-[LIVM]-G-G-[AG]-T PS: PS01192 A-[LIVM]-x-[STAN]-x(2)-[LI]-x-[KRNQ]-[GSA]-H-[LM]-x- [FYLH] PS: PS50065 Hydroxymethylglutaryl- coenzyme A reductases family profile PS: PS50156 Sterol-sensing domain (SSD) profile STRUCTURES PDB: 1DQ8 1DQ9 1DQA 1HW8 1HW9 1HWI 1HWJ 1HWK 1HWL REFERENCE 1 Bucher, N.L.R., Overath, P. and Lynen, F. beta-Hydroxy-beta-methylglutaryl coenzyme A reductase, cleavage and condensing enzymes in relation to cholesterol formation in rat liver. Biochim. Biophys. Acta 40 (1960) 491-501. 2 Durr, I.F. and Rudney, H. The reduction of beta-hydroxy-beta-methylglutaryl coenzyme A to mevalonic acid. J. Biol. Chem. 235 (1960) 2572-2578. 3 [PMID:4985697] Kawachi, T. and Rudney, H. Solubilization and purification of beta-hydroxy-beta-methylglutaryl coenzyme A reductase from rat liver. Biochemistry 9 (1970) 1700. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.34 ExPASy - ENZYME nomenclature database: 1.1.1.34 ERGO genome analysis and discovery system: 1.1.1.34 BRENDA, the Enzyme Database: 1.1.1.34 CAS: 9028-35-7 /// ENTRY EC 1.1.1.35 NAME 3-hydroxyacyl-CoA dehydrogenase beta-hydroxyacyl dehydrogenase beta-keto-reductase 3-keto reductase 3-hydroxyacyl coenzyme A dehydrogenase beta-hydroxyacyl-coenzyme A synthetase beta-hydroxyacylcoenzyme A dehydrogenase beta-hydroxybutyrylcoenzyme A dehydrogenase 3-hydroxyacetyl-coenzyme A dehydrogenase L-3-hydroxyacyl coenzyme A dehydrogenase L-3-hydroxyacyl CoA dehydrogenase beta-hydroxyacyl CoA dehydrogenase 3beta-hydroxyacyl coenzyme A dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase beta-ketoacyl-CoA reductase beta-hydroxy acid dehydrogenase 3-L-hydroxyacyl-CoA dehydrogenase 3-hydroxyisobutyryl-CoA dehydrogenase 1-specific DPN-linked beta-hydroxybutyric dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase REACTION (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+ SUBSTRATE (S)-3-hydroxyacyl-CoA NAD+ PRODUCT 3-oxoacyl-CoA NADH H+ COMMENT Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacyl-hydrolipoate. Some enzymes act, more slowly, with NADP+. Broad specificity to acyl chain-length (cf. EC 1.1.1.211 [long-chain-3-hydroxyacyl-CoA dehydrogenase]). PATHWAY PATH: map00062 Fatty acid biosynthesis (path 2) PATH: map00071 Fatty acid metabolism PATH: map00280 Valine, leucine and isoleucine degradation PATH: map00310 Lysine degradation PATH: map00380 Tryptophan metabolism PATH: map00632 Benzoate degradation via CoA ligation PATH: map00650 Butanoate metabolism ORTHOLOG KO: K00022 3-hydroxyacyl-CoA dehydrogenase GENES HSA: 1962(EHHADH) 3028(HADH2) 3030(HADHA) 3033(HADHSC) MMU: 15107(Hadhsc) 15108(Hadh2) 74147(Ehhadh) RNO: 113965(Hadhsc) 63864(Hsd17b10) DME: CG7113-PA(CG7113) CEL: B0272.3 C29F3.1 F01G10.2 F01G10.3 F01G4.2(ard-1) F54C8.1 R09B5.6 CAL: orf19.1809(FOX2) CHO: Chro.30048 ECO: b2341(yfcX) b3846(fadB) ECJ: JW2338(yfcX) JW3822(fadB) ECE: Z3604 Z5367(fadB) ECS: ECs3224 ECs4774 ECC: c2886 c4793(fadB) STY: STY2620 STY3577(fadB) STT: t0476 t3315(fadB) STM: STM2388(yfcX) STM3983(fadB) YPE: YPO2747(faoA) YPO3766(fadB) YPK: y0464(fadB) y1580 YPM: YP2417(faoA) YP3282(fadB) YPS: YPTB0267(fadB) YPTB2636(faoA) SFL: SF2419 SF3922(fadB) SFX: S2554 S3830(fadB) ECA: ECA0208(fadB) ECA3078 PLU: plu3200 plu4402(fadB) XCC: XCC1266(fadB) XCC1831(hadH2) XCC1979(fadB) XAC: XAC1318(fadB) XAC1850(hadH2) XAC2013(fadB) VCH: VC1047 VC2758 VVU: VV10981 VV11976 VVY: VV0029 VV2440 VPA: VP2208 PPR: PBPRA0064 PBPRA0962 PAE: PA1737 PA2554 PA3014(faoA) PA5188 PA5386 PPU: PP0302 PP2047 PP2136(fadB) PP2214(fadB2x) PST: PSPTO3517(fadB) ACI: ACIAD0335(fadB) ACIAD1565 ACIAD2416 SON: SO0021(fadB) SO3088 CBU: CBU0847 LPN: lpg0905 CVI: CV2720(fadB) RSO: RS02946 RS04421 RS05766 BPE: BP0669 BP2038 BP2770 BPA: BPP1725 BPP2559 BPP4217 BBR: BB0762 BB2004 BB3383 BB4805 NEU: NE1528 BBA: Bd1836 RPR: RP560(fadB) RTY: RT0547(fadB) RCO: RC0836 RC0837 RC0838 RC0839 RC0840 RC0841 RC0842 MLO: mll4199 mlr2803 mlr5041 mlr5629 SME: SMa1452 SMb21632 SMc01638 SMc02227(fadB) ATU: Atu0503(fadB) Atu1415 Atu5344 ATC: AGR_C_2613 AGR_C_888 AGR_pAT_493 BME: BMEII0497 BMEII0816 BMS: BRA0449 BRA0793(fadB) BJA: bll7804 bll7821 blr1160(fadB) blr2428 blr7846 RPA: RPA0482 RPA0818 RPA1705 RPA2303 RPA3717(pimF) CCR: CC0076 CC0124 CC3189 BSU: BG14024(yusL) BHA: BH3488 BAN: BA5249 BAR: GBAA5249 BAA: BA_0114 BAT: BAS4877 BCE: BC5004 BCA: BCE5144 BCZ: BTZK4734(fadB) BTK: BT9727_5027(hbd) BLI: BL02180(yusL) OIH: OB0997 OB2395 OB2673 SAU: SA0224 SAV: SAV0232 SAM: MW0208 SAR: SAR0224(fadB) SAS: SAS0208 SEP: SE0220 CTC: CTC02426 MTU: Rv0468(fadB2) Rv0860(fadB) Rv1144 MTC: MT0484 MT0883 MT1177 MBO: Mb0883(fadB) Mb1176 MLE: ML2161(fadB) ML2461(fadB2) MPA: MAP0790(fadB_1) MAP1715(fadB_2) MAP2637c MAP3116c MAP3962(fadB2) CEF: CE0722 SCO: SCO0984(SCBAC19F3.11) SCO1591(SCI35.13) SCO6297(SCBAC8D1.10c) SCO6732(SC5F2A.15) SCO6789(SC6A5.38) SMA: SAV1680(fadB1) SAV2045(fadC2) SAV2889(fadC4) SAV6748(fadC5) SAV716(fadC6) LXX: Lxx04210(fadB) RBA: RB1092(faoA) LIL: LA4138(had) LIC: LIC13300(fadB) DRA: DR1487 DRA0143 TTH: TTC0331 TTC0534 AFU: AF0017(hbd-1) AF0285(hbd-2) AF0434(hbd-3) AF1025(hbd-4) AF1122(hbd-5) AF1177(hbd-6) AF1190(hbd-7) AF1206(hbd-8) AF2017(hbd-9) AF2273(hbd-10) HAL: VNG0681G(hbd1) VNG1313G(hbd2) HMA: rrnAC0264(hbd-1) rrnAC0771(paaH) rrnAC1083(hbd1) rrnAC1982(hbd2) rrnB0238(hbd3) TAC: Ta0291 Ta0476 TVO: TVG0862758 TVG1375310 APE: APE1484 SSO: SSO2514 STO: ST0069 PAI: PAE1383 DISEASE MIM: 300256 Hydroxlacyl-CoA dehydrogenase, type II MIM: 600890 Hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/ MIM: 601609 L-3-hydroxyacyl-CoA dehydrogenase, short chain MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] PS: PS00067 [DNE]-x(2)-[GA]-F-[LIVMFY]-x-[NT]-R-x(3)-[PA]- [LIVMFY](2)-x(5)-[LIVMFYCT]-[LIVMFY]-x(2)-[GV] PS: PS00166 [LIVM]-[STA]-x-[LIVM]-[DENQRHSTA]-G-x(3)-[AG](3)-x(4)- [LIVMST]-x-[CSTA]-[DQHP]-[LIVMFY] PS: PS00342 [STAGCN]-[RKH]-[LIVMAFY]> STRUCTURES PDB: 1E3S 1E3W 1E6W 1F0Y 1F12 1F14 1F17 1IL0 1LSJ 1LSO 1M75 1M76 1SO8 1U7T 1WDK 1WDL 1WDM 2HDH 3HAD 3HDH REFERENCE 1 Hillmer, P. and Gottschalk, G. Solubilization and partial characterisation of particulate dehydrogenases from Clostridium kluyveri. Biochim. Biophys. Acta 334 (1974) 12-23. 2 [PMID:13115428] Lehninger, A.L. and Greville, G.D. The enzymatic oxidation of d- and l-beta-hydroxybutyrate. Biochim. Biophys. Acta 12 (1953) 188-202. 3 Stern, J.R. Crystalline beta-hydroxybutyrate dehydrogenase from pig heart. Biochim. Biophys. Acta 26 (1957) 448-449. 4 Wakil, S.J., Green, D.E., Mii, S. and Mahler, H.R. Studies on the fatty acid oxidizing system of animal tissues. VI. beta-Hydroxyacyl coenzyme A dehydrogenase. J. Biol. Chem. 207 (1954) 631-638. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.35 ExPASy - ENZYME nomenclature database: 1.1.1.35 ERGO genome analysis and discovery system: 1.1.1.35 BRENDA, the Enzyme Database: 1.1.1.35 CAS: 9028-40-4 /// ENTRY EC 1.1.1.36 NAME acetoacetyl-CoA reductase acetoacetyl coenzyme A reductase hydroxyacyl coenzyme-A dehydrogenase NADP-linked acetoacetyl CoA reductase NADPH:acetoacetyl-CoA reductase D(-)-beta-hydroxybutyryl CoA-NADP oxidoreductase short chain beta-ketoacetyl(acetoacetyl)-CoA reductase beta-ketoacyl-CoA reductase D-3-hydroxyacyl-CoA reductase (R)-3-hydroxyacyl-CoA dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase REACTION (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH + H+ SUBSTRATE (R)-3-hydroxyacyl-CoA NADP+ PRODUCT 3-oxoacyl-CoA NADPH H+ PATHWAY PATH: map00650 Butanoate metabolism ORTHOLOG KO: K00023 acetoacetyl-CoA reductase GENES XFA: XF0319 XFT: PD0262(fabG) XCC: XCC2294(phbB) XCC3355(phbB) XAC: XAC2401(phbB) XAC3486(phbB) VCH: VCA0691 VVU: VV20742 VVY: VVA1211 VPA: VPA1205 PPR: PBPRB1841(phbB) SON: SO3263 LPN: lpg0560(phaB) lpg0561(phaB) lpg1059(phaB) CVI: CV2364(phaB) RSO: RS03996(phbB) BMA: BMA1320(phbB-1) BMAA0166(phbB-2) BPS: BPSL1536(phbB) BPSS1916(phbB) BPE: BP0772 BP1150(phbB) BPA: BPP0333 BPP3195(phbB) BBR: BB0336 BB3595(phbB) BB4750 RPR: RP035(phbB) RTY: RT0095(phbB) RCO: RC0054(phbB) MLO: mlr3848 SME: SMc03878(phbB) ATU: Atu2770(phbB) ATC: AGR_C_5024(phbB) BJA: bll0225(phbB) blr3725(phbB) RPA: RPA0532 CCR: CC0511 BAN: BA1330 BAR: GBAA1330 BAA: BA_1853 BAT: BAS1230 BCE: BC1317 BCA: BCE1429 BTK: BT9727_1207(phaB) CGL: NCgl2358(Cgl2444) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] REFERENCE 1 Wakil, S.J. and Bressler, R. Studies on the mechanism of fatty acid synthesis. X. Reduced triphosphopyridine nucleotide-acetoacetyl coenzyme A reductase. J. Biol. Chem. 237 (1962) 687-693. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.36 ExPASy - ENZYME nomenclature database: 1.1.1.36 ERGO genome analysis and discovery system: 1.1.1.36 UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.36 BRENDA, the Enzyme Database: 1.1.1.36 CAS: 9028-41-5 /// ENTRY EC 1.1.1.37 NAME malate dehydrogenase malic dehydrogenase L-malate dehydrogenase NAD-L-malate dehydrogenase malic acid dehydrogenase NAD-dependent malic dehydrogenase NAD-malate dehydrogenase NAD-malic dehydrogenase malate (NAD) dehydrogenase NAD-dependent malate dehydrogenase NAD-specific malate dehydrogenase NAD-linked malate dehydrogenase MDH L-malate-NAD+ oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S)-malate:NAD+ oxidoreductase REACTION (S)-malate + NAD+ = oxaloacetate + NADH + H+ SUBSTRATE (S)-malate NAD+ PRODUCT oxaloacetate NADH H+ COMMENT Also oxidizes some other 2-hydroxydicarboxylic acids. PATHWAY PATH: map00020 Citrate cycle (TCA cycle) PATH: map00620 Pyruvate metabolism PATH: map00630 Glyoxylate and dicarboxylate metabolism PATH: map00710 Carbon fixation PATH: map00720 Reductive carboxylate cycle (CO2 fixation) ORTHOLOG KO: K00024 malate dehydrogenase KO: K00025 malate dehydrogenase KO: K00026 malate dehydrogenase GENES HSA: 4190(MDH1) 4191(MDH2) MMU: 17448(Mdh2) 17449(Mdh1) RNO: 24551(Mdh1) 81829(Mor1) DME: CG10748-PA(CG10748) CG10749-PA(CG10749) CG5362-PA(CG5362) CG7998-PA(CG7998) CEL: F20H11.3(mdh-1) F46E10.10a ATH: At1g04410(F19P19.13) At1g53240(F12M16.14) At2g22780(T30L20.4) At3g15020(K15M2.16) At3g47520(F1P2.70) At5g09660(F17I14.150) At5g43330(MNL12.18) At5g56720(MIK19.17) CME: CMP193C CMT611C SCE: YDL078C(MDH3) YKL085W(MDH1) YOL126C(MDH2) AGO: ADL164C(ADL164Cp) ADR152C(ADR152Cp) ADR252W(ADR252Wp) CAL: orf19.4602(MDH1) orf19.5323(MDH3) orf19.7481(MDH2) SPO: SPCC306.08c PFA: MAL6P1.242 CHO: Chro.70062 ECO: b0801(ybiC) b3236(mdh) b3575(yiaK) ECJ: JW0786(ybiC) JW3205(mdh) JW3547(yiaK) ECE: Z1022(ybiC) Z4595(mdh) ECS: ECs0879 ECs4109 ECC: c0885(ybiC) c3991(mdh) c4396(yiaK) c5039 STY: STY3539(mdh) STY4130 STT: t3274(mdh) t3851 STM: STM3081 STM3359(mdh) STM3668(yiaK) YPE: YPO3516(mdh) YPK: y0668(mdh) YPM: YP0567(mdh) YPS: YPTB0460(mdh) SFL: SF0751(ybiC) SF3276(mdh) SF3619(yiaK) SFX: S0792(ybiC) S3491(mdh) S4150(yiaK) ECA: ECA0685(mdh) ECA1527 PLU: plu4547(mdh) HIN: HI1031 HI1210(mdh) HDU: HD0264(mdh) PMU: PM0550(mdh_2) PM1256 MSU: MS0054 XFA: XF1211 XFT: PD0492(mdh) XCC: XCC0928(mdh) XAC: XAC1006(mdh) VCH: VC0432 VVU: VV10673 VVY: VV0467 VPA: VP0325 PPR: PBPRA0391(mdh) PAE: PA1252 PPU: PP0654(mdh) PP3591 PST: PSPTO2359(allD) ACI: ACIAD3155(mdh) SON: SO0770(mdh) CBU: CBU1241(mdh) LPN: lpg2352(mdh) MCA: MCA0610(mdh) CVI: CV1062(mdh) RSO: RS03566(mdh) BMA: BMAA1751(mdh) BPS: BPSS1722(mdh) BPE: BP2365(mdH) BP2521 BP2780 BPA: BPP2552 BPP3232(mdH) BPP4084 BBR: BB1997 BB2374 BB3684(mdH) BB4555 NEU: NE0773 HHE: HH1571(mdh) WSU: WS1064(citH) CJE: Cj0532(mdh) GSU: GSU1466(mdh) BBA: Bd0928(mdh) DPS: DP0661 RPR: RP376(mdh) RTY: RT0365(mdh) RCO: RC0520(mdh) WOL: WD1121(mdh) MLO: mll4308 mll5197 mlr9117 mlr9216 SME: SMa0265 SMa1459 SMb20261 SMc02035 SMc02479(mdh) ATU: Atu0164(mdh) Atu2639(mdh) Atu3208 Atu4676(mdh) ATC: AGR_C_268 AGR_C_4782 AGR_L_3209 AGR_L_410 BME: BMEI0137 BMEII1005 BMS: BR1927(mdh) BRA0240 BJA: bll0456(mdh) bll2917 bll6274 blr7581 RPA: RPA0192(mdh) RPA3756 BHE: BH16570(mdh) BQU: BQ13450(mdh) CCR: CC3655 BSU: BG11386(mdh) BG13206(yjmC) BHA: BH3158(citH) BAN: BA4837(mdh) BAR: GBAA4837(mdh) BAA: BA_5260 BAT: BAS4486 BCE: BC4592 BCA: BCE4723(mdh) BCZ: BTZK4333(mdh) BTZK4344(mdh) BTK: BT9727_4321(mdh) BT9727_4332(mdh) BLI: BL00397(mdh) OIH: OB2166(citH) OB2846 SEP: SE0461 LPL: lp_3150 CAC: CAC0566 MTU: Rv1240(mdh) MTC: MT1278 MBO: Mb1272(mdh) MLE: ML1091(mdh) MPA: MAP2541c(mdh) CGL: NCgl2297(Cgl2380) CEF: CE2285(mdh) CDI: DIP1787(mdh) SCO: SCO4827(SC2A6.12) SMA: SAV3436(mdh) PAC: PPA1740 STH: STH2543 RBA: RB7652(mdh) RB856(ldh) CTR: CT376(mdhC) CMU: TC0655 CPN: CPn1028 CPA: CP0824 CPJ: CPj1028(mdhC) CPT: CpB1067 CCA: CCA00734(mdh) PCU: pc1772(mdh) LIL: LA2139(mdh) LIC: LIC11781(mdh) BTH: BT2510 BT3911 PGI: PG1949(mdh) SYN: sll0891(citH) GVI: gll2542 ANA: alr4322 CTE: CT1507(mdh) DRA: DR0325 TTH: TTC0168 AAE: aq_1665(mdh2) aq_1782(mdh1) MJA: MJ0490(ldh) MMP: MMP0645(mdh) MAC: MA0819 MMA: MM1966 MTH: MTH188 MKA: MK1069(ldh) AFU: AF0855(mdhA) HAL: VNG2367G(mdhA) HMA: rrnAC2706(mdh) TAC: Ta0952 TVO: TVG1151701 PTO: PTO0994 PHO: PH1277 PAB: PAB1791 APE: APE0672 SSO: SSO2585(sqdB) STO: ST1811 ST2090 PAI: PAE2370 DISEASE MIM: 154100 Malate dehydrogenase, mitochondrial MIM: 154200 Malate dehydrogenase, soluble MOTIF PS: PS00064 [LIVMA]-G-[EQ]-H-G-[DN]-[ST] PS: PS00068 [LIVM]-T-[TRKMN]-L-D-x(2)-R-[STA]-x(3)-[LIVMFY] PS: PS00342 [STAGCN]-[RKH]-[LIVMAFY]> STRUCTURES PDB: 1BDM 1BMD 1D3A 1EMD 1GT2 1GUY 1GUZ 1GV0 1GV1 1HLP 1HR9 1IB6 1IE3 1IZ9 1MLD 1O6Z 1OJS 1OJU 1UR5 1UXG 1UXH 1UXI 1UXJ 1UXK 2CMD 2HLP 4MDH 5MDH REFERENCE 1 Banaszak, L.J. and Bradshaw, R.A. Malate dehydrogenase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic Press, New York, 1975, p. 369-396. 2 [PMID:5637713] Guha, A., Englard, S. and Listowsky, I. Beef heart malic dehydrogenases. VII. Reactivity of sulfhydryl groups and conformation of the supernatant enzyme. J. Biol. Chem. 243 (1968) 609-615. 3 [PMID:4313528] McReynolds, M.S. and Kitto, G.B. Purification and properties of Drosophila malate dehydrogenases. Biochim. Biophys. Acta 198 (1970) 165-175. 4 Wolfe, R.G. and Nielands, J.B. Some molecular and kinetic properties of heart malic dehydrogenase. J. Biol. Chem. 221 (1956) 61-69. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.37 ExPASy - ENZYME nomenclature database: 1.1.1.37 ERGO genome analysis and discovery system: 1.1.1.37 BRENDA, the Enzyme Database: 1.1.1.37 CAS: 9001-64-3 /// ENTRY EC 1.1.1.38 NAME malate dehydrogenase (oxaloacetate-decarboxylating) 'malic' enzyme pyruvic-malic carboxylase NAD-specific malic enzyme NAD-malic enzyme NAD-linked malic enzyme CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating) REACTION (S)-malate + NAD+ = pyruvate + CO2 + NADH SUBSTRATE (S)-malate NAD+ PRODUCT pyruvate CO2 NADH COMMENT Also decarboxylates added oxaloacetate. PATHWAY PATH: map00620 Pyruvate metabolism ORTHOLOG KO: K00027 malate dehydrogenase (oxaloacetate-decarboxylating) GENES HSA: 4200(ME2) SCE: YKL029C(MAE1) AGO: AGL068W(AGL068Wp) CAL: orf19.3419(MAE1) SPO: SPCC794.12c(mae2) ECO: b1479(sfcA) ECJ: JW1475(sfcA) ECE: Z2231(sfcA) ECS: ECs2083 ECC: c1912(sfcA) STY: STY1494(sfcA) STT: t1481(sfcA) STM: STM1566(sfcA) YPE: YPO1511(sfcA) YPK: y2658(sfcA) YPM: YP1401(sfcA1) YPS: YPTB1526(sfcA) SFL: SF1746(sfcA) SFX: S1879(sfcA) ECA: ECA2831(sfcA) PLU: plu1546(maeA) VCH: VC1188 VC2681 VVU: VV11361 VV12801 VVY: VV1464 VV2242 VV3010 VPA: VP1258 VP2767 PPR: PBPRA0259 PBPRA1997 PBPRB1354 PAE: PA3471 PA5046 PPU: PP5085(maeB) PST: PSPTO3924(sfcA) PSPTO5134 ACI: ACIAD0166(sfcA) SON: SO3855(sfcA) SO4118 CBU: CBU0823(sfcA) LPN: lpg0651 lpg1280(sfcA) lpg2971(maeA) MCA: MCA1836(sfcA) NME: NMB0671 NMA: NMA0870(maeA) NEU: NE0438 HHE: HH1094 CJE: Cj1287c GSU: GSU2308(scfA) BBA: Bd2834(sfcA) DPS: DP2203 RTY: RT0361(tme) BJA: bll6469 BSU: BG11312(ywkA) BG11764(yqkJ) BG12614(malS) BG13922(ytsJ) BHA: BH0399 BH3168 BAN: BA0579 BA1801(ykwA) BA3145 BA4848 BAR: GBAA0579 GBAA1801(ykwA) GBAA3145 GBAA4848 BAA: BA_1159 BA_2306 BA_5271 BAT: BAS0548 BAS1668 BAS2923 BAS4497 BCE: BC0580 BC1741 BC4604 BCA: BCE0642 BCE1873(ykwA) BCE4734 BCZ: BTZK0492(sfcA) BTZK1615 BTK: BT9727_0490(sfcA) BT9727_1650 BLI: BL00044(malS) BL00406(ytsJ) BL00922(mleA) BL03976(ywkA) OIH: OB2176 OB3218 SAU: SA1524 SAV: SAV1702 SAM: MW1645 SAR: SAR0824 SAR1780 SAS: SAS1629 SEP: SE1377 LMO: lmo1915 LMF: LMOf2365_1944(sfcA) LIN: lin2029 LLA: L121483(mleS) L3227(mae) SMU: SMU.137(mleS) LPL: lp_1105(mae) lp_1118(mleS) EFA: EF3316 CAC: CAC1589(malS) CAC1596(malS) CPE: CPE1151 CTC: CTC00356 CTC02463 TTE: TTE2332(sfcA) POY: PAM721(sfcA) MTU: Rv2332(mez) MTC: MT2394 MBO: Mb2360(mez) MPA: MAP2540c SCO: SCO2951(SCE59.10c) SCO5261(2SC7G11.23) SMA: SAV1514(malS1) SAV2981 SAV3870(malS2) SAV5126 PAC: PPA0313 PPA0888 STH: STH1319 STH2534 RBA: RB307 TDE: TDE2446 SYN: slr0721(me) SYC: syc0256_c TEL: tll1440 GVI: gll2149 ANA: alr4596 DRA: DR2583 DRA0276 TMA: TM0542 MAC: MA1735 MMA: MM2632 AFU: AF1727(mae) TAC: Ta0456 TVO: TVG0785282 PTO: PTO0957 PHO: PH1275 PAB: PAB1792(mae) PFU: PF1026 APE: APE0392 SSO: SSO2869 STO: ST0114 ST0278 PAI: PAE1688 DISEASE MIM: 154270 Malic enzyme, mitochondrial MOTIF PS: PS00331 F-x-[DV]-D-x(2)-G-T-[GSA]-x-[IV]-x-[LIVMA]-[GAST](2)- [LIVMF](2) STRUCTURES PDB: 1GZ3 1LLQ 1O0S 1PJL REFERENCE 1 Kaufman, S., Korkes, S. and del Campillo, A. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. V. Further studies of the "malic" enzyme of Lactobacillus arabinosus. J. Biol. Chem. 192 (1951) 301-312. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.38 ExPASy - ENZYME nomenclature database: 1.1.1.38 ERGO genome analysis and discovery system: 1.1.1.38 BRENDA, the Enzyme Database: 1.1.1.38 CAS: 9080-52-8 /// ENTRY EC 1.1.1.39 NAME malate dehydrogenase (decarboxylating) 'malic' enzyme pyruvic-malic carboxylase NAD-specific malic enzyme NAD-malic enzyme CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S)-malate:NAD+ oxidoreductase (decarboxylating) REACTION (S)-malate + NAD+ = pyruvate + CO2 + NADH SUBSTRATE (S)-malate NAD+ PRODUCT pyruvate CO2 NADH COMMENT Does not decarboxylate added oxaloacetate. PATHWAY PATH: map00620 Pyruvate metabolism PATH: map00710 Carbon fixation ORTHOLOG KO: K00028 malate dehydrogenase (decarboxylating) GENES ATH: At4g00570(F6N23.16) MLO: mlr0809 SME: SMc00169(dme) ATU: Atu1652(maeB) ATC: AGR_C_3042 BME: BMEI0967 BMS: BR1017(maeB) BJA: blr4145(dme) BHE: BH07470 BQU: BQ05320 SPY: SPy1110 SPM: spyM18_1072 SPG: SpyM3_0771 SPS: SPs0971 SPA: M6_Spy0831 SAG: SAG1919 SAN: gbs1906 EFA: EF1206 MOTIF PS: PS00331 F-x-[DV]-D-x(2)-G-T-[GSA]-x-[IV]-x-[LIVMA]-[GAST](2)- [LIVMF](2) STRUCTURES PDB: 1DO8 1EFK 1EFL 1PJ2 1PJ3 1PJ4 1QR6 REFERENCE 1 Saz, H.J. and Hubbard, J.A. The oxidative decarboxylation of malate by Ascoris lumbricoides. J. Biol. Chem. 225 (1957) 921-933. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.39 ExPASy - ENZYME nomenclature database: 1.1.1.39 ERGO genome analysis and discovery system: 1.1.1.39 BRENDA, the Enzyme Database: 1.1.1.39 CAS: 9028-46-0 /// ENTRY EC 1.1.1.40 NAME malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) 'malic' enzyme pyruvic-malic carboxylase malate dehydrogenase (decarboxylating, NADP) NADP-linked decarboxylating malic enzyme NADP-malic enzyme NADP-specific malic enzyme NADP-specific malate dehydrogenase malate dehydrogenase (NADP, decarboxylating) L-malate:NADP oxidoreductase malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S)-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating) REACTION (S)-malate + NADP+ = pyruvate + CO2 + NADPH SUBSTRATE (S)-malate NADP+ PRODUCT pyruvate CO2 NADPH COMMENT Also decarboxylates added oxaloacetate. PATHWAY PATH: map00620 Pyruvate metabolism PATH: map00710 Carbon fixation ORTHOLOG KO: K00029 malate dehydrogenase (oxaloacetate-decarboxylating)(NADP+) GENES HSA: 10873(ME3) 4199(ME1) MMU: 109264(B230207H15Rik) 17436(Mod1) RNO: 24552(Me1) DME: CG10120-PA(CG10120) CG10120-PB(CG10120) CG5889-PA(CG5889) CEL: Y48B6A.12 ATH: At1g79750(F19K16.27) At2g19900(F6F22.7) At5g11670(T22P22.60) At5g25880(F18A17.1) CME: CMJ051C CHO: Chro.50314 ECO: b2463(maeB) ECJ: JW2447(421#19) ECE: Z3719 ECS: ECs3325 ECC: c2988 STY: STY2709(maeB) STT: t0387(maeB) STM: STM2472(maeB) YPE: YPO3034(maeB) YPK: y1449 YPM: YP2657(sfcA2) YPS: YPTB2756(maeB) SFL: SF2505 SFX: S2656 ECA: ECA0871(maeB) PLU: plu2719(maeB) HIN: HI1245 HDU: HD1247(maeA) PMU: PM0002(mdh_1) MSU: MS0390(sfcA) XFA: XF0977 XFT: PD0272(maeB) XCC: XCC3345(maeB) XAC: XAC3470(maeB) ACI: ACIAD2287 CVI: CV0916(maeB) RSO: RS00080(maeB2) RS01481(maeB1) BMA: BMA2477(maeB1) BMA2586(maeB-2) BPS: BPSL2959(maeB) BPSL3242 BPE: BP1064(maeB) BP1120(maeB) BP3456(maeB) BPA: BPP0832(maeB) BPP1160(maeB) BPP3221(maeB) BBR: BB0926(maeB) BB1376(maeB) BB3673(maeB) GSU: GSU1700(maeB) DVU: DVU0414 BBA: Bd1833(mdh) Bd1834 RPR: RP373(tme) RCO: RC0507(tme) WOL: WD0488(maeB) MLO: mlr5329 SME: SMc01126(tme) ATU: Atu3356 ATC: AGR_L_2933 BME: BMEI1802 BMEI1803 BJA: blr3726(tme) RPA: RPA3042(mao) BHE: BH01010(maeB) BQU: BQ00940(maeB) CCR: CC2622 CC3549 BSU: BG12614(malS) BLI: BL00044(malS) CAC: CAC1589(malS) CGL: NCgl2904(Cgl3007) CEF: CE2839(malE) LIL: LA0181(maeB) LIC: LIC10160(maeB) BTH: BT1969 PGI: PG0279(maeB) TTH: TTC0144 HAL: VNG1624G(mdh) HMA: rrnAC1754(maeB) DISEASE MIM: 154250 Malic enzyme, cytoplasmic MIM: 604626 Malic enzyme 3 MOTIF PS: PS00331 F-x-[DV]-D-x(2)-G-T-[GSA]-x-[IV]-x-[LIVMA]-[GAST](2)- [LIVMF](2) STRUCTURES PDB: 1GQ2 1GZ4 REFERENCE 1 Harary, I., Korey, S.R. and Ochoa, S. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. VII. Equilibrium of "malic" enzyme reaction. J. Biol. Chem. 203 (1953) 595-604. 2 Ochoa, S., Mehler, A.H. and Kornberg, A. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. I. Isolation and properties of an enzyme from pigeon liver catalyzing the reversible oxidative decarboxylation of l-malic acid. J. Biol. Chem. 174 (1948) 979-1000. 3 Rutter, W.J. and Lardy, H.A. Purification and properties of pigeon liver malic enzyme. J. Biol. Chem. 233 (1958) 374-382. 4 Strickland, R.G. Some properties of the malic enzyme of pigeon liver. 1. Conversion of malate into pyruvate. Biochem. J. 73 (1959) 646-654. 5 Strickland, R.G. Some properties of the malic enzyme of pigeon liver. 2. Synthesis of malate from pyruvate. Biochem. J. 73 (1959) 654-659. 6 Walker, D.A. Physiological studies on acid metabolism. 7. Malic enzyme from Kalanchoe crenata: effects of carbon dioxide concentration. Biochem. J. 74 (1960) 216-223. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.40 ExPASy - ENZYME nomenclature database: 1.1.1.40 ERGO genome analysis and discovery system: 1.1.1.40 BRENDA, the Enzyme Database: 1.1.1.40 CAS: 9028-47-1 /// ENTRY EC 1.1.1.41 NAME isocitrate dehydrogenase (NAD+) isocitric dehydrogenase beta-ketoglutaric-isocitric carboxylase isocitric acid dehydrogenase NAD dependent isocitrate dehydrogenase NAD isocitrate dehydrogenase NAD-linked isocitrate dehydrogenase NAD-specific isocitrate dehydrogenase NAD isocitric dehydrogenase isocitrate dehydrogenase (NAD) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME isocitrate:NAD+ oxidoreductase (decarboxylating) REACTION isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH SUBSTRATE isocitrate NAD+ PRODUCT 2-oxoglutarate CO2 NADH COMMENT The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate, formerly termed threo-D(s)-isocitrate. Does not decarboxylate added oxalosuccinate. PATHWAY PATH: map00020 Citrate cycle (TCA cycle) ORTHOLOG KO: K00030 isocitrate dehydrogenase (NAD+) GENES HSA: 3419(IDH3A) 3420(IDH3B) 3421(IDH3G) MMU: 15929(Idh3g) 67834(Idh3a) RNO: 114096(Idh3a) DME: CG12233-PA(CG12233) CG12233-PB(CG12233) CG5028-PA(CG5028) CG6439-PA(CG6439) CEL: C30F12.7 C37E2.1 F35G12.2 F43G9.1 ATH: At2g17130(F6P23.14) At4g35260(F23E12.180) At4g35650(F8D20.160) At5g03290(F12E4.20) CME: CMS272C CMT412C SCE: YNL037C(IDH1) YOR136W(IDH2) AGO: ADL223W(ADL223Wp) AFR137C(AFR137Cp) CAL: orf19.4826(IDH1) orf19.5791(IDH2) SPO: SPAC11G7.03 SPBC902.05c XFA: XF2596 XFT: PD1973(icdA) XCC: XCC0967(icd) XAC: XAC1046(icd) SON: SO1538 WOL: WD0791 CAC: CAC0972(citC) LIL: LA4067(icd1) LIC: LIC13244(icdA) TEL: tlr0302 GVI: gll3088(icd) DISEASE MIM: 300089 Isocitrate dehydrogenase 3 (NAD+), gamma MIM: 601149 Isocitrate dehydrogenase 3 (NAD+) alpha MIM: 604526 Isocitrate dehydrogenase 3, beta subunit MOTIF PS: PS00470 [NS]-[LIMYT]-[FYDN]-G-[DNGST]-[IMVY]-x-[STGDN]-[DN]- x(2)-[SGAP]-x(3,4)-G-[STG]-[LIVMPA]-G-[LIVMF] REFERENCE 1 Hathaway, J.A. and Atkinson, D.E. The effect of adenylic acid on yeast nicotinamide adenine dinucleotide isocitrate dehydrogenase, a possible metabolic control mechanism. J. Biol. Chem. 238 (1963) 2875-2881. 2 Kornberg, A. and Pricer, W.E. Di- and triphosphopyridine nucleotide isocitric dehydrogenase in yeast. J. Biol. Chem. 189 (1951) 123-136. 3 Plaut, G.W.E. Isocitrate dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 105-126. 4 Plaut, G.W.E. and Sung, S.-C. Diphosphopyridine nucleotide isocitric dehydrogenase from animal tissue. J. Biol. Chem. 207 (1954) 305-314. 5 Ramakrishnan, C.V. and Martin, S.M. Isocitric dehydrogenase in Aspergillus niger. Arch. Biochem. Biophys. 55 (1955) 403-407. 6 Vickery, H.B. A suggested new nomenclature for the isomers of isocitric acid. J. Biol. Chem. 237 (1962) 1739-1741. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.41 ExPASy - ENZYME nomenclature database: 1.1.1.41 ERGO genome analysis and discovery system: 1.1.1.41 BRENDA, the Enzyme Database: 1.1.1.41 CAS: 9001-58-5 /// ENTRY EC 1.1.1.42 NAME isocitrate dehydrogenase (NADP+) oxalosuccinate decarboxylase isocitrate dehydrogenase (NADP) oxalsuccinic decarboxylase isocitrate (NADP) dehydrogenase isocitrate (nicotinamide adenine dinucleotide phosphate) $dehydrogenase NADP-specific isocitrate dehydrogenase NADP-linked isocitrate dehydrogenase NADP-dependent isocitrate dehydrogenase NADP isocitric dehydrogenase isocitrate dehydrogenase (NADP-dependent) NADP-dependent isocitric dehydrogenase NADP+-linked isocitrate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME isocitrate:NADP+ oxidoreductase (decarboxylating) REACTION isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH SUBSTRATE isocitrate NADP+ PRODUCT 2-oxoglutarate CO2 NADPH COMMENT The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate, formerly termed threo-D(s)-isocitrate. Also decarboxylates added oxalosuccinate. PATHWAY PATH: map00020 Citrate cycle (TCA cycle) PATH: map00480 Glutathione metabolism PATH: map00720 Reductive carboxylate cycle (CO2 fixation) ORTHOLOG KO: K00031 isocitrate dehydrogenase GENES HSA: 3417(IDH1) 3418(IDH2) MMU: 15926(Idh1) 269951(Idh2) RNO: 24479(Idh1) DME: CG7176-PA(CG7176) CG7176-PB(CG7176) CG7176-PC(CG7176) CG7176-PD(CG7176) CEL: C34F6.8 F59B8.2 ATH: At1g54340(F20D21.16) At1g65930(F12P19.10) At5g14590(T15N1.80) CME: CMT216C SCE: YDL066W(IDP1) YLR174W(IDP2) YNL009W(IDP3) AGO: AAL022W(AAL022Wp) AER061C(AER061Cp) CAL: orf19.2525(LYS12) orf19.3733(IDP2) orf19.5211(IDP1) SPO: SPAC6G10.08 PFA: PF13_0242 ECO: b1136(icdA) ECJ: JW1122(icdA) ECE: Z1865(icdA) ECS: ECs1608 ECC: c1517(icdA) STY: STY1278(icdA) STT: t1682(icdA) STM: STM1238(icdA) YPE: YPO1641(icdA) YPK: y1802(icdA) YPM: YP1771(icdA) YPS: YPTB2427(icdA) SFL: SF1155(icdA) SFX: S1238(icdA) ECA: ECA2439(icd) PLU: plu2801(icd) PMU: PM1606(idp) XFA: XF2700 XFT: PD2056(icd) XCC: XCC3782(icd) XAC: XAC3835(icd) VCH: VC1141 VVU: VV12118 VVY: VV2325 VPA: VP1011 PPR: PBPRA1149 PAE: PA2623(icd) PA2624(idh) PPU: PP4011(icd) PP4012 PST: PSPTO3356 ACI: ACIAD1187(idh) ACIAD1190(icd) SON: SO2629(icd) CBU: CBU1200(icd) LPN: lpg0816(icd) NME: NMB0920 NMA: NMA1116(icd) CVI: CV3664 RSO: RS01106(icd) BMA: BMA0486(icd) BPS: BPSL0896(icd) BPE: BP2488(icd) BPA: BPP3475(icd) BBR: BB3924(icd) NEU: NE1730(icd) HPY: HP0027(icd) HPJ: jhp0023 HHE: HH1196 WSU: WS1454 CJE: Cj0531(icd) GSU: GSU1465(icd) DVU: DVU0477(icd) BBA: Bd3723(icdA) RPR: RP265(icd) RTY: RT0256(icd) RCO: RC0353(icd) MLO: mll0036 SME: SMc00480(icd) ATU: Atu1870(icdA) ATC: AGR_C_3429 BME: BMEI0791 BMS: BR1199 BJA: blr5747(icdA) RPA: RPA3834(idh) BHE: BH10050(icdA) BQU: BQ07780(icdA) CCR: CC2522 BSU: BG10856(citC) BHA: BH3159(citC) BAN: BA4838(citC) BAR: GBAA4838(citC) BAA: BA_5261 BAT: BAS4487 BCE: BC4593 BCA: BCE4724(citC) BCZ: BTZK4334(citC) BTK: BT9727_4322(citC) BLI: BL00398(icd) OIH: OB2167(citC) SAU: SA1517(citC) SAV: SAV1694(citC) SAM: MW1638(citC) SAR: SAR1773(citC) SAS: SAS1622 SEP: SE1370 LMO: lmo1566(citC) LMF: LMOf2365_1588(icd) LIN: lin1601(citC) LLA: L71075(icd) SMU: SMU.672(idh) TTE: TTE0387(icd) MTU: Rv0066c Rv3339c(icd1) MTC: MT0072 MT3442 MBO: Mb0067c(icd2) Mb3371c(icd1) MLE: ML2672(icd2) MPA: MAP3455c(icd1) MAP3456c(icd2) CGL: NCgl0634(Cgl0664) CEF: CE0682(icd) CDI: DIP0631(icd) SCO: SCO7000(SC8F11.26c) SMA: SAV7214(icdA) LXX: Lxx19490(icd) PAC: PPA1738 BLO: BL1499(icd1) STH: STH2544 RBA: RB1593(icd) PCU: pc1783(icd) LIL: LA4171(icd2) LIC: LIC13328 BTH: BT2071 SYN: slr1289(icd) SYW: SYNW0166(icd) SYC: syc2372_d(icd) GVI: gll3998 ANA: alr1827(icd) PMA: Pro1752(icd) PMM: PMM1596(icd) PMT: PMT1935(icd) CTE: CT0351(icd) DRA: DR1540 DR1674 TTH: TTC1172 AAE: aq_1512(icd) TMA: TM1148 MJA: MJ1596(icd) MAC: MA4265 MMA: MM0642 MM1003 MTH: MTH184 AFU: AF0647(icd) HAL: VNG1873G(icd) HMA: rrnAC3419(icd) TAC: Ta0117 TVO: TVG0201218 PTO: PTO0168 PTO0426 PFU: PF0202 APE: APE0689 SSO: SSO2182(idh) STO: ST2166 PAI: PAE1651 DISEASE MIM: 147650 Isocitrate dehydrogenase, mitochondrial MIM: 147700 Isocitrate dehydrogenase, soluble MOTIF PS: PS00470 [NS]-[LIMYT]-[FYDN]-G-[DNGST]-[IMVY]-x-[STGDN]-[DN]- x(2)-[SGAP]-x(3,4)-G-[STG]-[LIVMPA]-G-[LIVMF] STRUCTURES PDB: 1AI2 1AI3 1BL5 1CW1 1CW4 1CW7 1GRO 1GRP 1HJ6 1HQS 1IDC 1IDD 1IDE 1IDF 1IKA 1ISO 1ITW 1J1W 1LWD 1P8F 1PB1 1PB3 1SJS 1T09 1T0L 3ICD 4ICD 5ICD 6ICD 7ICD 8ICD 9ICD REFERENCE 1 Agosin, M.U. and Weinbach, E.C. Partial purification and characterization of the isocitric dehydrogenase from Trypanosoma cruzi. Biochim. Biophys. Acta 21 (1956) 117-126. 2 Moyle, J. and Dixon, M. Purification of the isocitrate enzyme (triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase). Biochem. J. 63 (1956) 548-552. 3 Plaut, G.W.E. Isocitrate dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 105-126. 4 Siebert, G., Dubuc, J., Warner, R.C. and Plaut, G.W.E. The preparation of isocitrate dehydrogenase from mammalian heart. J. Biol. Chem. 226 (1957) 965-975. 5 Vickery, H.B. A suggested new nomenclature for the isomers of isocitric acid. J. Biol. Chem. 237 (1962) 1739-1741. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.42 ExPASy - ENZYME nomenclature database: 1.1.1.42 ERGO genome analysis and discovery system: 1.1.1.42 BRENDA, the Enzyme Database: 1.1.1.42 CAS: 9028-48-2 /// ENTRY EC 1.1.1.43 NAME phosphogluconate 2-dehydrogenase 6-phosphogluconic dehydrogenase phosphogluconate dehydrogenase gluconate 6-phosphate dehydrogenase 6-phosphogluconate dehydrogenase (NAD) 2-keto-6-phosphogluconate reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 6-phospho-D-gluconate:NAD(P)+ 2-oxidoreductase REACTION 6-phospho-D-gluconate + NAD(P)+ = 6-phospho-2-dehydro-D-gluconate + NAD(P)H + H+ SUBSTRATE 6-phospho-D-gluconate NAD+ NADP+ PRODUCT 6-phospho-2-dehydro-D-gluconate NADH NADPH H+ PATHWAY PATH: map00030 Pentose phosphate pathway PATH: map00480 Glutathione metabolism ORTHOLOG KO: K00032 phosphogluconate 2-dehydrogenase REFERENCE 1 Frampton, E.W. and Wood, W.A. Carbohydrate oxidation by Pseudomonas fluorescens. VI. Conversion of 2-keto-6-phosphogluconate to pyruvate. J. Biol. Chem. 236 (1961) 2571-2577. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.43 ExPASy - ENZYME nomenclature database: 1.1.1.43 ERGO genome analysis and discovery system: 1.1.1.43 BRENDA, the Enzyme Database: 1.1.1.43 CAS: 9001-82-5 /// ENTRY EC 1.1.1.44 NAME phosphogluconate dehydrogenase (decarboxylating) phosphogluconic acid dehydrogenase 6-phosphogluconic dehydrogenase 6-phosphogluconic carboxylase 6-phosphogluconate dehydrogenase (decarboxylating) 6-phospho-D-gluconate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating) REACTION 6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH SUBSTRATE 6-phospho-D-gluconate NADP+ PRODUCT D-ribulose 5-phosphate CO2 NADPH COMMENT Certain preparations reduce NAD+ as well as NADP+. PATHWAY PATH: map00030 Pentose phosphate pathway ORTHOLOG KO: K00033 6-phosphogluconate dehydrogenase GENES HSA: 5226(PGD) MMU: 110208(Pgd) DME: CG3724-PA(CG3724) CEL: T25B9.9 ATH: At1g64190(F22C12.5) At3g02360(F11A12.5) At5g41670(MBK23.20) CME: CML036C CML059C CMM231C CMS195C CMX012C SCE: YGR256W(GND2) YHR183W(GND1) AGO: AFR129W(AFR129Wp) CAL: orf19.5024(GND1) SPO: SPBC660.16 ECU: ECU05_0860 PFA: PF14_0520 ECO: b2029(gnd) ECJ: JW2011(gnd) ECE: Z3191(gnd) ECS: ECs2830 ECC: c2556(gnd) STY: STY2290(gnd) STT: t0792(gnd) STM: STM2081(gnd) YPE: YPO1541(gnd) YPK: y2629(gnd) YPM: YP1430(gnd) YPS: YPTB1553(gnd) SFL: SF2091(gnd) SFX: S2212(gnd) ECA: ECA1444(gnd) PLU: plu1560(gnd) BUC: BU107(gnd) BAS: BUsg100(gnd) BAB: bbp101(gnd) BFL: Bfl470(gnd) HIN: HI0553(gnd) HDU: HD0833(gnd) PMU: PM1554(gnd) MSU: MS0013(gnd) XCC: XCC3439(gndA) XAC: XAC0680(gndA) VCH: VCA0898 VVU: VV12682 VVY: VV1607 VPA: VP1708 PPR: PBPRA1444(gnd) PPU: PP4043(gnd) PST: PSPTO3122(gnd) SON: SO1902(gnd) MCA: MCA1950(gnd) NME: NMB0015 NMA: NMA0262(gnd) BMA: BMAA0420(gnd) BPS: BPSS1749(gnd) NEU: NE0397 MLO: mll3321 mlr4206 SME: SMc04262(gnd) ATU: Atu1526(gnd) Atu4834 ATC: AGR_C_2814 AGR_L_99 BME: BMEII1124 BMS: BRA0111(gnd) BJA: blr6759 RPA: RPA3635(gnd) BSU: BG10651(gntZ) BG11631(yqeC) BG11738(yqjI) BHA: BH2674 BAN: BA0164(yqjI) BA3431 BAR: GBAA0164(yqjI) GBAA3431 BAA: BA_0746 BA_3929 BAT: BAS0166 BAS3180 BCE: BC2225 BC3372 BCA: BCE2304(gnd) BCE3410 BCZ: BTZK0157(gnd) BTZK3081(gnd) BTK: BT9727_0159(gntZ) BT9727_3164(gnd) BLI: BL00198(gntZ) BL01383(yqjI) BLD: BLi04289(gntZ) OIH: OB0185 OB3187(gntZ) SAU: SA1342(gnd) SAV: SAV1511(gnd) SAM: MW1464(gnd) SAR: SAR1589(gnd) SAS: SAS1450 SEP: SE1192 LMO: lmo1376 LMF: LMOf2365_1395(gnd) LIN: lin1413 LLA: L0046(gnd) L53699(gntZ) SPN: SP0375 SPR: spr0335(gnd) LPL: lp_1251(gnd1) lp_1541(gnd2) LJO: LJ1852 EFA: EF1049(gnd) EF3142 CTC: CTC01865 TTE: TTE0195(gnd) TTE1941(gnd2) MTU: Rv1122(gnd2) Rv1844c(gnd) MTC: MT1154 MT1892 MBO: Mb1153(gnd2) Mb1875c(gnd1) MLE: ML2065(gnd) MPA: MAP1557c(gnd) MAP2670c(gnd2) CGL: NCgl1396(Cgl1452) CEF: CE1588 CDI: DIP1213(gnd) SCO: SCO0975(SCBAC19F3.02) SCO3877(SCH18.14c) SCO6658(SC5A7.08c) SMA: SAV1771(gnd1) SAV4318(gnd2) SAV7249(gnd3) TWH: TW492(gnd) TWS: TW272(gnd) LXX: Lxx00030(gnd) Lxx17380(gnd) PAC: PPA1629 BLO: BL0444(gnt) RBA: RB2817(6pgD) CTR: CT063(gnd) CMU: TC0333 CPN: CPn0360 CPA: CP0398 CPJ: CPj0360(gnd) CPT: CpB0369 CCA: CCA00432(gnd) PCU: pc0317(pgd) BBU: BB0561(gnd) TPA: TP0331 BTH: BT1222 SYN: sll0329(gnd) SYW: SYNW1119(gnd) SYC: syc1460_c(gnd) TEL: tlr0576 GVI: gll1117 ANA: alr5275 PMA: Pro0843(gnd) PMM: PMM0770(gnd) PMT: PMT0565(gnd) CTE: CT1874 DRA: DR1595 AAE: aq_498(gnd) TMA: TM0438 HMA: rrnAC2180(gnd) DISEASE MIM: 172200 6-phosphogluconate dehydrogenase MOTIF PS: PS00461 [LIVM]-x-D-x(2)-[GA]-[NQS]-K-G-T-G-x-W STRUCTURES PDB: 1PGJ 1PGN 1PGO 1PGP 1PGQ 2PGD REFERENCE 1 Dickens, F. and Glock, G.E. Direct oxidation of glucose-6-phosphate, 6-phosphogluconate and pentose-5-phosphate by enzymes of animal origin. Biochem. J. 50 (1951) 81-95. 2 Pontremoli, S., de Flora, A., Grazi, E., Mangiarotti, G., Bonsignore, A. and Horecker, B.L. Purification and properties of beta-L-hydroxy acid dehydrogenase. II. Isolation of beta-keto-L-gluconic acid, an intermediate in L-xylulose biosynthesis. J. Biol. Chem. 236 (1961) 2975-2980. 3 Scott, D.B.M. and Cohen, S.S. The oxidative pathway of carbohydrate metabolism in Escherichia coli. 1. The isolation and properties of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Biochem. J. 55 (1953) 23-33. 4 Scott, D.B.M. and Cohen, S.S. The oxidative pathway of carbohydrate metabolism in Escherichia coli. 5. Isolation and identification of ribulose phosphate produced from 6-phosphogluconate by the dehydrogenase of E. coli. Biochem. J. 65 (1957) 686-689. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.44 ExPASy - ENZYME nomenclature database: 1.1.1.44 ERGO genome analysis and discovery system: 1.1.1.44 BRENDA, the Enzyme Database: 1.1.1.44 CAS: 9073-95-4 /// ENTRY EC 1.1.1.45 NAME L-gulonate 3-dehydrogenase L-3-aldonate dehydrogenase L-3-aldonic dehydrogenase L-gulonic acid dehydrogenase L-beta-hydroxyacid dehydrogenase L-beta-hydroxy-acid-NAD-oxidoreductase L-3-hydroxyacid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-gulonate:NAD+ 3-oxidoreductase REACTION L-gulonate + NAD+ = 3-dehydro-L-gulonate + NADH + H+ SUBSTRATE L-gulonate NAD+ PRODUCT 3-dehydro-L-gulonate NADH H+ COMMENT Also oxidizes other L-3-hydroxyacids. PATHWAY PATH: map00040 Pentose and glucuronate interconversions REFERENCE 1 Dworsky, P. and Hoffmann-Ostenhof, O. L-3-Aldonic acid dehydrogenase from Schwanniomyces occidentalis. Acta Biochim. Pol. 11 (1964) 269-277. 2 Smiley, J.D. and Ashwell, G. Purification and properties of beta-L-hydroxy acid dehydrogenase. II. Isolation of beta-keto-L-gluconic acid, an intermediate in L-xylulose biosynthesis. J. Biol. Chem. 236 (1961) 357-364. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.45 ExPASy - ENZYME nomenclature database: 1.1.1.45 ERGO genome analysis and discovery system: 1.1.1.45 BRENDA, the Enzyme Database: 1.1.1.45 CAS: 9028-51-7 /// ENTRY EC 1.1.1.46 NAME L-arabinose 1-dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-arabinose:NAD+ 1-oxidoreductase REACTION L-arabinose + NAD+ = L-arabinono-1,4-lactone + NADH + H+ SUBSTRATE L-arabinose NAD+ PRODUCT L-arabinono-1,4-lactone NADH H+ PATHWAY PATH: map00053 Ascorbate and aldarate metabolism REFERENCE 1 Weimberg, R. and Doudoroff, M. The oxidation of L-arabinose by Pseudomonas saccharophila. J. Biol. Chem. 217 (1955) 607-624. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.46 ExPASy - ENZYME nomenclature database: 1.1.1.46 ERGO genome analysis and discovery system: 1.1.1.46 BRENDA, the Enzyme Database: 1.1.1.46 CAS: 9028-52-8 /// ENTRY EC 1.1.1.47 NAME glucose 1-dehydrogenase D-glucose dehydrogenase (NAD(P)) hexose phosphate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME beta-D-glucose:NAD(P)+ 1-oxidoreductase REACTION beta-D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+ SUBSTRATE beta-D-glucose NAD+ NADP+ PRODUCT D-glucono-1,5-lactone NADH NADPH H+ COMMENT Also oxidizes D-xylose. PATHWAY PATH: map00030 Pentose phosphate pathway ORTHOLOG KO: K00034 glucose 1-dehydrogenase GENES HSA: 9563(H6PD) CAL: orf19.2899(SPS23) orf19.320 PST: PSPTO2492 BMA: BMA1859 BME: BMEI0861 BMS: BR1122 BJA: bll7157 bll7185(gdh) BSU: BG10545(gdh) BG12761(ycdF) BAN: BA4968(gdH) BAR: GBAA4968(gdH) BAA: BA_5386 BAT: BAS4612 BCE: BC3460 BC4715 BCA: BCE4858(gdH) BCZ: BTZK4466(gdh) BTK: BT9727_4448(gdh) BLI: BL01382(gdh) BL01687 OIH: OB3183 SEP: SE1830 EFA: EF2382(gdh) CGL: NCgl0689(Cgl0719) SMA: SAV1922(gdh) RBA: RB10002(gcd) RB7294(gdh) SYN: sll1709(gdh) GVI: gll1114 gll1167 ANA: all3836 HMA: rrnAC0011(ywfD1) rrnAC2741(ywfD2) TAC: Ta0897 TVO: TVG1073292 PTO: PTO0230 PTO0639 PTO1070 PFU: PF1853 SSO: SSO3003(dhg-1) SSO3042(dhg-2) SSO3204(dhg-3) STO: ST1704 MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] PS: PS00069 D-H-Y-L-G-K-[EQK] STRUCTURES PDB: 1G6K 1GCO 1GEE 1RWB REFERENCE 1 [PMID:810982] Banauch, D., Brummer, W., Ebeling, W., Metz, H., Rindfrey, H., Lang, H., Leybold, K. and Rick, W. A glucose dehydrogenase for the determination of glucose concentrations in body fluids. Z. Klin. Chem. Klin. Biochem. 13 (1975) 101-107. 2 Brink, N.G. Beef liver glucose dehydrogenase. 1. Purification and properties. Acta Chem. Scand. 7 (1953) 1081-1089. 3 Pauly, H.E. and Pfleiderer, G. D-Glucose dehydrogenase from Bacillus megaterium M 1286: purification, properties and structure. Hoppe-Seyler's Z. Physiol. Chem. 356 (1976) 1613-1623. 4 Strecker, H.J. and Korkes, S. Glucose dehydrogenase. J. Biol. Chem. 196 (1952) 769-784. 5 [PMID:4392298] Thompson, R.E. and Carper, W.R. Glucose dehydrogenase from pig liver. I. Isolation and purification. Biochim. Biophys. Acta 198 (1970) 397-406. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.47 ExPASy - ENZYME nomenclature database: 1.1.1.47 ERGO genome analysis and discovery system: 1.1.1.47 BRENDA, the Enzyme Database: 1.1.1.47 CAS: 9028-53-9 /// ENTRY EC 1.1.1.48 NAME galactose 1-dehydrogenase D-galactose dehydrogenase beta-galactose dehydrogenase NAD-dependent D-galactose dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-galactose:NAD+ 1-oxidoreductase REACTION D-galactose + NAD+ = D-galactono-1,4-lactone + NADH + H+ SUBSTRATE D-galactose NAD+ PRODUCT D-galactono-1,4-lactone NADH H+ PATHWAY PATH: map00052 Galactose metabolism ORTHOLOG KO: K00035 D-galactose 1-dehydrogenase GENES XCC: XCC0744(dgd) XAC: XAC0797(dgd) PST: PSPTO4782(gal) MLO: mll0280 SME: SMc00588(gal) ATU: Atu1113 ATC: AGR_C_2059 BME: BMEII0355 BMS: BRA0941 BJA: blr3205 CCR: CC0967 REFERENCE 1 De Ley, J. and Doudoroff, M. The metabolism of D-galactose in Pseudomonas saccharophila. J. Biol. Chem. 227 (1957) 745-757. 2 Hu, A.S.L. and Cline, A.L. The regulation of some sugar dehydrogenases in a pseudomonad. Biochim. Biophys. Acta 93 (1964) 237-245. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.48 ExPASy - ENZYME nomenclature database: 1.1.1.48 ERGO genome analysis and discovery system: 1.1.1.48 BRENDA, the Enzyme Database: 1.1.1.48 CAS: 9028-54-0 /// ENTRY EC 1.1.1.49 NAME glucose-6-phosphate 1-dehydrogenase NADP-glucose-6-phosphate dehydrogenase Zwischenferment D-glucose 6-phosphate dehydrogenase glucose 6-phosphate dehydrogenase (NADP) NADP-dependent glucose 6-phosphate dehydrogenase 6-phosphoglucose dehydrogenase Entner-Doudoroff enzyme CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-glucose-6-phosphate:NADP+ 1-oxidoreductase REACTION D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate + NADPH + H+ SUBSTRATE D-glucose 6-phosphate NADP+ PRODUCT D-glucono-1,5-lactone 6-phosphate NADPH H+ COMMENT Also acts slowly on beta-D-glucose and other sugars. Certain preparations reduce NAD+ as well as NADP+. PATHWAY PATH: map00030 Pentose phosphate pathway PATH: map00480 Glutathione metabolism ORTHOLOG KO: K00036 glucose-6-phosphate 1-dehydrogenase GENES HSA: 2539(G6PD) MMU: 14380(G6pd2) 14381(G6pdx) RNO: 24377(G6pdx) DME: CG12529-PA(CG12529) CG12529-PB(CG12529) CG7140-PA(CG7140) CEL: B0035.5 ATH: At1g09420(F14J9.8) At1g24280(F3I6.22) At3g27300(K17E12.12) At5g13110(T19L5.70) At5g35790(MWP19.3) At5g40760(MNF13.6) CME: CMI224C CMR014C SCE: YNL241C(ZWF1) AGO: ABL206C(ABL206Cp) CAL: orf19.1355(SOL1) orf19.4754(ZWF1) SPO: SPAC3C7.13c SPAC9.01 SPCC794.01c ECU: ECU08_1850 PFA: PF14_0511 ECO: b1852(zwf) ECJ: JW1841(zwf) ECE: Z2904(zwf) ECS: ECs2562 ECC: c2265(zwf) STY: STY2094(zwf) STT: t0991(zwf) STM: STM1886(zwf) YPE: YPO2066(zwf) YPK: y2244(zwf) YPM: YP1909(zwf) YPS: YPTB2049(zwf) SFX: S1928(zwf) ECA: ECA2479(zwf) PLU: plu2122(zwf) BUC: BU320(zwf) BAS: BUsg312(zwf) BAB: bbp298(zwf) BFL: Bfl449(zwf) HIN: HI0558(zwf) HDU: HD0838(zwf) PMU: PM1549(zwf) MSU: MS0016(zwf) XFA: XF1065 XFT: PD0346(zwf) XCC: XCC2136(zwf) XCC3993(zwf) XAC: XAC2071(zwf) XAC4081(zwf) VCH: VCA0896 VVU: VV12684 VVY: VV1605 VPA: VP1710 PPR: PBPRA1442 PAE: PA3183(zwf) PA5439 PPU: PP1022(zwf-1) PP4042(zwf-2) PP5351(zwf-3) PST: PSPTO1300(zwf-1) PSPTO3121(zwf-2) SON: SO2489(zwf) LPN: lpg0416(zwf) MCA: MCA0025(zwf-1) MCA2971(zwf-2) NME: NMB1392 NMA: NMA1609(zwf) CVI: CV0145(zwf) RSO: RS02115(zwf) BMA: BMA2130(zwf) BPS: BPSL2612(zwf) NEU: NE0398(zwf) HPY: HP1101(zwf) HPJ: jhp1027 MLO: mll6516 mlr4207 SME: SMc03070(zwf) ATU: Atu0600(zwf) Atu4835 ATC: AGR_C_1065 AGR_L_98 BME: BMEII0513 BMS: BRA0778(zwf) BJA: blr6760(zwf) RPA: RPA3636(zwf) BHE: BH03910(zwf) BQU: BQ02930(zwf) CCR: CC2057 BSU: BG11739(zwf) BAN: BA3433(zwf) BAR: GBAA3433(zwf) BAA: BA_3931 BAT: BAS3182 BCA: BCE3412(zwf) BCZ: BTZK3083(zwf) BTZK3084(g6pD) BTK: BT9727_3166(zwf) BLI: BL01964(zwf) OIH: OB2938 SAU: SA1336 SAV: SAV1505 SAM: MW1459 SAR: SAR1582(zwf) SAS: SAS1445 SEP: SE1188 LMO: lmo1978 LMF: LMOf2365_2002(zwf) LIN: lin2085 LLA: L0044(zwf) SPN: SP1243 SPR: spr1122(zwf) LPL: lp_2681(gpd) LJO: LJ0470 EFA: EF1004(zwf) CTC: CTC01864 TTE: TTE1005(zwf) MTU: Rv1121(zwf) Rv1447c(zwf2) MTC: MT1153 MT1494 MBO: Mb1152(zwf1) Mb1482c(zwf2) MPA: MAP1176c(zwf2) MAP2671c(zwf) CGL: NCgl1514(Cgl1576) CEF: CE1696 CDI: DIP1304(zwf) SCO: SCO1937(SCC22.19) SCO6661(SC5A7.11c) SMA: SAV1768(zwf1) SAV6313(zwf2) TWH: TW343(zwf) TWS: TW428(zwf) LXX: Lxx11590(zwf) PAC: PPA1563 BLO: BL0440(zwf2) RBA: RB2735(g6pD) CTR: CT185(zwf) CMU: TC0457 CPN: CPn0238 CPA: CP0524 CPJ: CPj0238(zwf) CPT: CpB0244 CCA: CCA00540(zwf) PCU: pc0821(zwf) BBU: BB0636(zwf) TPA: TP0478 BTH: BT1221 SYN: slr1843(zwf) SYW: SYNW0750(zwf) SYC: syc1768_d(zwf) TEL: tll0540(zwf) GVI: gll1170(zwf) glr3178(zwf) ANA: all4019(zwf) PMA: Pro1124(zwf) PMM: PMM1074(zwf) PMT: PMT1102(zwf) CTE: CT1873(zwf) DRA: DR1596 AAE: aq_497(gsdA) TMA: TM1155 DISEASE MIM: 305900 Glucose-6-phosphate dehydrogenase MOTIF PS: PS00069 D-H-Y-L-G-K-[EQK] STRUCTURES PDB: 1DPG 1E77 1E7M 1E7Y 1H93 1H94 1H9A 1H9B 1QKI 2DPG REFERENCE 1 [PMID:5363983] Engel, H.J., Domschke, W., Alberti, M. and Domagk, G.F. Protein structure and enzymatic activity. II. Purification and properties of a crystalline glucose-6-phosphate dehydrogenase from Candida utilis. Biochim. Biophys. Acta 191 (1969) 509-516. 2 Glaser, L. and Brown, D.H. Purification and properties of D-glucose-6-phosphate dehydrogenase. J. Biol. Chem. 216 (1955) 67-79. 3 Julian, G.R., Wolfe, R.G. and Reithel, F.J. The enzymes of mammary gland. II. The preparation of glucose 6-phosphate dehydrogenase. J. Biol. Chem. 236 (1961) 754-758. 4 Noltmann, E.A., Gubler, C.J. and Kuby, S.A. Glucose 6-phosphate dehydrogenase (Zwischenferment). I. Isolation of the crystalline enzyme from yeast. J. Biol. Chem. 236 (1961) 1225-1230. 5 [PMID:11457850] Miclet, E., Stoven, V., Michels, P.A., Opperdoes, F.R., Lallemand, J.-Y. and Duffieux, F. NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase. J. Biol. Chem. 276 (2001) 34840-34846. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.49 ExPASy - ENZYME nomenclature database: 1.1.1.49 ERGO genome analysis and discovery system: 1.1.1.49 BRENDA, the Enzyme Database: 1.1.1.49 CAS: 9001-40-5 /// ENTRY EC 1.1.1.50 NAME 3alpha-hydroxysteroid dehydrogenase (B-specific) hydroxyprostaglandin dehydrogenase 3alpha-hydroxysteroid oxidoreductase sterognost 3alpha CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3alpha-hydroxysteroid:NAD(P)+ oxidoreductase (B-specific) REACTION androsterone + NAD(P)+ = 5alpha-androstane-3,17-dione + NAD(P)H + H+ SUBSTRATE androsterone NAD+ NADP+ PRODUCT 5alpha-androstane-3,17-dione NADH NADPH H+ COMMENT Also acts on other 3alpha-hydroxysteroids and on 9-, 11- and 15-hydroxyprostaglandin. B-specific with respect to NAD+ or NADP+. PATHWAY PATH: map00120 Bile acid biosynthesis PATH: map00140 C21-Steroid hormone metabolism PATH: map00150 Androgen and estrogen metabolism ORTHOLOG KO: K00037 3-alpha-hydroxysteroid dehydrogenase GENES HSA: 1109(AKR1C4) RSO: RS05193 MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] PS: PS00062 [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY] PS: PS00063 [LIVM]-[PAIV]-[KR]-[ST]-x(4)-R-x(2)-[GSTAEQK]-[NSL]- x(2)-[LIVMFA] PS: PS00798 G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGC]-[AS]-x(5)-E-x(2)- [LIVM]-G STRUCTURES PDB: 1AFS 1FJH 1FK8 1LWI 1RAL REFERENCE 1 Jarabak, J. and Talalay, P. Stereospecificity of hydrogen transfer by pyridine nucleotide-linked hydroxysteroid hydrogenase. J. Biol. Chem. 235 (1960) 2147-2151. 2 Kochakian, C.D., Carroll, B.R. and Uhri, B. Comparison of the oxidation of C19-hydroxy steroids by guinea pig liver homogenate. J. Biol. Chem. 224 (1957) 811-818. 3 Marcus, P.I. and Talalay, P. Induction and purification of alpha- and beta-hydroxysteroid dehydrogenases. J. Biol. Chem. 218 (1956) 661-674. 4 [PMID:3479982] Penning, T.M. and Sharp, R.B. Prostaglandin dehydrogenase activity of purified rat liver 3 alpha-hydroxysteroid dehydrogenase. Biochem. Biophys. Res. Commun. 148 (1987) 646-652. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.50 ExPASy - ENZYME nomenclature database: 1.1.1.50 ERGO genome analysis and discovery system: 1.1.1.50 BRENDA, the Enzyme Database: 1.1.1.50 CAS: 9028-56-2 /// ENTRY EC 1.1.1.51 NAME 3(or 17)beta-hydroxysteroid dehydrogenase beta-hydroxy steroid dehydrogenase 17-ketoreductase 17beta-hydroxy steroid dehydrogenase 3beta-hydroxysteroid dehydrogenase 3beta-hydroxy steroid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3(or 17)beta-hydroxysteroid:NAD(P)+ oxidoreductase REACTION testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H + H+ SUBSTRATE testosterone NAD+ NADP+ PRODUCT androst-4-ene-3,17-dione NADH NADPH H+ COMMENT Also acts on other 3beta- or 17beta-hydroxysteroids. cf. EC 1.1.1.209 3(or 17)alpha-hydroxysteroid dehydrogenase. PATHWAY PATH: map00150 Androgen and estrogen metabolism ORTHOLOG KO: K05296 3(or 17)beta-hydroxysteroid dehydrogenase GENES CAL: orf19.6167(AYR1) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] STRUCTURES PDB: 1HXH REFERENCE 1 Dahm, K. and Breuer, H. Anreicherung einer 17beta-hydroxysteroid:NAD(P)-oxydoreduktase aus der Nebenniere der Ratte. Hoppe-Seyler's Z. Physiol. Chem. 336 (1964) 63-68. 2 Lynn, W.S. and Brown, R.H. The conversion of progesterone to androgens by testes. J. Biol. Chem. 232 (1958) 1015-1030. 3 Marcus, P.I. and Talalay, P. Induction and purification of alpha- and beta-hydroxysteroid dehydrogenases. J. Biol. Chem. 218 (1956) 661-674. 4 [PMID:193845] Schultz, R.M., Groman, F.V. and Engel, L.L. 3(17)beta-Hydroxysteroid dehydrogenase of Pseudomonas testosteroni. A convenient purification and demonstration of multiple molecular forms. J. Biol. Chem. 252 (1977) 3775-3783. 5 Talalay, P. and Dobson, M.M. Purification and properties of a alpha-hydroxysteroid dehydrogenase. J. Biol. Chem. 205 (1953) 823-837. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.51 ExPASy - ENZYME nomenclature database: 1.1.1.51 ERGO genome analysis and discovery system: 1.1.1.51 BRENDA, the Enzyme Database: 1.1.1.51 CAS: 9015-81-0 /// ENTRY EC 1.1.1.52 NAME 3alpha-hydroxycholanate dehydrogenase alpha-hydroxy-cholanate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3alpha-hydroxy-5beta-cholanate:NAD+ oxidoreductase REACTION 3alpha-hydroxy-5beta-cholanate + NAD+ = 3-oxo-5beta-cholanate + NADH + H+ SUBSTRATE 3alpha-hydroxy-5beta-cholanate NAD+ PRODUCT 3-oxo-5beta-cholanate NADH H+ COMMENT Also acts on other 3alpha-hydroxysteroids with an acidic side-chain. STRUCTURES PDB: 1IHI REFERENCE 1 Hayaishi, O., Saito, Y., Jakoby, W.B. and Stohlman, E.F. Reversible enzymatic oxidation of bile acids. Arch. Biochem. Biophys. 56 (1955) 554-555. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.52 ExPASy - ENZYME nomenclature database: 1.1.1.52 ERGO genome analysis and discovery system: 1.1.1.52 BRENDA, the Enzyme Database: 1.1.1.52 CAS: 9028-57-3 /// ENTRY EC 1.1.1.53 NAME 3alpha(or 20beta)-hydroxysteroid dehydrogenase cortisone reductase (R)-20-hydroxysteroid dehydrogenase dehydrogenase, 20beta-hydroxy steroid delta4-3-ketosteroid hydrogenase 20beta-hydroxysteroid dehydrogenase 3alpha,20beta-hydroxysteroid:NAD+-oxidoreductase NADH-20beta-hydroxysteroid dehydrogenase 20beta-HSD CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3alpha(or 20beta)-hydroxysteroid:NAD+ oxidoreductase REACTION androstan-3alpha,17beta-diol + NAD+ = 17beta-hydroxyandrostan-3-one + NADH + H+ SUBSTRATE androstan-3alpha,17beta-diol NAD+ PRODUCT 17beta-hydroxyandrostan-3-one NADH H+ COMMENT The 3alpha-hydroxy group or 20beta-hydroxy group of pregnane and androstane steroids can act as donor. PATHWAY PATH: map00120 Bile acid biosynthesis PATH: map00140 C21-Steroid hormone metabolism ORTHOLOG KO: K00038 3alpha(or 20beta)-hydroxysteroid dehydrogenase GENES OIH: OB0329 MBO: Mb2025(fabG3) MPA: MAP1739c(fabG3_1) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] STRUCTURES PDB: 1HDC 1N5D 1NFF 1NFQ 1NFR 2HSD REFERENCE 1 [PMID:718844] Edwards, C.A.F. and Orr, J.C. Comparison of the 3alpha-and 20beta-hydroxysteroid dehydrogenase activities of the cortisone reductase of Streptomyces hydrogenans. Biochemistry 17 (1978) 4370-4376. 2 Hubener, H.J. and Sahrholz, F.G. 20beta-hydroxy-steroid-dehydrogenase. II. Darstellung und Kristallisation. Biochem. Z. 333 (1960) 95-105. 3 Hubener, H.J., Sahrholz, F.G., Schmidt-Thome, J., Nesemann, G. and Junk, R. 20beta-Hydroxy-Steroid-Dehydrogenase, ein neues kristallines Enzym. Biochim. Biophys. Acta 35 (1959) 270-272. 4 Lynn, W.S. and Brown, R.H. The conversion of progesterone to androgens by testes. J. Biol. Chem. 232 (1958) 1015-1030. 5 [PMID:6936053] Strickler, R.C., Covey, D.F. and Tobias, B. Study of 3alpha, 20 beta-hydroxysteroid dehydrogenase with an enzyme-generated affinity alkylator: dual enzyme activity at a single active site. Biochemistry 19 (1980) 4950-4954. 6 [PMID:6928375] Sweet, F. and Samant, B.S. Bifunctional enzyme activity at the same active site: study of 3alpha and 20beta activity by affinity alkylation of 3alpha, 20beta-hydroxysteroid dehydrogenase with 17-(bromoacetoxy)steroids. Biochemistry 19 (1980) 978-986. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.53 ExPASy - ENZYME nomenclature database: 1.1.1.53 ERGO genome analysis and discovery system: 1.1.1.53 BRENDA, the Enzyme Database: 1.1.1.53 CAS: 9028-42-6 /// ENTRY EC 1.1.1.54 NAME allyl-alcohol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME allyl-alcohol:NADP+ oxidoreductase REACTION allyl alcohol + NADP+ = acrolein + NADPH + H+ SUBSTRATE allyl alcohol NADP+ PRODUCT acrolein NADPH H+ COMMENT Also acts on saturated primary alcohols. REFERENCE 1 Otsuka, K. Triphosphopyridine nucleotide-allyl and -ethyl alcohol dehydrogenases from Escherichia coli. J. Gen. Appl. Microbiol. 4 (1958) 211-215. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.54 ExPASy - ENZYME nomenclature database: 1.1.1.54 ERGO genome analysis and discovery system: 1.1.1.54 BRENDA, the Enzyme Database: 1.1.1.54 CAS: 9028-58-4 /// ENTRY EC 1.1.1.55 NAME lactaldehyde reductase (NADPH) lactaldehyde (reduced nicotinamide adenine dinucleotide phosphate) $reductase NADP-1,2-propanediol dehydrogenase propanediol dehydrogenase 1,2-propanediol:NADP+ oxidoreductase lactaldehyde reductase (NADPH2) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME propane-1,2-diol:NADP+ oxidoreductase REACTION propane-1,2-diol + NADP+ = L-lactaldehyde + NADPH + H+ SUBSTRATE propane-1,2-diol NADP+ PRODUCT L-lactaldehyde NADPH H+ COMMENT May be identical with EC 1.1.1.2 alcohol dehydrogenase (NADP+). REFERENCE 1 Gupta, N.K. and Robinson, W.G. The enzymatic conversion of lactaldehyde to propanediol. J. Biol. Chem. 235 (1960) 1609-1612. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.55 ExPASy - ENZYME nomenclature database: 1.1.1.55 ERGO genome analysis and discovery system: 1.1.1.55 BRENDA, the Enzyme Database: 1.1.1.55 CAS: 9028-43-7 /// ENTRY EC 1.1.1.56 NAME ribitol 2-dehydrogenase adonitol dehydrogenase ribitol dehydrogenase A (wild type) ribitol dehydrogenase B (mutant enzyme with different properties) ribitol dehydrogenase D (mutant enzyme with different properties) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME ribitol:NAD+ 2-oxidoreductase REACTION ribitol + NAD+ = D-ribulose + NADH + H+ SUBSTRATE ribitol NAD+ PRODUCT D-ribulose NADH H+ PATHWAY PATH: map00040 Pentose and glucuronate interconversions ORTHOLOG KO: K00039 ribitol 2-dehydrogenase GENES CAL: orf19.4633 orf19.5615(AYR1) orf19.6131(TSC10) ATU: Atu4323(rdh) ATC: AGR_L_1076 BME: BMEII0980 BMS: BRA0268 BJA: bll6662(rdh) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] REFERENCE 1 Hollmann, S. and Touster, O. The L-xylulose-xylitol enzyme and other polyol dehydrogenases of guinea pig liver mitochondria. J. Biol. Chem. 225 (1957) 87-102. 2 Nordlie, R.C. and Fromm, H.J. Ribitol dehydrogenase. II. Studies on the reaction mechanism. J. Biol. Chem. 234 (1959) 2523-2531. 3 Wood, W.A., McDonough, M.J. and Jacobs, L.B. Ribitol and D-arabitol utilization by Aerobacter aerogenes. J. Biol. Chem. 236 (1961) 2190-2195. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.56 ExPASy - ENZYME nomenclature database: 1.1.1.56 ERGO genome analysis and discovery system: 1.1.1.56 BRENDA, the Enzyme Database: 1.1.1.56 CAS: 9014-23-7 /// ENTRY EC 1.1.1.57 NAME fructuronate reductase mannonate oxidoreductase mannonic dehydrogenase D-mannonate dehydrogenase D-mannonate:NAD oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-mannonate:NAD+ 5-oxidoreductase REACTION D-mannonate + NAD+ = D-fructuronate + NADH + H+ SUBSTRATE D-mannonate NAD+ PRODUCT D-fructuronate NADH H+ COMMENT Also reduces D-tagaturonate. PATHWAY PATH: map00040 Pentose and glucuronate interconversions ORTHOLOG KO: K00040 fructuronate reductase GENES ECO: b4323(uxuB) ECJ: JW4286(uxuB) ECE: Z5921(uxuB) ECS: ECs5282 ECC: c5403(uxuB) STY: STY1553 STY3307(uxuB) STT: t3057(uxuB) STM: STM1508(ydfI) STM3136 YPE: YPO1280 YPK: y2903 YPM: YP1309(mtlD1) YPS: YPTB1314 SFL: SF4197(uxuB) SFX: S4453(uxuB) ECA: ECA0819(uxuB) PLU: plu0175(uxuB) XAC: XAC4232(mtlD) VVU: VV21069 VVY: VVA1593 VPA: VPA1705 PPR: PBPRB1880 SME: SMb20749(uxuB) ATU: Atu3530(uxuB) ATC: AGR_L_2604 BME: BMEII0478 BJA: blr6836(uxuB) LLA: L0241(uxuB) CEF: CE2378 RBA: RB2403(uxuB) TMA: TM0068 MOTIF PS: PS00974 [LIVMY]-x-[FS]-x(2)-[STAGCV]-x-V-D-R-[IV]-x-[PS] REFERENCE 1 Hickman, J. and Ashwell, G. Uronic acid metabolism in bacteria. II. Purification and properties of D-altronic acid and D-mannonic acid dehyrogenases in Escherichia coli. J. Biol. Chem. 235 (1960) 1566-1570. 2 Kilgore, W.W. and Starr, M.P. Catabolism of galacturonic and glucuronic acids by Erwinia carotovora. J. Biol. Chem. 234 (1959) 2227-2235. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.57 ExPASy - ENZYME nomenclature database: 1.1.1.57 ERGO genome analysis and discovery system: 1.1.1.57 BRENDA, the Enzyme Database: 1.1.1.57 CAS: 9028-44-8 /// ENTRY EC 1.1.1.58 NAME tagaturonate reductase altronic oxidoreductase altronate oxidoreductase TagUAR altronate dehydrogenase D-tagaturonate reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-altronate:NAD+ 3-oxidoreductase REACTION D-altronate + NAD+ = D-tagaturonate + NADH + H+ SUBSTRATE D-altronate NAD+ PRODUCT D-tagaturonate NADH H+ PATHWAY PATH: map00040 Pentose and glucuronate interconversions ORTHOLOG KO: K00041 tagaturonate reductase GENES ECO: b1521(uxaB) ECJ: JW1514(uxaB) ECE: Z2184(uxaB) ECS: ECs2128 YPE: YPO0580(uxaB) YPK: y3599(uxaB) YPM: YP2900(uxaB) YPS: YPTB3477(uxaB) SFL: SF1572(uxaB) SFX: S1699(uxaB) ECA: ECA0646(uxaB1) ECA4383(uxaB2) PPR: PBPRB1516 BBA: Bd3477 ATU: Atu2813(uxaB) ATC: AGR_C_5101 BSU: BG13212(uxaB) BHA: BH0492 BLI: BL00711(uxaB) CAC: CAC0695 BTH: BT0825 REFERENCE 1 Hickman, J. and Ashwell, G. Uronic acid metabolism in bacteria. II. Purification and properties of D-altronic acid and D-mannonic acid dehyrogenases in Escherichia coli. J. Biol. Chem. 235 (1960) 1566-1570. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.58 ExPASy - ENZYME nomenclature database: 1.1.1.58 ERGO genome analysis and discovery system: 1.1.1.58 BRENDA, the Enzyme Database: 1.1.1.58 CAS: 9028-45-9 /// ENTRY EC 1.1.1.59 NAME 3-hydroxypropionate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3-hydroxypropanoate:NAD+ oxidoreductase REACTION 3-hydroxypropanoate + NAD+ = 3-oxopropanoate + NADH + H+ SUBSTRATE 3-hydroxypropanoate NAD+ PRODUCT 3-oxopropanoate NADH H+ PATHWAY PATH: map00410 beta-Alanine metabolism PATH: map00640 Propanoate metabolism REFERENCE 1 Den, H., Robinson, W.G. and Coon, M.J. Enzymatic conversion of beta-hydroxypropionate to malonic semialdehyde. J. Biol. Chem. 234 (1959) 1666-1671. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.59 ExPASy - ENZYME nomenclature database: 1.1.1.59 ERGO genome analysis and discovery system: 1.1.1.59 BRENDA, the Enzyme Database: 1.1.1.59 CAS: 9028-59-5 /// ENTRY EC 1.1.1.60 NAME 2-hydroxy-3-oxopropionate reductase tartronate semialdehyde reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-glycerate:NAD(P)+ oxidoreductase REACTION (R)-glycerate + NAD(P)+ = 2-hydroxy-3-oxopropanoate + NAD(P)H + H+ SUBSTRATE (R)-glycerate NAD+ NADP+ PRODUCT 2-hydroxy-3-oxopropanoate NADH NADPH H+ PATHWAY PATH: map00630 Glyoxylate and dicarboxylate metabolism ORTHOLOG KO: K00042 2-hydroxy-3-oxopropionate reductase GENES ECO: b0509(glxR) b3125(garR) ECJ: JW0497(ybbQ) JW3094(yhaE) ECE: Z0663(ybbQ) Z4477(yhaE) ECS: ECs0570 ECs4003 ECC: c0624(ybbQ) c3880(yhaE) STY: STY0567(garR) STY3430(garR) STT: t2341(garR) t3168(garR) STM: STM0519(glxR) STM3248(garR) YPE: YPO3648 YPK: y0219 YPM: YP3899(mmsB) YPS: YPTB3582 SFL: SF3162(yhaE) SFX: S3377(yhaE) ECA: ECA0489 ECA3573(garR) PPR: PBPRA2273 PAE: PA1500 PPU: PP4299(glxR) CVI: CV3870 RSO: RS02512(glxR) RS02679 BMA: BMAA0577(garR) BPS: BPSL1450(glxR) BPE: BP1169 BPA: BPP1597 BPP3639 BBR: BB2674 BB4074 NEU: NE0676 MLO: mlr0254 SME: SMa0237 SMb20679(glxR) ATU: Atu2737 ATC: AGR_C_4961 BJA: blr3168 BCA: BCE2381(garR) BCE4109 BLD: BLi02105 SCO: SCO6205(SC2G5.26c) SMA: SAV2025 SYW: SYNW2331 PTO: PTO1147 MOTIF PS: PS00895 [LIVMFY](2)-G-L-G-x-[MQ]-G-x(2)-[MA]-[SAV]-x-[SNHR] REFERENCE 1 Gotto, A.M. and Kornberg, H.L. The metabolism of C2 compounds in micro-organisms. 7. Preparation and properties of crystalline tartronic semialdehyde reductase. Biochem. J. 81 (1961) 273-284. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.60 ExPASy - ENZYME nomenclature database: 1.1.1.60 ERGO genome analysis and discovery system: 1.1.1.60 BRENDA, the Enzyme Database: 1.1.1.60 CAS: 9028-68-6 /// ENTRY EC 1.1.1.61 NAME 4-hydroxybutyrate dehydrogenase gamma-hydroxybutyrate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 4-hydroxybutanoate:NAD+ oxidoreductase REACTION 4-hydroxybutanoate + NAD+ = succinate semialdehyde + NADH + H+ SUBSTRATE 4-hydroxybutanoate NAD+ PRODUCT succinate semialdehyde NADH H+ PATHWAY PATH: map00650 Butanoate metabolism ORTHOLOG KO: K00043 4-hydroxybutyrate dehydrogenase GENES RSO: RS02318(gbd2) BPA: BPP2084(gbd) BBR: BB1480(gbd) BME: BMEII1094 MOTIF PS: PS00060 [GSW]-x-[LIVTSACD]-[GH]-x(2)-[GSAE]-[GSHYQ]-x-[LIVTP]- [GAST]-[GAS]-x(3)-[LIVMT]-x-[HNS]-[GA]-x-[GTAC] PS: PS00913 [STALIV]-[LIVF]-x-[DE]-x(6,7)-P-x(4)-[ALIV]-x-[GST]- x(2)-D-[TAIVM]-[LIVMF]-x(4)-E REFERENCE 1 Nirenberg, M.W. and Jakoby, W.B. Enzymatic utilization of gamma-hydroxybutyric acid J. Biol. Chem. 235 (1960) 954-960. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.61 ExPASy - ENZYME nomenclature database: 1.1.1.61 ERGO genome analysis and discovery system: 1.1.1.61 BRENDA, the Enzyme Database: 1.1.1.61 CAS: 9028-60-8 /// ENTRY EC 1.1.1.62 NAME estradiol 17beta-dehydrogenase 20alpha-hydroxysteroid dehydrogenase 17beta,20alpha-hydroxysteroid dehydrogenase 17beta-estradiol dehydrogenase estradiol dehydrogenase estrogen 17-oxidoreductase 17beta-HSD CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME estradiol-17beta:NAD(P)+ 17-oxidoreductase REACTION estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+ SUBSTRATE estradiol-17beta NAD+ NADP+ PRODUCT estrone NADH NADPH H+ COMMENT Also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group. B-specific with respect to NAD(P)+ (cf. EC 1.1.1.149 20alpha-hydroxysteroid dehydrogenase). PATHWAY PATH: map00150 Androgen and estrogen metabolism ORTHOLOG KO: K00044 estradiol 17beta-dehydrogenase GENES HSA: 3292(HSD17B1) 3293(HSD17B3) 3294(HSD17B2) 3295(HSD17B4) 51478(HSD17B7) 7923(HSD17B8) MMU: 14979(H2-Ke6) 15485(Hsd17b1) 15486(Hsd17b2) 15487(Hsd17b3) 15488(Hsd17b4) 15490(Hsd17b7) RNO: 117182(Hsd17b3) 25322(Hsd17b1) 29540(Hsd17b7) 79243(Hsd17b2) 79244(Hsd17b4) DME: CG3415-PA(CG3415) CAL: orf19.1709(PXP18) orf19.3859 DISEASE MIM: 109685 Hydroxysteroid (17-beta) dehydrogenase 2 MIM: 601860 Hydroxysteroid (17-beta) dehydrogenase 4 MIM: 605573 Hydroxysteroid (17-beta) dehydrogenase 3 MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] STRUCTURES PDB: 1A27 1BHS 1DHT 1EQU 1FDS 1FDT 1FDU 1FDV 1FDW 1GZ6 1I5R 1IKT 1IOL 1JTV 1QYV 1QYW 1QYX 1S1P 1S1R 1S2A 1S2C 1XF0 3DHE REFERENCE 1 [PMID:4314937] Kautsky, M.P. and Hagerman, D.D. 17beta-Estradiol dehydrogenase of ovine ovaries J. Biol. Chem. 245 (1970) 1978-1984. 2 Langer, L.J., Alexander, J.A. and Engel, L.L. Human placental estradiol-17beta dehydrogenase. II. Kinetics and substrate specificities. J. Biol. Chem. 234 (1959) 2609-2614. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.62 ExPASy - ENZYME nomenclature database: 1.1.1.62 ERGO genome analysis and discovery system: 1.1.1.62 BRENDA, the Enzyme Database: 1.1.1.62 CAS: 9028-61-9 /// ENTRY EC 1.1.1.63 NAME testosterone 17beta-dehydrogenase 17-ketoreductase 17beta-HSD CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 17beta-hydroxysteroid:NAD+ 17-oxidoreductase REACTION testosterone + NAD+ = androst-4-ene-3,17-dione + NADH + H+ SUBSTRATE testosterone NAD+ PRODUCT androst-4-ene-3,17-dione NADH H+ PATHWAY PATH: map00150 Androgen and estrogen metabolism REFERENCE 1 Endahl, G.L., Kochakia, C.D. and Hamm, D. Separation of a triphosphopyridine nucleotide-specific from a diphosphopyridine-specific 17beta-hydroxy (testosterone) dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 2792-2796. 2 Sweat, M.L., Samuels, L.T. and Lumry, R. Preparation and characterisation of the enzyme which converts testosterone to androstendione. J. Biol. Chem. 185 (1950) 75-84. 3 Villee, C.A. and Spencer, J.M. Some properties of the pyridine nucleotide-specific 17beta-hydroxy steroid dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 3615-3619. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.63 ExPASy - ENZYME nomenclature database: 1.1.1.63 ERGO genome analysis and discovery system: 1.1.1.63 BRENDA, the Enzyme Database: 1.1.1.63 CAS: 9028-62-0 /// ENTRY EC 1.1.1.64 NAME testosterone 17beta-dehydrogenase (NADP+) 17-ketoreductase NADP-dependent testosterone-17beta-oxidoreductase testosterone 17beta-dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 17beta-hydroxysteroid:NADP+ 17-oxidoreductase REACTION testosterone + NADP+ = androst-4-ene-3,17-dione + NADPH + H+ SUBSTRATE testosterone NADP+ PRODUCT androst-4-ene-3,17-dione NADPH H+ COMMENT Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital. PATHWAY PATH: map00150 Androgen and estrogen metabolism REFERENCE 1 Endahl, G.L., Kochakia, C.D. and Hamm, D. Separation of a triphosphopyridine nucleotide-specific from a diphosphopyridine-specific 17beta-hydroxy (testosterone) dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 2792-2796. 2 Sweat, M.L., Samuels, L.T. and Lumry, R. Preparation and characterisation of the enzyme which converts testosterone to androstendione. J. Biol. Chem. 185 (1950) 75-84. 3 Villee, C.A. and Spencer, J.M. Some properties of the pyridine nucleotide-specific 17beta-hydroxy steroid dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 3615-3619. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.64 ExPASy - ENZYME nomenclature database: 1.1.1.64 ERGO genome analysis and discovery system: 1.1.1.64 BRENDA, the Enzyme Database: 1.1.1.64 CAS: 9028-63-1 /// ENTRY EC 1.1.1.65 NAME pyridoxine 4-dehydrogenase pyridoxin dehydrogenase pyridoxol dehydrogenase pyridoxine dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME pyridoxine:NADP+ 4-oxidoreductase REACTION pyridoxine + NADP+ = pyridoxal + NADPH + H+ SUBSTRATE pyridoxine NADP+ PRODUCT pyridoxal NADPH H+ COMMENT Also oxidizes pyridoxine phosphate. PATHWAY PATH: map00750 Vitamin B6 metabolism ORTHOLOG KO: K05275 pyridoxine 4-dehydrogenase REFERENCE 1 Holzer, H. and Schneider, S. Reinigung und charakterisierung einer TPN-abhangigen Pyridoxol-dehydrogenase aus bierhefe. Biochim. Biophys. Acta 48 (1961) 71-76. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.65 ExPASy - ENZYME nomenclature database: 1.1.1.65 ERGO genome analysis and discovery system: 1.1.1.65 BRENDA, the Enzyme Database: 1.1.1.65 CAS: 9028-64-2 /// ENTRY EC 1.1.1.66 NAME omega-hydroxydecanoate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 10-hydroxydecanoate:NAD+ 10-oxidoreductase REACTION 10-hydroxydecanoate + NAD+ = 10-oxodecanoate + NADH + H+ SUBSTRATE 10-hydroxydecanoate NAD+ PRODUCT 10-oxodecanoate NADH H+ COMMENT Also acts, more slowly, on 9-hydroxynonanoate and 11-hydroxyundecanoate. REFERENCE 1 Kamei, S., Wakabayashi, K. and Shimazono, M. omega-Oxidation of fatty acids in vitro. II. omega-Hydroxy fatty acid-NAD oxidoreductase. J. Biochem. (Tokyo) 56 (1964) 72-76. 2 Mitz, M.A. and Henrikson, R.L. Omega hydroxy fatty acid dehydrogenase. Biochim. Biophys. Acta 46 (1961) 45-50. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.66 ExPASy - ENZYME nomenclature database: 1.1.1.66 ERGO genome analysis and discovery system: 1.1.1.66 BRENDA, the Enzyme Database: 1.1.1.66 CAS: 9028-65-3 /// ENTRY EC 1.1.1.67 NAME mannitol 2-dehydrogenase D-mannitol dehydrogenase mannitol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-mannitol:NAD+ 2-oxidoreductase REACTION D-mannitol + NAD+ = D-fructose + NADH + H+ SUBSTRATE D-mannitol NAD+ PRODUCT D-fructose NADH H+ PATHWAY PATH: map00051 Fructose and mannose metabolism ORTHOLOG KO: K00045 mannitol 2-dehydrogenase GENES MLO: mll4920 mlr4057 SME: SMc01501(mtlK) ATU: Atu4451(mtlK) ATC: AGR_L_830 CCR: CC1487 MPA: MAP3809c CGL: NCgl0108(Cgl0109) MOTIF PS: PS00974 [LIVMY]-x-[FS]-x(2)-[STAGCV]-x-V-D-R-[IV]-x-[PS] STRUCTURES PDB: 1LJ8 1M2W REFERENCE 1 Martinez, G., Barker, H.A. and Horecker, B.L. A specific mannitol dehydrogenase from Lactobacillus brevis. J. Biol. Chem. 238 (1963) 1598-1603. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.67 ExPASy - ENZYME nomenclature database: 1.1.1.67 ERGO genome analysis and discovery system: 1.1.1.67 BRENDA, the Enzyme Database: 1.1.1.67 CAS: 9001-65-4 /// ENTRY EC 1.1.1.68 Obsolete NAME Transferred to 1.7.99.5 CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Transferred entry: now EC 1.7.99.5 5,10-methylenetetrahydrofolate reductase (FADH2) (EC 1.1.1.68 created 1965, deleted 1978 [transferred to EC 1.1.99.15, deleted 1980]) DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.68 ExPASy - ENZYME nomenclature database: 1.1.1.68 ERGO genome analysis and discovery system: 1.1.1.68 BRENDA, the Enzyme Database: 1.1.1.68 /// ENTRY EC 1.1.1.69 NAME gluconate 5-dehydrogenase 5-keto-D-gluconate 5-reductase 5-ketogluconate 5-reductase 5-ketogluconate reductase 5-keto-D-gluconate reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-gluconate:NAD(P)+ 5-oxidoreductase REACTION D-gluconate + NAD(P)+ = 5-dehydro-D-gluconate + NAD(P)H + H+ SUBSTRATE D-gluconate NAD+ NADP+ PRODUCT 5-dehydro-D-gluconate NADH NADPH H+ GENES CAL: orf19.6322(ARD1) ECO: b4266(idnO) ECJ: JW4223(idnO) ECC: c0321 c5367(idnO) STM: STM4483(idnO) YPE: YPO2539(idnO) YPK: y1645 YPM: YP2350(idnO) YPS: YPTB2571(idnO) RSO: RS05386(idnO) BPE: BP0464(idnO) BPA: BPP4378(idnO) BBR: BB1512 BB4964(idnO) MLO: mlr3785 SME: SMa0513(idnO1) SMb20692(idnO1) SMb20750 ATU: Atu1407 Atu2417 Atu4086(idnO) ATC: AGR_C_2598 AGR_C_4386 AGR_L_1541 BJA: blr5277 CCR: CC1286 SPY: SPy0636(idnO) SPM: spyM18_0699 SPG: SpyM3_0448 SPS: SPs1408 SPA: M6_Spy0545 SPN: SP0320 SPR: spr0290(gno) SAG: SAG1904 SAN: gbs1891 EFA: EF0426 EF2263 CAC: CAC2607 SCO: SCO1681(SCI30A.02) SMA: SAV6627(kduD) FNU: FN1687 RBA: RB6802 BTH: BT3232 TTH: TTC0235 MAC: MA0107(gno) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] STRUCTURES PDB: 1VL8 REFERENCE 1 Ameyama, M. and Adachi, O. 5-Keto-D-gluconate reductase from Gluconobacter suboxydans. Methods Enzymol. 89 (1982) 198-202. 2 De Ley, J. 5-Ketogluconic acid reductase Methods Enzymol. 9 (1966) 200-203. 3 Okamoto, K. Enzymic studies on the formation of 5-ketogluconic acid by Acetobacter suboxydans. II. 5-Ketogluconate reductase. J. Biochem. (Tokyo) 53 (1963) 448. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.69 ExPASy - ENZYME nomenclature database: 1.1.1.69 ERGO genome analysis and discovery system: 1.1.1.69 BRENDA, the Enzyme Database: 1.1.1.69 CAS: 9028-70-0 /// ENTRY EC 1.1.1.70 Obsolete NAME Deleted entry CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Deleted entry: D-glucuronolactone dehydrogenase. Now included with EC 1.2.1.3 aldehyde dehydrogenase (NAD+) (EC 1.1.1.70 created 1965, deleted 1978) DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.70 ExPASy - ENZYME nomenclature database: 1.1.1.70 ERGO genome analysis and discovery system: 1.1.1.70 BRENDA, the Enzyme Database: 1.1.1.70 /// ENTRY EC 1.1.1.71 NAME alcohol dehydrogenase [NAD(P)+] retinal reductase aldehyde reductase (NADPH/NADH) alcohol dehydrogenase [NAD(P)] CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME alcohol:NAD(P)+ oxidoreductase REACTION an alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+ SUBSTRATE alcohol NAD+ NADP+ PRODUCT aldehyde NADH NADPH H+ COMMENT Reduces aliphatic aldehydes of carbon chain length from 2 to 14, with greatest activity on C4, C6 and C8 aldehydes; also reduces retinal to retinol. PATHWAY PATH: map00010 Glycolysis / Gluconeogenesis REFERENCE 1 [PMID:4300551] Fidge, N.H. and Goodman, D.S. The enzymatic reducation of retinal to retinol in rat intestine. J. Biol. Chem. 243 (1968) 4372-4379. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.71 ExPASy - ENZYME nomenclature database: 1.1.1.71 ERGO genome analysis and discovery system: 1.1.1.71 UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.71 BRENDA, the Enzyme Database: 1.1.1.71 CAS: 37250-10-5 /// ENTRY EC 1.1.1.72 NAME glycerol dehydrogenase (NADP+) glycerol dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME glycerol:NADP+ oxidoreductase REACTION glycerol + NADP+ = D-glyceraldehyde + NADPH + H+ SUBSTRATE glycerol NADP+ PRODUCT D-glyceraldehyde NADPH H+ PATHWAY PATH: map00561 Glycerolipid metabolism MOTIF PS: PS00062 [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY] PS: PS00063 [LIVM]-[PAIV]-[KR]-[ST]-x(4)-R-x(2)-[GSTAEQK]-[NSL]- x(2)-[LIVMFA] PS: PS00798 G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGC]-[AS]-x(5)-E-x(2)- [LIVM]-G REFERENCE 1 [PMID:4400494] Kormann, A.W., Hurst, R.O. and Flynn, T.G. Purification and properties of an NADP+-dependent glycerol dehydrogenase from rabbit skeletal muscle. Biochim. Biophys. Acta 258 (1972) 40-55. 2 Toews, C.J. The kinetics and reaction mechanism of the nicotinamide-adinine dinucleotide phosphate-specific glycerol dehydrogenase of rat skeletal muscle. Biochem. J. 105 (1967) 1067-1073. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.72 ExPASy - ENZYME nomenclature database: 1.1.1.72 ERGO genome analysis and discovery system: 1.1.1.72 BRENDA, the Enzyme Database: 1.1.1.72 CAS: 37250-11-6 /// ENTRY EC 1.1.1.73 NAME octanol dehydrogenase 1-octanol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME octanol:NAD+ oxidoreductase REACTION 1-octanol + NAD+ = 1-octanal + NADH + H+ SUBSTRATE 1-octanol NAD+ PRODUCT 1-octanal NADH H+ COMMENT Acts, less rapidly, on other long-chain alcohols. MOTIF PS: PS00059 G-H-E-x(2)-G-x(5)-[GA]-x(2)-[IVSAC] REFERENCE 1 [PMID:4308448] Roche, B. and Azoulay, E. Regulation des alcool-deshydrogenases chez Saccharomyces cerevisiae. Eur. J. Biochem. 8 (1969) 426-434. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.73 ExPASy - ENZYME nomenclature database: 1.1.1.73 ERGO genome analysis and discovery system: 1.1.1.73 BRENDA, the Enzyme Database: 1.1.1.73 CAS: 9031-31-6 /// ENTRY EC 1.1.1.74 Obsolete NAME Deleted entry CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Deleted entry: D-aminopropanol dehydrogenase (reaction due to EC 1.1.1.4 (R,R)-butanediol dehydrogenase) (EC 1.1.1.74 created 1972, deleted 1976) DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.74 ExPASy - ENZYME nomenclature database: 1.1.1.74 ERGO genome analysis and discovery system: 1.1.1.74 BRENDA, the Enzyme Database: 1.1.1.74 /// ENTRY EC 1.1.1.75 NAME (R)-aminopropanol dehydrogenase L-aminopropanol dehydrogenase 1-aminopropan-2-ol-NAD+ dehydrogenase L(+)-1-aminopropan-2-ol:NAD+ oxidoreductase 1-aminopropan-2-ol-dehydrogenase DL-1-aminopropan-2-ol: NAD+ dehydrogenase L(+)-1-aminopropan-2-ol-NAD/NADP oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-1-aminopropan-2-ol:NAD+ oxidoreductase REACTION (R)-1-aminopropan-2-ol + NAD+ = aminoacetone + NADH + H+ SUBSTRATE (R)-1-aminopropan-2-ol NAD+ PRODUCT aminoacetone NADH H+ COMMENT Requires K+. PATHWAY PATH: map00260 Glycine, serine and threonine metabolism REFERENCE 1 [PMID:4385233] Dekker, E.E. and Swain, R.R. Formation of D(g)-1-amino-2-propanol by a highly purified enzyme from Escherichia coli. Biochim. Biophys. Acta 158 (1968) 306-307. 2 [PMID:5329339] Turner, J.M. Microbial metabolism of amino ketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrgenase in Escherichia coli. Biochem. J. 99 (1966) 427-433. 3 [PMID:5340733] Turner, J.M. Microbial metabolism of amino ketones. L-1-Aminopropan-2-ol dehydrogenase and L-threonine dehydrogenase in Escherichia coli. Biochem. J. 104 (1967) 112-121. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.75 ExPASy - ENZYME nomenclature database: 1.1.1.75 ERGO genome analysis and discovery system: 1.1.1.75 BRENDA, the Enzyme Database: 1.1.1.75 CAS: 37250-13-8 /// ENTRY EC 1.1.1.76 NAME (S,S)-butanediol dehydrogenase L-butanediol dehydrogenase L-BDH L(+)-2,3-butanediol dehydrogenase (L-acetoin forming) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S,S)-butane-2,3-diol:NAD+ oxidoreductase REACTION (S,S)-butane-2,3-diol + NAD+ = acetoin + NADH + H+ SUBSTRATE (S,S)-butane-2,3-diol NAD+ PRODUCT acetoin NADH H+ PATHWAY PATH: map00650 Butanoate metabolism REFERENCE 1 Taylor, M.B. and Juni, E. Stereoisomeric specificities of 2,3-butanediol dehydrogenases. Biochim. Biophys. Acta 39 (1960) 448-457. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.76 ExPASy - ENZYME nomenclature database: 1.1.1.76 ERGO genome analysis and discovery system: 1.1.1.76 BRENDA, the Enzyme Database: 1.1.1.76 CAS: 37250-14-9 /// ENTRY EC 1.1.1.77 NAME lactaldehyde reductase propanediol:nicotinamide adenine dinucleotide (NAD) oxidoreductase L-lactaldehyde:propanediol oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)[or (S)]-propane-1,2-diol:NAD+ oxidoreductase REACTION (R)[or (S)]-propane-1,2-diol + NAD+ = (R)[or (S)]-lactaldehyde + NADH + H+ SUBSTRATE (R)-propane-1,2-diol (S)-propane-1,2-diol NAD+ PRODUCT (R)-lactaldehyde (S)-lactaldehyde NADH H+ PATHWAY PATH: map00620 Pyruvate metabolism PATH: map00630 Glyoxylate and dicarboxylate metabolism ORTHOLOG KO: K00048 lactaldehyde reductase GENES ECO: b2799(fucO) ECJ: JW2770(fucO) ECE: Z4116(fucO) ECS: ECs3659 ECC: c3367(fucO) STY: STY3112(fucO) STT: t2881(fucO) STM: STM2973(fucO) SFL: SF2813(fucO) SFX: S3008(fucO) ECA: ECA0742(fucO) BLO: BL1673(fucO) BTH: BT3767 MOTIF PS: PS00060 [GSW]-x-[LIVTSACD]-[GH]-x(2)-[GSAE]-[GSHYQ]-x-[LIVTP]- [GAST]-[GAS]-x(3)-[LIVMT]-x-[HNS]-[GA]-x-[GTAC] PS: PS00913 [STALIV]-[LIVF]-x-[DE]-x(6,7)-P-x(4)-[ALIV]-x-[GST]- x(2)-D-[TAIVM]-[LIVMF]-x(4)-E STRUCTURES PDB: 1RRM REFERENCE 1 Ting, S.-M., Sellinger, O.Z. and Miller, O.N. The metabolism of lactaldehyde. VI. The reduction of D- and L-lactaldehyde in rat liver. Biochim. Biophys. Acta 89 (1964) 217-225. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.77 ExPASy - ENZYME nomenclature database: 1.1.1.77 ERGO genome analysis and discovery system: 1.1.1.77 BRENDA, the Enzyme Database: 1.1.1.77 CAS: 37250-15-0 /// ENTRY EC 1.1.1.78 NAME D-lactaldehyde dehydrogenase methylglyoxal reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-lactaldehyde:NAD+ oxidoreductase REACTION (R)-lactaldehyde + NAD+ = methylglyoxal + NADH + H+ SUBSTRATE (R)-lactaldehyde NAD+ PRODUCT methylglyoxal NADH H+ PATHWAY PATH: map00620 Pyruvate metabolism REFERENCE 1 Ting, S.-M., Miller, O.N. and Sellinger, O.Z. The metabolism of lactaldehyde. VII. The oxidation of D-lactaldehyde in rat liver. Biochim. Biophys. Acta 97 (1965) 407. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.78 ExPASy - ENZYME nomenclature database: 1.1.1.78 ERGO genome analysis and discovery system: 1.1.1.78 BRENDA, the Enzyme Database: 1.1.1.78 CAS: 37250-16-1 /// ENTRY EC 1.1.1.79 NAME glyoxylate reductase (NADP+) NADPH-glyoxylate reductase glyoxylate reductase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME glycolate:NADP+ oxidoreductase REACTION glycolate + NADP+ = glyoxylate + NADPH + H+ SUBSTRATE glycolate NADP+ PRODUCT glyoxylate NADPH H+ COMMENT Also reduces hydroxypyruvate to glycerate; has some affinity for NAD+. PATHWAY PATH: map00620 Pyruvate metabolism PATH: map00630 Glyoxylate and dicarboxylate metabolism ORTHOLOG KO: K00049 glyoxylate reductase (NADP+) GENES HSA: 9380(GRHPR) CME: CMQ289C ECO: b1033(ycdW) REFERENCE 1 Cartwright, L.N. and Hullin, R.P. Purification and properties of two glyoxylate reductases from a species of Pseudomonas. Biochem. J. 101 (1966) 781-791. 2 [PMID:3548703] Kleczkowski, L.A., Randall, D.D. and Blevins, D.G. Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate reductase from spinach leaves. Comparison of immunological properties of leaf glyoxylate reductase and hydroxypyruvate reductase. Biochem. J. 239 (1986) 653-659. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.79 ExPASy - ENZYME nomenclature database: 1.1.1.79 ERGO genome analysis and discovery system: 1.1.1.79 BRENDA, the Enzyme Database: 1.1.1.79 CAS: 37250-17-2 /// ENTRY EC 1.1.1.80 NAME isopropanol dehydrogenase (NADP+) isopropanol dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME propan-2-ol:NADP+ oxidoreductase REACTION propan-2-ol + NADP+ = acetone + NADPH + H+ SUBSTRATE propan-2-ol NADP+ PRODUCT acetone NADPH H+ COMMENT Also acts on other short-chain secondary alcohols and, slowly, on primary alcohols. PATHWAY PATH: map00640 Propanoate metabolism REFERENCE 1 Hoshino, K. Organism producing isopropanol from acetone. V. Enzymological [studies] on the oxidation-reduction of Lactobacillus brevis var. hofuensis. [in Japanese] Nippon Nogei Kagaku Kaishi 34 (1960) 608-615. 2 Hoshino, K. and Udagawa, K. Organism producing isopropanol from acetone. VI. Isopropanol dehydrogenase and alcohol dehydrogenase of Lactobacillus brevis var. hofuensis. [in Japanese] Nippon Nogei Kagaku Kaishi 34 (1960) 616-619. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.80 ExPASy - ENZYME nomenclature database: 1.1.1.80 ERGO genome analysis and discovery system: 1.1.1.80 BRENDA, the Enzyme Database: 1.1.1.80 CAS: 37250-18-3 /// ENTRY EC 1.1.1.81 NAME hydroxypyruvate reductase beta-hydroxypyruvate reductase NADH:hydroxypyruvate reductase D-glycerate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-glycerate:NADP+ 2-oxidoreductase REACTION D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H + H+ SUBSTRATE D-glycerate NAD+ NADP+ PRODUCT hydroxypyruvate NADH NADPH H+ PATHWAY PATH: map00260 Glycine, serine and threonine metabolism PATH: map00630 Glyoxylate and dicarboxylate metabolism ORTHOLOG KO: K00050 hydroxypyruvate reductase GENES CAL: orf19.3584 YPE: YPO2536 YPS: YPTB2568 PPR: PBPRA2272 PAE: PA1499 PPU: PP4300 CVI: CV3660(ttuD) RSO: RS03094(ttuD1) RS05749(ttuD2) NEU: NE2456(ttuD2) DVU: DVU0765 BBA: Bd3195 MLO: mlr5146 SME: SMa1406(ttuD3) SMb20678(ttuD2) SMc04389(ttuD1) ATU: Atu3232 Atu5334 ATC: AGR_L_3166 AGR_pAT_bx66 BME: BMEI1570 BMS: BR0355 BJA: blr7830 RPA: RPA1797 LIL: LA2527(ttuD) LIC: LIC11445 TTH: TTC0124 HMA: pNG7015(ttuD) REFERENCE 1 Kleczkowski, L.A. and Edwards, G.E. Identification of hydroxypyruvate and glyoxylate reductases in maize leaves. Plant Physiol. 91 (1989) 278-286. 2 [PMID:3281657] Kleczkowski, L.A. and Randall, D.D. Purification and characterization of a novel NADPH(NADH)-dependent hydroxypyruvate reductase from spinach leaves. Comparison of immunological properties of leaf hydroxypyruvate reductases. Biochem. J. 250 (1988) 145-152. 3 [PMID:4385077] Kohn, L.D. and Jakoby, W.B. Tartaric acid metabolism. VII. Crystalline hydroxypyruvate reductase (D-glycerate dehydrogenase). J. Biol. Chem. 243 (1968) 2494-2499. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.81 ExPASy - ENZYME nomenclature database: 1.1.1.81 ERGO genome analysis and discovery system: 1.1.1.81 BRENDA, the Enzyme Database: 1.1.1.81 CAS: 9059-44-3 /// ENTRY EC 1.1.1.82 NAME malate dehydrogenase (NADP+) NADP-malic enzyme NADP-malate dehydrogenase malic dehydrogenase (nicotinamide adenine dinucleotide phosphate) malate NADP dehydrogenase NADP malate dehydrogenase NADP-linked malate dehydrogenase malate dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S)-malate:NADP+ oxidoreductase REACTION (S)-malate + NADP+ = oxaloacetate + NADPH + H+ SUBSTRATE (S)-malate NADP+ PRODUCT oxaloacetate NADPH H+ COMMENT Activated by light. PATHWAY PATH: map00620 Pyruvate metabolism PATH: map00710 Carbon fixation ORTHOLOG KO: K00051 malate dehydrogenase (NADP+) GENES ATH: At5g58330(MCK7.20) CGL: NCgl0631(Cgl0661) MJA: MJ0490(ldh) MMP: MMP0645(mdh) MOTIF PS: PS00064 [LIVMA]-G-[EQ]-H-G-[DN]-[ST] PS: PS00068 [LIVM]-T-[TRKMN]-L-D-x(2)-R-[STA]-x(3)-[LIVMFY] STRUCTURES PDB: 1CIV 7MDH REFERENCE 1 [PMID:5689906] Connelly, J.L., Danner, D.J. and Bowden, J.A. Branched chain alpha-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver alpha-ketoisocaproic:alpha-keto-beta-methylvaleric acid dehydrogenase. J. Biol. Chem. 243 (1968) 1198-1203. 2 [PMID:4397919] Johnson, H.S. NADP-malate dehydrogenase: photoactivation in leaves of plants with Calvin cycle photosynthesis. Biochem. Biophys. Res. Commun. 43 (1971) 703-709. 3 [PMID:4395182] Johnson, H.S. and Hatch, M.D. Properties and regulation of leaf nicotinamide-adenine dinucleotide phosphate-malate dehydrogenase and 'malic' enzyme in plants with the C4-dicarboxylic acid pathway of photosynthesis. Biochem. J. 119 (1970) 273-280. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.82 ExPASy - ENZYME nomenclature database: 1.1.1.82 ERGO genome analysis and discovery system: 1.1.1.82 BRENDA, the Enzyme Database: 1.1.1.82 CAS: 37250-19-4 /// ENTRY EC 1.1.1.83 NAME D-malate dehydrogenase (decarboxylating) D-malate dehydrogenase D-malic enzyme bifunctional L(+)-tartrate dehydrogenase-D(+)-malate $(decarboxylating) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-malate:NAD+ oxidoreductase (decarboxylating) REACTION (R)-malate + NAD+ = pyruvate + CO2 + NADH SUBSTRATE (R)-malate NAD+ PRODUCT pyruvate CO2 NADH PATHWAY PATH: map00650 Butanoate metabolism REFERENCE 1 [PMID:4889267] Stern, J.R. and O'Brien, R.W. Oxidation D-malic and beta-alkylmalic acids wild-type and mutant strains of Salmonella typhimurium and by Aerobacter aerogenes. J. Bacteriol. 98 (1969) 147-151. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.83 ExPASy - ENZYME nomenclature database: 1.1.1.83 ERGO genome analysis and discovery system: 1.1.1.83 BRENDA, the Enzyme Database: 1.1.1.83 CAS: 37250-20-7 /// ENTRY EC 1.1.1.84 NAME dimethylmalate dehydrogenase beta,beta-dimethylmalate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-3,3-dimethylmalate:NAD+ oxidoreductase (decarboxylating) REACTION (R)-3,3-dimethylmalate + NAD+ = 3-methyl-2-oxobutanoate + CO2 + NADH SUBSTRATE (R)-3,3-dimethylmalate NAD+ PRODUCT 3-methyl-2-oxobutanoate CO2 NADH COMMENT Requires K+ or NH4+ and Mn2+ or Co2+; also acts on (R)-malate. PATHWAY PATH: map00770 Pantothenate and CoA biosynthesis REFERENCE 1 [PMID:4287371] Magee, P.T. and Snell, E.E. The bacterial degradation of pantothenic acid. IV. Enzymatic conversion of aldopantoate to alpha-ketoisovalerate. Biochemistry 5 (1966) 409-416. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.84 ExPASy - ENZYME nomenclature database: 1.1.1.84 ERGO genome analysis and discovery system: 1.1.1.84 BRENDA, the Enzyme Database: 1.1.1.84 CAS: 37250-21-8 /// ENTRY EC 1.1.1.85 NAME 3-isopropylmalate dehydrogenase beta-isopropylmalic enzyme beta-isopropylmalate dehydrogenase threo-D(s)-3-isopropylmalate dehydrogenase 3-carboxy-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (2R,3S)-3-isopropylmalate:NAD+ oxidoreductase REACTION (2R,3S)-3-isopropylmalate + NAD+ = (2S)-2-isopropyl-3-oxosuccinate + NADH + H+ SUBSTRATE (2R,3S)-3-isopropylmalate NAD+ PRODUCT (2S)-2-isopropyl-3-oxosuccinate NADH H+ COMMENT The product decarboxylates spontaneously to 4-methyl-2-oxopentanoate. PATHWAY PATH: map00290 Valine, leucine and isoleucine biosynthesis ORTHOLOG KO: K00052 3-isopropylmalate dehydrogenase GENES ATH: At1g31180(F28K20.14) At1g80560(F5I6.21) At5g14200(MUA22.20) CME: CMM229C SCE: YCL018W(LEU2) AGO: AAL012C(AAL012Cp) CAL: orf19.7079(BUD3) orf19.7080(LEU2) ECO: b0073(leuB) ECJ: JW0072(leuB) ECE: Z0082(leuB) ECS: ECs0077 ECC: c0090(leuB) STY: STY0131(leuB) STT: t0116(leuB) STM: STM0112(leuB) YPE: YPO0532(leuB) YPK: y3646(leuB) YPM: YP3650(leuB2) YPS: YPTB0671(leuB) SFL: SF0068(leuB) SFX: S0070(leuB) ECA: ECA3832(leuB) PLU: plu3674(leuB) BUC: BUpL05(leuB) BAB: bbp496(leuB) BFL: Bfl132(leuB) HIN: HI0987(leuB) PMU: PM1961(leuB) XFA: XF2372 XFT: PD1397(leuB) XCC: XCC3328(leuB) XAC: XAC3456(leuB) VCH: VC2491 VVU: VV10655 VVY: VV0486 VPA: VP0344 PPR: PBPRA0418 PAE: PA3118(leuB) PPU: PP1988(leuB) PST: PSPTO2175(leuB) ACI: ACIAD0469(leuB) SON: SO4235(leuB) MCA: MCA2063(leuB) NME: NMB1031 NMA: NMA1456(leuB) CVI: CV2778(leuB) RSO: RS03417(leuB1) RS05429(leuB2) BMA: BMAA1726(leuB) BPS: BPSS1705(leuB) BPE: BP1483(leuB) BPA: BPP1944(leuB) BBR: BB1014(leuB) BB2132(leuB) NEU: NE0688(leuB) HHE: HH1134(leuB) WSU: WS1813 CJE: Cj1718c(leuB) GSU: GSU2879(leuB) DVU: DVU2985(leuB) BBA: Bd1264(leuB) DPS: DP1284 MLO: mll4399 SME: SMc04405(leuB) ATU: Atu2791(leuB) ATC: AGR_C_5067 BME: BMEII0271 BMEII0404 BMS: BRA0890(leuB) BJA: bll0414(leuB) bll0504(leuB) bll6321(leuB) blr2741 blr2781 RPA: RPA0227(leuB) CCR: CC0193 BSU: BG10675(leuB) BHA: BH3057(leuB) BAN: BA1421(leuB) BAR: GBAA1421(leuB) BAA: BA_1941 BAT: BAS1312 BCE: BC1401 BCA: BCE1521(leuB) BCZ: BTZK1286(leuB) BTK: BT9727_1285(leuB) BLI: BL00612(leuB) OIH: OB2619(leuB) SAU: SA1863(leuB) SAV: SAV2058(leuB) SAM: MW1982(leuB) SAR: SAR2145(leuB) SAS: SAS1963 SEP: SE1659 LMO: lmo1988(leuB) LMF: LMOf2365_2011(leuB) LIN: lin2095(leuB) LLA: L0074(leuB) SPR: spr1135(leuB) SMU: SMU.1383(leuB) CAC: CAC3171(leuB) TTE: TTE0019(leuB) MTU: Rv2995c(leuB) MTC: MT3073 MBO: Mb3019c(leuB) MLE: ML1691(leuB) MPA: MAP3032c(leuB) CGL: NCgl1237(Cgl1286) CEF: CE1383(leuB) CDI: DIP1105(leuB) SCO: SCO5522(leuB) SMA: SAV2718(leuB) LXX: Lxx13130(leuB) BLO: BL1218(leuB) RBA: RB12597(leuB) RB3767(leuB) LIL: LA2152(leuB) LIC: LIC11768(leuB) BTH: BT1857 SYN: slr1517(leuB) SYW: SYNW0784(leuB) SYC: syc2490_c(leuB) TEL: tlr1600(leuB) GVI: gll3551(leuB) ANA: alr1313(leuB) PMA: Pro0862(leuB) PMM: PMM0786(leuB) PMT: PMT0531(leuB) CTE: CT0615(leuB) DRA: DR1785 TTH: TTC0867 AAE: aq_244(leuB) TMA: TM0556 MJA: MJ0720 MMP: MMP0539(leuB) MAC: MA0201(leuB) MA3748(leuB) MMA: MM1489 MTH: MTH1388 MKA: MK0782(leuB_1) MK1215(leuB_2) AFU: AF0628(leuB) HMA: rrnAC0340(ipmD) PTO: PTO0910 PHO: PH1722 PAB: PAB0289(leuB-2) PAB2424(leuB-1) PFU: PF0940 SSO: SSO0723(leuB) STO: ST0433 PAI: PAE1995(leuB) MOTIF PS: PS00470 [NS]-[LIMYT]-[FYDN]-G-[DNGST]-[IMVY]-x-[STGDN]-[DN]- x(2)-[SGAP]-x(3,4)-G-[STG]-[LIVMPA]-G-[LIVMF] STRUCTURES PDB: 1A05 1DPZ 1DR0 1DR8 1G2U 1GC8 1GC9 1HEX 1IDM 1IPD 1OSI 1OSJ 1VLC 1WPW 1XAA 1XAB 1XAC 1XAD 2AYQ REFERENCE 1 Burns, R.O., Umbarger, H.E. and Gross, S.R. The biosynthesis of leucine. III. The conversion of alpha-hydroxy-beta-carboxyisocaproate to alpha-ketoisocaproate. Biochemistry 2 (1963) 1053. 2 [PMID:4889950] Parsons, S.J. and Burns, R.O. Purification and properties of beta-isopropylmalate dehydrogenase. J. Biol. Chem. 244 (1969) 996-1003. 3 [PMID:10683439] Nemeth, A., Svingor, Á., Pocsik, M., Dobo, J., Magyar, C, Szilaagyi, A., Gal, P. and Zavodszky, P. Mirror image mutations reveal the significance of an intersubuit ion cluster in the stability of 3-isopropylmalate dehydrogenase. FEBS Lett. 468 (2000) 48-52. 4 [PMID:14269331] Calvo, J. M., Stevens, C. M., Kalyanpur, M. G., and Umbarger, H. E. The absolute configuration of alpha-hydroxy-beta-carboxyisocaproic acid (3-isopropylmalic acid), an intermediate in leucine biosynthesis. Biochemistry 3 (1964) 2024-2027. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.85 ExPASy - ENZYME nomenclature database: 1.1.1.85 ERGO genome analysis and discovery system: 1.1.1.85 BRENDA, the Enzyme Database: 1.1.1.85 CAS: 9030-97-1 /// ENTRY EC 1.1.1.86 NAME ketol-acid reductoisomerase dihydroxyisovalerate dehydrogenase (isomerizing) acetohydroxy acid isomeroreductase ketol acid reductoisomerase alpha-keto-beta-hydroxylacyl reductoisomerase 2-hydroxy-3-keto acid reductoisomerase acetohydroxy acid reductoisomerase acetolactate reductoisomerase dihydroxyisovalerate (isomerizing) dehydrogenase isomeroreductase reductoisomerase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-2,3-dihydroxy-3-methylbutanoate:NADP+ oxidoreductase $(isomerizing) REACTION (R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+ SUBSTRATE (R)-2,3-dihydroxy-3-methylbutanoate NADP+ PRODUCT (S)-2-hydroxy-2-methyl-3-oxobutanoate NADPH H+ COMMENT Also catalyses the reduction of 2-aceto-2-hydroxybutanoate to 2,3-dihydroxy-3-methylpentanoate. PATHWAY PATH: map00290 Valine, leucine and isoleucine biosynthesis PATH: map00770 Pantothenate and CoA biosynthesis ORTHOLOG KO: K00053 ketol-acid reductoisomerase GENES ATH: At3g58610(F14P22.200) CME: CMR121C SCE: YLR355C(ILV5) AGO: ACL198W(ACL198Wp) CAL: orf19.88(ILV5) ECO: b3774(ilvC) ECJ: JW3747(ilvC) ECE: Z5285(ilvC) ECS: ECs4708 ECC: c4696(ilvC) STY: STY3648(ilvC) STT: t3389(ilvC) STM: STM3909(ilvC) YPE: YPO3888(ilvC) YPK: y0345(ilvC) YPM: YP3158(ilvC) YPS: YPTB0145(ilvC) SFL: SF3848(ilvY) SFX: S3910(ilvC) ECA: ECA4221(ilvC) PLU: plu4668(ilvC) BUC: BU599(ilvC) BAS: BUsg575(ilvC) BAB: bbp541(ilvC) BFL: Bfl588(ilvC) HIN: HI0682(ilvC) PMU: PM1284(ilvC) MSU: MS0045(ilvC) XFA: XF1822 XFT: PD1043(ilvC) XCC: XCC3323(ilvC) XAC: XAC3451(ilvC) VCH: VC0162 VVU: VV11077 VVY: VV0035 VPA: VP0035 PPR: PBPRA0085 PAE: PA4694(ilvC) PPU: PP4678(ilvC) PST: PSPTO0983(ilvC) ACI: ACIAD3102(ilvC) SON: SO4349(ilvC) MCA: MCA2272(ilvC) NME: NMB1574 NMA: NMA1763(ilvC) CVI: CV0588(ilvC) RSO: RS03640(ilvC) BMA: BMA1846(ilvC) BPS: BPSL1198(ilvC) BPE: BP0791(ilvC) BPA: BPP3435(ilvC) BBR: BB3885(ilvC) NEU: NE1323(ilvC) HPY: HP0330(ilvC) HPJ: jhp0313 HHE: HH1204(ilvC) WSU: WS1878(ilvC) CJE: Cj0632(ilvC) GSU: GSU1909(ilvC) DVU: DVU1378(ilvC) DPS: DP0726 MLO: mll1405 SME: SMc04346(ilvC) ATU: Atu2019(ilvC) ATC: AGR_C_3660 BME: BMEI0624 BMS: BR1380(ilvC) BJA: bll6497(ilvC) RPA: RPA2035(ilvC) BHE: BH10890(ilvC) BQU: BQ08540(ilvC) CCR: CC2120 BSU: BG10672(ilvC) BHA: BH3059(ilvC) BAN: BA1419(ilvC-1) BA1852(ilvC-2) BAR: GBAA1419(ilvC-1) GBAA1852(ilvC-2) BAA: BA_1939(ilvC) BA_2355(ilvC) BAT: BAS1310 BAS1716 BCE: BC1399 BC1779 BCA: BCE1519(ilvC) BCE1936(ilvC) BCZ: BTZK1284(ilvC) BTZK1668(ilvC) BTK: BT9727_1283(ilvC) BT9727_1693(ilvC) BLI: BL00610(ilvC) OIH: OB2621(ilvC) SAU: SA1861(ilvC) SAV: SAV2056(ilvC) SAM: MW1980(ilvC) SAR: SAR2143(ilvC) SAS: SAS1961 SEP: SE1657 LMO: lmo1986(ilvC) LMF: LMOf2365_2009(ilvC) LIN: lin2093(ilvC) LLA: L0080(ilvC) SPN: SP0447 SPR: spr0403(ilvC) SMU: SMU.233(ilvC) CAC: CAC0091(ilvC) TTE: TTE0015(ilvC) MTU: Rv3001c(ilvC) MTC: MT3081 MBO: Mb3026c(ilvC) MLE: ML1694(ilvC) MPA: MAP3036c(ilvC) CGL: NCgl1224(Cgl1273) CEF: CE1367(ilvC) CDI: DIP1100(ilvC) SCO: SCO5514(SC8D9.26) SCO7154(SC9A4.16c) SMA: SAV2731(ilvC) TWH: TW207(ilvC) TWS: TW565(ilvC) LXX: Lxx13170(ilvC) PAC: PPA1372 BLO: BL0530(ilvC1) BL0531(ilvC2) STH: STH2688 RBA: RB9869(ilvC) LIL: LA4242(ilvC) LIC: LIC13393(ilvC) BTH: BT2074 SYN: sll1363(ilvC) SYW: SYNW1650(ilvC) SYC: syc0010_c(ilvC) TEL: tll2254(ilvC) GVI: gll2657(ilvC) ANA: all2315 PMA: Pro1389(ilvC) PMM: PMM1315(ilvC) PMT: PMT0313 CTE: CT0616(ilvC) DRA: DR1519 TTH: TTC0850 AAE: aq_1245(ilvC) TMA: TM0550 MJA: MJ1543(ilvC) MMP: MMP0654(ilvC) MAC: MA3790(ilvC) MMA: MM0668 MTH: MTH1442 MKA: MK0832(ilvC) AFU: AF1985(ilvC) HMA: rrnAC0332(ilvC) PTO: PTO1073 PAB: PAB0889(ilvC) PFU: PF0936 SSO: SSO0576(ilvC-1) SSO1322(ilvC-2) SSO1942(ilvC-3) STO: ST1445 PAI: PAE3298(ilvC) STRUCTURES PDB: 1NP3 1QMG 1YVE REFERENCE 1 [PMID:4388025] Arfin, S.M. and Umbarger, H.E. Purification and properties of the acetohydroxy acid isomeroreductase of Salmonella typhimurium. J. Biol. Chem. 244 (1969) 1118-1127. 2 Hill, R.K., Sawada, S. and Arfin, S.M. Stereochemistry of valine and isoleucine biosynthesis. IV. Synthesis, configuration, and enzymatic specificity of alpha-acetolactate and alpha-aceto-alpha-hydroxybutyrate. Bioorg. Chem. 8 (1979) 175-189. 3 Kiritani, K., Narise, S. and Wagner, R.P. The reductoisomerase of Neurospora crassa. J. Biol. Chem. 241 (1966) 2047-2051. 4 [PMID:5866387] Satyanarayana, T. and Radhakrishnan, A.N. Biosynthesis of valine and isoleucine in plants. 3. Reductoisomerase of Phaseolus radiatus. Biochim. Biophys. Acta 110 (1965) 380-388. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.86 ExPASy - ENZYME nomenclature database: 1.1.1.86 ERGO genome analysis and discovery system: 1.1.1.86 BRENDA, the Enzyme Database: 1.1.1.86 CAS: 9075-02-9 /// ENTRY EC 1.1.1.87 NAME homoisocitrate dehydrogenase 2-hydroxy-3-carboxyadipate dehydrogenase 3-carboxy-2-hydroxyadipate dehydrogenase homoisocitric dehydrogenase (-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase $(decarboxylating) 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase $(decarboxylating) REACTION (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+ SUBSTRATE (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate NAD+ PRODUCT 2-oxoadipate CO2 NADH H+ COMMENT Forms part of the lysine biosynthesis pathway in fungi [3]. REFERENCE 1 [PMID:4284830] Strassman, M. and Ceci, L.N. Enzymatic formation of a-ketoadipic acid from homoisocitric acid. J. Biol. Chem. 240 (1965) 4357-4361. 2 [PMID:4395693] Rowley, B. and Tucci, A.F. Homoisocitric dehydrogenase from yeast. Arch. Biochem. Biophys. 141 (1970) 499-510. 3 [PMID:10714900] Zabriskie, T.M. and Jackson, M.D. Lysine biosynthesis and metabolism in fungi. Nat. Prod. Rep. 17 (2000) 85-97. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.87 ExPASy - ENZYME nomenclature database: 1.1.1.87 ERGO genome analysis and discovery system: 1.1.1.87 BRENDA, the Enzyme Database: 1.1.1.87 CAS: 37250-23-0 /// ENTRY EC 1.1.1.88 NAME hydroxymethylglutaryl-CoA reductase beta-hydroxy-beta-methylglutaryl coenzyme A reductase beta-hydroxy-beta-methylglutaryl CoA-reductase 3-hydroxy-3-methylglutaryl coenzyme A reductase hydroxymethylglutaryl coenzyme A reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-mevalonate:NAD+ oxidoreductase (CoA-acylating) REACTION (R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+ SUBSTRATE (R)-mevalonate CoA NAD+ PRODUCT 3-hydroxy-3-methylglutaryl-CoA NADH H+ GENES HSA: 3156(HMGCR) CAL: orf19.1031(HMG1) BBA: Bd1627 SAR: SAR2625(mvaA) SAS: SAS2431 DISEASE MIM: 142910 3-hydroxy-3-methylglutaryl-Coenzyme A reductase; MOTIF PS: PS00066 [RKH]-x(6)-D-x-M-G-x-N-x-[LIVMA] PS: PS00318 [LIVM]-G-x-[LIVM]-G-G-[AG]-T PS: PS01192 A-[LIVM]-x-[STAN]-x(2)-[LI]-x-[KRNQ]-[GSA]-H-[LM]-x- [FYLH] PS: PS50065 Hydroxymethylglutaryl- coenzyme A reductases family profile STRUCTURES PDB: 1R31 1R7I 1T02 REFERENCE 1 Fimognari, G.M. and Rodwell, V.W. Substrate-competitive inhibition of bacterial mevalonate:nicotinamide-adenine dinucleotide oxidoreductase (acylating CoA). Biochemistry 4 (1965) 2086-2090. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.88 ExPASy - ENZYME nomenclature database: 1.1.1.88 ERGO genome analysis and discovery system: 1.1.1.88 BRENDA, the Enzyme Database: 1.1.1.88 CAS: 37250-24-1 /// ENTRY EC 1.1.1.89 Obsolete NAME Deleted entry CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Deleted entry: dihydroxyisovalerate dehydrogenase (isomerizing). Now included with EC 1.1.1.86 ketol-acid reductoisomerase (EC 1.1.1.89 created 1972, deleted 1976) DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.89 ExPASy - ENZYME nomenclature database: 1.1.1.89 ERGO genome analysis and discovery system: 1.1.1.89 BRENDA, the Enzyme Database: 1.1.1.89 /// ENTRY EC 1.1.1.90 NAME aryl-alcohol dehydrogenase p-hydroxybenzyl alcohol dehydrogenase benzyl alcohol dehydrogenase coniferyl alcohol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME aryl-alcohol:NAD+ oxidoreductase REACTION an aromatic alcohol + NAD+ = an aromatic aldehyde + NADH + H+ SUBSTRATE aromatic alcohol NAD+ PRODUCT aromatic aldehyde NADH H+ COMMENT A group of enzymes with broad specificity towards primary alcohols with an aromatic or cyclohex-1-ene ring, but with low or no activity towards short-chain aliphatic alcohols. PATHWAY PATH: map00350 Tyrosine metabolism PATH: map00360 Phenylalanine metabolism PATH: map00621 Biphenyl degradation PATH: map00622 Toluene and xylene degradation PATH: map00930 Caprolactam degradation ORTHOLOG KO: K00055 aryl-alcohol dehydrogenase GENES ACI: ACIAD1429(areB) ACIAD1578 NEU: NE0742 CCR: CC2396 BHA: BH2011 LPL: lp_3054 SCO: SCO6442(SC9B5.09) SCO6782(SC6A5.31c) MOTIF PS: PS00059 G-H-E-x(2)-G-x(5)-[GA]-x(2)-[IVSAC] STRUCTURES PDB: 1F8F REFERENCE 1 [PMID:5778658] Suhara, K., Takemori, S. and Katagiri, M. The purification and properties of benzylalcohol dehydrogenase from Pseudomonas sp. Arch. Biochem. Biophys. 130 (1969) 422-429. 2 Yamanaka, K. and Minoshima, R. Identification and characterization of a nicotinamide adenine dinucleotide-dependent para-hydroxybenzyl alcohol-dehydrogenase from Rhodopseudomonas acidophila M402 Agric. Biol. Chem. 48 (1984) 1161-1171. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.90 ExPASy - ENZYME nomenclature database: 1.1.1.90 ERGO genome analysis and discovery system: 1.1.1.90 UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.90 BRENDA, the Enzyme Database: 1.1.1.90 CAS: 37250-26-3 /// ENTRY EC 1.1.1.91 NAME aryl-alcohol dehydrogenase (NADP+) aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide $phosphate) coniferyl alcohol dehydrogenase NADPH-linked benzaldehyde reductase aryl-alcohol dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME aryl-alcohol:NADP+ oxidoreductase REACTION an aromatic alcohol + NADP+ = an aromatic aldehyde + NADPH + H+ SUBSTRATE aromatic alcohol NADP+ PRODUCT aromatic aldehyde NADPH H+ COMMENT Also acts on some aliphatic aldehydes, but cinnamaldehyde was the best substrate found. GENES CAL: orf19.1048(IFD1) orf19.3311 orf19.4476(IFD6) orf19.4477(IFD4) orf19.629 orf19.771 CGL: NCgl0099(Cgl0100) REFERENCE 1 [PMID:4389864] Gross, G.G. and Zenk, M.H. Reduktionaromatische Sauren zu Aldehyden und Alkoholen im zellfreien System. 2. Reinigung und Eigenschaften von Aryl Alkohol:NADP-Oxidoreductase aus Neurospora crassa. Eur. J. Biochem. 8 (1969) 420-425. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.91 ExPASy - ENZYME nomenclature database: 1.1.1.91 ERGO genome analysis and discovery system: 1.1.1.91 BRENDA, the Enzyme Database: 1.1.1.91 CAS: 37250-27-4 /// ENTRY EC 1.1.1.92 NAME oxaloglycolate reductase (decarboxylating) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-glycerate:NAD(P)+ oxidoreductase (carboxylating) REACTION D-glycerate + NAD(P)+ + CO2 = 2-hydroxy-3-oxosuccinate + NAD(P)H + 2 H+ SUBSTRATE D-glycerate NAD+ NADP+ CO2 PRODUCT 2-hydroxy-3-oxosuccinate NADH NADPH H+ COMMENT Also reduces hydroxypyruvate to D-glycerate and glyoxylate to glycolate. PATHWAY PATH: map00630 Glyoxylate and dicarboxylate metabolism REFERENCE 1 [PMID:4385076] Kohn, L.D. and Jakoby, W.B. Tartaric acid metabolism. VI. Crystalline oxaloglycolate reductive decarboxylase. J. Biol. Chem. 243 (1968) 2486-2493. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.92 ExPASy - ENZYME nomenclature database: 1.1.1.92 ERGO genome analysis and discovery system: 1.1.1.92 BRENDA, the Enzyme Database: 1.1.1.92 CAS: 37250-28-5 /// ENTRY EC 1.1.1.93 NAME tartrate dehydrogenase mesotartrate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME tartrate:NAD+ oxidoreductase REACTION tartrate + NAD+ = oxaloglycolate + NADH + H+ SUBSTRATE tartrate NAD+ PRODUCT oxaloglycolate NADH H+ COMMENT meso-tartrate and (R,R)-tartrate act as substrates. Requires Mn2+ and a monovalent cation. PATHWAY PATH: map00630 Glyoxylate and dicarboxylate metabolism ORTHOLOG KO: K00056 tartrate dehydrogenase GENES ECO: b1800(yeaU) ECJ: JW1789(ttuC) ECE: Z2843(yeaU) ECS: ECs2509 YPE: YPO2496 YPK: y1692 YPM: YP2311(leuB1) YPS: YPTB2532 PST: PSPTO2662 RSO: RS02169(ttuC) RS02328(ttuC2) BMA: BMAA0011(ttuC) BPS: BPSS0011 BPE: BP2291 BPA: BPP2437 BPP4066 BBR: BB1886 BB4539 MLO: mll7044 SME: SMa1846 ATU: Atu3402 ATC: AGR_L_2841 BJA: blr2916 blr6570 RPA: RPA1742(yeaU) BHA: BH1070 BLI: BL03389(ycsA) OIH: OB0661 STH: STH2344 MOTIF PS: PS00470 [NS]-[LIMYT]-[FYDN]-G-[DNGST]-[IMVY]-x-[STGDN]-[DN]- x(2)-[SGAP]-x(3,4)-G-[STG]-[LIVMPA]-G-[LIVMF] REFERENCE 1 [PMID:4297261] Kohn, L.D., Packman, P.M., Allen, R.H. and Jakoby, W.B. Tartaric acid metabolism. V. Crystalline tartrate dehydrogenase. J. Biol. Chem. 243 (1968) 2479-2485. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.93 ExPASy - ENZYME nomenclature database: 1.1.1.93 ERGO genome analysis and discovery system: 1.1.1.93 BRENDA, the Enzyme Database: 1.1.1.93 CAS: 37250-29-6 /// ENTRY EC 1.1.1.94 NAME glycerol-3-phosphate dehydrogenase [NAD(P)+] L-glycerol-3-phosphate:NAD(P) oxidoreductase glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide $(phosphate)) glycerol 3-phosphate dehydrogenase (NADP) glycerol-3-phosphate dehydrogenase [NAD(P)] CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME sn-glycerol-3-phosphate:NAD(P)+ 2-oxidoreductase REACTION sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+ SUBSTRATE sn-glycerol 3-phosphate NAD+ NADP+ PRODUCT glycerone phosphate NADH NADPH H+ PATHWAY PATH: map00561 Glycerolipid metabolism ORTHOLOG KO: K00057 glycerol-3-phosphate dehydrogenase (NAD(P)+) GENES ECO: b3608(gpsA) ECJ: JW3583(gpsA) ECE: Z5035(gpsA) ECS: ECs4486 ECC: c4430(gpsA) STY: STY4095(gpsA) STT: t3819(gpsA) STM: STM3700(gpsA) YPE: YPO0068(gpsA) YPK: y0073(gpsA) YPM: YP0068(gpsA) YPS: YPTB0064(gpsA) SFL: SF3647(gpsA) SFX: S4121(gpsA) ECA: ECA0173(gpsA) PLU: plu4838(gpsA) WBR: Wbr0214(gpsA) BFL: Bfl604(gpsA) HIN: HI0605(gpsA) HDU: HD0660(gpsA) PMU: PM1431(gspA) XFA: XF1802 XFT: PD1064(gpsA) XCC: XCC0204(gpdA) XAC: XAC0222(gpdA) VCH: VC2651 VVU: VV11277 VVY: VV3087 VPA: VP2832 PPR: PBPRA0227 PAE: PA1614(gpsA) PPU: PP4169(gpsA) PST: PSPTO2213(gpsA) ACI: ACIAD1317(gpsA) SON: SO0053(gpsA) CBU: CBU1518(gpsA) MCA: MCA2538(gpsA) NME: NMB2060 NMA: NMA0375(gpsA) CVI: CV1129(gpsA) RSO: RS03324 BMA: BMA3204(gpsA) BPS: BPSL0447(gpsA) BPE: BP0603(gpsA) BPA: BPP0291(gpsA) BBR: BB0294(gpsA) NEU: NE2208(gpsA) HPY: HP0961 HPJ: jhp0895 HHE: HH0794(gpsA) WSU: WS2004 CJE: Cj1196c(gpsA) GSU: GSU0006(gpsA) DVU: DVU3159(gpsA) DPS: DP0651 RPR: RP442(gpsA) RTY: RT0429(gpsA) RCO: RC0615(gpsA) MLO: mlr4225 SME: SMc03229(gpsA) ATU: Atu2650(gpsA) ATC: AGR_C_4804 BME: BMEI0174 BMS: BR1889(gpsA) BJA: blr0568(gpsA) RPA: RPA0254(gpdA) BHE: BH01260(gpsA) BQU: BQ01190(gpsA) CCR: CC0070 BSU: BG11366(gpsA) BHA: BH1640(gpsA) BAN: BA1526(gpsA) BAR: GBAA1526(gpsA) BAA: BA_2046 BAT: BAS1415 BCE: BC1505 BCA: BCE1632(gpsA) BCZ: BTZK1387(gpsA) BTK: BT9727_1387(gpsA) BLI: BL02791(gpsA) OIH: OB1796(gpsA) SAU: SA1306(gpsA) SAV: SAV1474(gpsA) SAM: MW1363(gpsA) SAR: SAR1483(gpsA) SAS: SAS1415 SEP: SE1162 LMO: lmo1936(gpsA) LMF: LMOf2365_1965(gpsA) LIN: lin2050(gpsA) LLA: L0016(gpdA) SPY: SPy0226(gpsA) SPM: spyM18_0212(gpdA) SPG: SpyM3_0161(gpdA) SPS: SPs0167 SPA: M6_Spy0225 SPN: SP2091 SPR: spr1902(gpdA) SAG: SAG0407(gpsA) SAN: gbs0442 SMU: SMU.323(gpsA) LPL: lp_0756(gspA) LJO: LJ0851 EFA: EF1747(gpsA) CAC: CAC1712(gpsA) CPE: CPE1754(gpdA) CTC: CTC01034 CTC01139 TTE: TTE1617(gpsA) MPU: MYPU_1240(gpsA) MPE: MYPE2300(gpsA) MGA: MGA_1133(GpsA) MMY: MSC_0409(gpsA) MMO: MMOB4820(gpsA) UUR: UU382(gpsA) POY: PAM241(gpsA) MTU: Rv0564c(gpdA1) Rv2982c(gpdA2) MTC: MT0590 MT3060 MBO: Mb0579c(gpdA1) Mb3006c(gpdA2) MLE: ML1679(gpdA) MPA: MAP3020c(gpdA2) MAP4061c(gpdA1) CGL: NCgl1266(Cgl1320) CEF: CE1430 CDI: DIP1130(gpsA) SCO: SCO5559(SC7A1.03) SMA: SAV2680(gpsA) TWH: TW506(gpsA) TWS: TW256(gpsA) LXX: Lxx09700(gpdA) PAC: PPA2315 BLO: BL0346 STH: STH1681 FNU: FN0906 CTR: CT714(gpdA) CMU: TC0087 CPN: CPn0855 CPA: CP1014 CPJ: CPj0855(gpdA) CPT: CpB0884 CCA: CCA00912(gpdA) PCU: pc0083(gpsA) BBU: BB0368(gpsA) TPA: TP1009 TDE: TDE2090 LIL: LA1112(gpsA1) LA3939(gpsA2) LA4264(gpsA3) LIC: LIC12563 LIC13145(gpsA) LIC13412(plsB) BTH: BT2123 PGI: PG1369(gpsA) SYN: slr1755(gpsA) TEL: tll2111 GVI: glr3667(glpD) ANA: all1693 CTE: CT0092(gpsA) DRA: DR2621 TTH: TTC1378 AAE: aq_1634(gspA) MTH: MTH368 AFU: AF0871(gpsA) MOTIF PS: PS00957 G-[ATIV]-[LIVMYC]-K-[DN]-[LIVM]-[LIVMFY]-[GA]-x-[GA]-x- G-[LIVMF]-x(2)-[SGA]-[LIVM]-x-[LIVMFYW]-G-x-N STRUCTURES PDB: 1TXG REFERENCE 1 [PMID:4389388] Kito, M. and Pizer, L.I. Purification and regulatory properties of the biosynthetic L-glycerol 3-phosphate dehydrogenase from Escherichia coli. J. Biol. Chem. 244 (1969) 3316-3323. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.94 ExPASy - ENZYME nomenclature database: 1.1.1.94 ERGO genome analysis and discovery system: 1.1.1.94 BRENDA, the Enzyme Database: 1.1.1.94 CAS: 37250-30-9 /// ENTRY EC 1.1.1.95 NAME phosphoglycerate dehydrogenase D-3-phosphoglycerate:NAD oxidoreductase alpha-phosphoglycerate dehydrogenase 3-phosphoglycerate dehydrogenase 3-phosphoglyceric acid dehydrogenase D-3-phosphoglycerate dehydrogenase glycerate 3-phosphate dehydrogenase glycerate-1,3-phosphate dehydrogenase phosphoglycerate oxidoreductase phosphoglyceric acid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3-phosphoglycerate:NAD+ 2-oxidoreductase REACTION 3-phosphoglycerate + NAD+ = 3-phosphohydroxypyruvate + NADH + H+ SUBSTRATE 3-phosphoglycerate NAD+ PRODUCT 3-phosphohydroxypyruvate NADH H+ PATHWAY PATH: map00260 Glycine, serine and threonine metabolism ORTHOLOG KO: K00058 D-3-phosphoglycerate dehydrogenase GENES HSA: 26227(PHGDH) MMU: 236539(Phgdh) RNO: 58835(Phgdh) DME: CG1236-PA(CG1236) CG6287-PA(CG6287) CEL: C31C9.2 ATH: At3g19480(MLD14.34) At4g34200(F28A23.40) CME: CMC149C SCE: YER081W(SER3) YIL074C(SER33) AGO: ACL032C(ACL032Cp) CAL: orf19.1796 orf19.2176 orf19.3584 orf19.5263(SER3) SPO: SPCC4G3.01 ECO: b2913(serA) ECJ: JW2880(serA) ECE: Z4251(serA) ECS: ECs3784 ECC: c3494(serA) STY: STY3218(serA) STT: t2980(serA) STM: STM3062(serA) YPE: YPO0914(serA) YPO1288 YPK: y2896 y3301(serA) YPM: YP1303(serA1) YP3611(serA2) YPS: YPTB1320 YPTB3189(serA) SFL: SF2898(serA) SFX: S3098(serA) ECA: ECA3905(serA) PLU: plu3605(serA) HIN: HI0465(serA) PMU: PM1671(serA) XFA: XF2206 XFT: PD1255(serA) XCC: XCC1825(serA) XAC: XAC1844(serA) VCH: VC2481 VVU: VV11546 VVY: VV2851 VPA: VP2593 PPR: PBPRA3123 PBPRA3124 PAE: PA0316(serA) PPU: PP5155(serA) PST: PSPTO5294(serA) ACI: ACIAD3302(serA) SON: SO0862(serA) CBU: CBU1732 LPN: lpg0242(serA) CVI: CV1724 RSO: RS00384(serA2) BPS: BPSL1250(serA) BPE: BP0155(serA) BPA: BPP4001(serA) BBR: BB4474(serA) BB4731 NEU: NE0334 NE1688(serA) HPY: HP0096 HP0397(serA) HPJ: jhp0088 jhp0984 HHE: HH0135(serA) HH0178 WSU: WS1313(serA) WS2143 CJE: Cj0891c(serA) GSU: GSU1198(serA) DVU: DVU0339 BBA: Bd1461(serA) Bd2892(serA) DPS: DP1709 MLO: mll1021 mll3875 mlr3367 mlr7269 SME: SMa1347 SMc00641(serA) SMc01622 ATU: Atu3706(serA) ATC: AGR_L_2264 BME: BMEI0349 BMEII0813 BMS: BR1685(serA-1) BRA0453(serA-2) BJA: bll7401(serA) bll7965 blr3173 RPA: RPA1744(serA) RPA2975(serA1) RPA4308(serA2) CCR: CC3215 BSU: BG10509(serA) BG13475(yoaD) BHA: BH1602 BAN: BA3320 BAR: GBAA3320 BAA: BA_3822 BAT: BAS3078 BCE: BC3248 BCA: BCE3284 BCZ: BTZK1299(serA) BTZK2968(serA) BTK: BT9727_3022(serA) BLI: BL00647(serA) OIH: OB2626(serA) SAU: SA1545(serA) SAV: SAV1724(serA) SAM: MW1666(serA) SAR: SAR1801 SAS: SAS1650 SEP: SE1401 LMO: lmo2824 LMF: LMOf2365_2815 LIN: lin2956 LLA: L0084(serA) SAG: SAG1566 SAN: gbs1619 SMU: SMU.1653(serA) LPL: lp_0203(serA1) lp_2790(serA3) CAC: CAC0015(serA) CAC0089(serA) CPE: CPE0054(serA) CTC: CTC00694 TTE: TTE2613(serA2) MTU: Rv0728c Rv2996c(serA) MTC: MT0753 MT3074 MBO: Mb0749c(serA2) Mb3020c(serA1) MLE: ML1692(serA) MPA: MAP3033c(serA) MAP4194c CGL: NCgl1235(Cgl1284) CEF: CE1379 CDI: DIP1104(serA) SCO: SCO5515(SC8D9.27) SMA: SAV2730(serA) SAV7481 LXX: Lxx13140(serA) PAC: PPA1272 PPA2251 BLO: BL1313(serA) STH: STH9 FNU: FN0965 RBA: RB10004(serA) RB6248(serA) RB6394 LIL: LA1126 LA1629 LA1911(serA) LIC: LIC11992(serA) LIC12153 LIC12554 BTH: BT1152 PGI: PG1279 SYN: sll1908(serA) SYW: SYNW0533(serA) SYC: syc2486_c(serA) TEL: tlr0325(serA) GVI: glr2139(serA) ANA: alr1890 PMA: Pro1436(serA) PMM: PMM1354(serA) PMT: PMT1431(serA) DRA: DR1291 TTH: TTC0586 TTC1209 AAE: aq_1905(serA) TMA: TM0327 TM1401 MJA: MJ1018(serA) MMP: MMP1588(serA) MAC: MA0592(serA) MMA: MM1753 MTH: MTH970 MKA: MK0297 MK0319 MK0320(serA) AFU: AF0813(serA) HAL: VNG2424G(serA1) HMA: rrnAC0362(serA4) rrnAC1762(serA2) rrnAC2056(serA3) rrnAC2451(serA5) rrnAC2696(serA1) PTO: PTO0372 PHO: PH0520 PH1387 PAB: PAB0514(serA-like) PAB1008 PFU: PF0370 PF1394 SSO: SSO0905(serA-1) SSO3187(serA-2) STO: ST0694 ST1218 PAI: PAE1038(serA) PAE3320(serA) DISEASE MIM: 606879 Phosphoglycerate dehydrogenase MOTIF PS: PS00065 [LIVMA]-[AG]-[IVT]-[LIVMFY]-[AG]-x-G-[NHKRQGSAC]-[LIV]- G-x(13,14)-[LIVMFT]-x(2)-[FYWCTH]-[DNSTK] PS: PS00670 [LIVMFYWA]-[LIVFYWC]-x(2)-[SAC]-[DNQHR]-[IVFA]-[LIVF]- x-[LIVF]-[HNI]-x-P-x(4)-[STN]-x(2)-[LIVMF]-x-[GSDN] PS: PS00671 [LMFATC]-[KPQ]-x-[GSTDN]-x-[LIVMFYWR]-[LIVMFYW](2)-N-x- [STAGC]-R-[GP]-x-[LIVH]-[LIVMC]-[DNV] STRUCTURES PDB: 1PSD REFERENCE 1 [PMID:4384871] Sugimoto, E. and Pizer, L.I. The mechanism of end product inhibition of serine biosynthesis. I. Purification and kinetics of phosphoglycerate dehydrogenase. J. Biol. Chem. 243 (1968) 2081-1089. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.95 ExPASy - ENZYME nomenclature database: 1.1.1.95 ERGO genome analysis and discovery system: 1.1.1.95 BRENDA, the Enzyme Database: 1.1.1.95 CAS: 9075-29-0 /// ENTRY EC 1.1.1.96 NAME diiodophenylpyruvate reductase aromatic alpha-keto acid KAR 2-oxo acid reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3-(3,5-diiodo-4-hydroxyphenyl)lactate:NAD+ oxidoreductase REACTION 3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD+ = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH + H+ SUBSTRATE 3-(3,5-diiodo-4-hydroxyphenyl)lactate NAD+ PRODUCT 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate NADH H+ COMMENT Substrates contain an aromatic ring with a pyruvate side chain. The most active substrates are halogenated derivatives. Compounds with hydroxy or amino groups in the 3 or 5 position are inactive. REFERENCE 1 [PMID:5935348] Zannoni, V.G. and Weber, W.W. Isolation and properties of aromatic alpha-keto acid reductase. J. Biol. Chem. 241 (1966) 1340-1344. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.96 ExPASy - ENZYME nomenclature database: 1.1.1.96 ERGO genome analysis and discovery system: 1.1.1.96 BRENDA, the Enzyme Database: 1.1.1.96 CAS: 37250-31-0 /// ENTRY EC 1.1.1.97 NAME 3-hydroxybenzyl-alcohol dehydrogenase m-hydroxybenzyl alcohol dehydrogenase m-hydroxybenzyl alcohol (NADP) dehydrogenase m-hydroxybenzylalcohol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3-hydroxybenzyl-alcohol:NADP+ oxidoreductase REACTION 3-hydroxybenzyl alcohol + NADP+ = 3-hydroxybenzaldehyde + NADPH + H+ SUBSTRATE 3-hydroxybenzyl alcohol NADP+ PRODUCT 3-hydroxybenzaldehyde NADPH H+ REFERENCE 1 [PMID:4335290] Forrester, P.I. and Gaucher, G.M. m-Hydroxybenzyl alcohol dehydrogenase from Penicillium urticae. Biochemistry 11 (1972) 1108-1114. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.97 ExPASy - ENZYME nomenclature database: 1.1.1.97 ERGO genome analysis and discovery system: 1.1.1.97 BRENDA, the Enzyme Database: 1.1.1.97 CAS: 9075-73-4 /// ENTRY EC 1.1.1.98 NAME (R)-2-hydroxy-fatty-acid dehydrogenase D-2-hydroxy fatty acid dehydrogenase 2-hydroxy fatty acid oxidase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-2-hydroxystearate:NAD+ oxidoreductase REACTION (R)-2-hydroxystearate + NAD+ = 2-oxostearate + NADH + H+ SUBSTRATE (R)-2-hydroxystearate NAD+ PRODUCT 2-oxostearate NADH H+ REFERENCE 1 [PMID:5443694] Levis, G.M. 2-Hydroxy fatty acid oxidases of rat kidney. Biochem. Biophys. Res. Commun. 38 (1970) 470-477. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.98 ExPASy - ENZYME nomenclature database: 1.1.1.98 ERGO genome analysis and discovery system: 1.1.1.98 BRENDA, the Enzyme Database: 1.1.1.98 CAS: 37250-32-1 /// ENTRY EC 1.1.1.99 NAME (S)-2-hydroxy-fatty-acid dehydrogenase dehydrogenase, L-2-hydroxy fatty acid L-2-hydroxy fatty acid dehydrogenase 2-hydroxy fatty acid oxidase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S)-2-hydroxystearate:NAD+ oxidoreductase REACTION (S)-2-hydroxystearate + NAD+ = 2-oxostearate + NADH + H+ SUBSTRATE (S)-2-hydroxystearate NAD+ PRODUCT 2-oxostearate NADH H+ REFERENCE 1 [PMID:4909888] Huang, W.Y. and Tang, J. Carboxyl-terminal sequence of human gastricsin and pepsin. J. Biol. Chem. 245 (1970) 2189-2193. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.99 ExPASy - ENZYME nomenclature database: 1.1.1.99 ERGO genome analysis and discovery system: 1.1.1.99 BRENDA, the Enzyme Database: 1.1.1.99 CAS: 37250-33-2 /// ENTRY EC 1.1.1.100 NAME 3-oxoacyl-[acyl-carrier-protein] reductase beta-ketoacyl-[acyl-carrier protein](ACP) reductase beta-ketoacyl acyl carrier protein (ACP) reductase beta-ketoacyl reductase beta-ketoacyl thioester reductase beta-ketoacyl-ACP reductase beta-ketoacyl-acyl carrier protein reductase 3-ketoacyl acyl carrier protein reductase NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase 3-oxoacyl-[ACP]reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase REACTION (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = 3-oxoacyl-[acyl-carrier protein] + NADPH + H+ SUBSTRATE (3R)-3-hydroxyacyl-[acyl-carrier protein] NADP+ PRODUCT 3-oxoacyl-[acyl-carrier protein] NADPH H+ COMMENT Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates. PATHWAY PATH: map00061 Fatty acid biosynthesis (path 1) ORTHOLOG KO: K00059 3-oxoacyl-[acyl-carrier protein] reductase GENES HSA: 2194(FASN) RNO: 50671(Fasn) CEL: F09E10.3 F32H2.5 ATH: At1g24360(F21J9.2) At3g03980(T11I18.9) At4g13180(F17N18.70) CME: CMS393C SCE: YPL231W(FAS2) AGO: AFL138W(AFL138Wp) CAL: orf19.271(SPS21) orf19.3283(OAR1) orf19.5949(FAS2) orf19.6838(SPS24) SPO: SPAC4A8.11c(fas2) PFA: PFI1125c ECO: b1093(fabG) ECJ: JW1079(fabG) ECE: Z1732(fabG) Z4865 ECS: ECs1471 ECs4340 ECC: c1187 c5303 STY: STY1234(fabG) STT: t1725(fabG) STM: STM1195(fabG) YPE: YPO1456 YPO1599(fabG) YPK: y1758(fabG) y2713(fabG) YPM: YP1348(fabG6) YP2255(fabG10) YPS: YPTB1474 YPTB2471(fabG) SFL: SF1097(fabG) SFX: S1177(fabG) ECA: ECA1797(fabG) ECA4492 PLU: plu1541 plu2833(fabG) plu4678 BUC: BU351(fabG) BAS: BUsg339(fabG) BAB: bbp321(fabG) WBR: Wbr0036(fabG) BFL: Bfl404(fabG) HIN: HI0155(fabG) HDU: HD0708(fabG) PMU: PM1916(fabG) XFA: XF0173 XF0671 XFT: PD0141(fabG) PD1503(fabG) XCC: XCC0384 XCC1018(fabG) XCC4003(fabG) XAC: XAC0083 XAC0384 XAC1127(fabG) XAC4090(fabG) VCH: VC2021 VVU: VV10060 VV13009 VV20488 VVY: VV1067 VV1275 VVA1037 VPA: VP0882 VP2054 VPA0626 VPA1117 VPA1304 PPR: PBPRA1195(fabG) PBPRB0105(fabG-2) PBPRB1106(fabG2) PBPRB1562(fabG) PBPRB1667 PAE: PA1470 PA2967(fabG) PA3387(rhlG) PA4389 PA5524 PPU: PP1914(fabG) PP2540 PP2783 PST: PSPTO3832(fabG) PSPTO4380 PSPTO5109 ACI: ACIAD0042 ACIAD0582(fabG) ACIAD0871(fabG) SON: SO1683 SO2776(fabG-1) SO4382(fabG-2) CBU: CBU0495(fabG) CBU0702 CBU1514 LPN: lpg1395(fabG) lpg2231(fabG) MCA: MCA2001(fabG) NME: NMB1702 NMB1921 NMA: NMA0533(fabG) CVI: CV1546 CV2707 CV3414(fabG1) CV3576(fabG2) CV3947 RSO: RS00769(fabG2) RS01413 RS03404 RS04176(fabG1) RS05466 BMA: BMA0532(fabG) BPS: BPSL2440(fabG) BPE: BP0813 BP1128(fabG) BP1668 BP1672(fabG) BP1785(fabG) BP2441(fabG) BP2554(fabG) BP3010 BPA: BPP0607 BPP1392 BPP2016(fabG) BPP2100 BPP2625(fabG) BPP3213(fabG) BPP3305(fabG) BPP3417 BPP3739 BBR: BB0613 BB1496 BB2068(fabG) BB2264(fabG) BB2461 BB3665(fabG) BB3756(fabG) BB3867 BB4185 BB4764(fabG) BB4780 NEU: NE1648(fabG1) HPY: HP0561(fabG) HPJ: jhp0508 HHE: HH0732(fabG) WSU: WS0631(fabG) CJE: Cj0435(fabG) GSU: GSU0461(fabG-1) GSU1603(fabG-2) DVU: DVU1206(fabG) BBA: Bd0281(fabG) Bd0405(fabG) Bd0506 Bd1969(fabG) Bd2012(fabG) Bd3814(linC) DPS: DP1847 DP2407 DP2790 RPR: RP762(fabG) RTY: RT0748(fabG) RCO: RC1183(fabG) WOL: WD0650(fabG) MLO: mll1017 mll1981 mll5243 mlr0808 mlr6807 mlr7850 SME: SMa0854(nodG) SMa0959 SMb20493 SMb21474 SMc00572(fabG) SMc01157 ATU: Atu0990 Atu1095(fabG) Atu3333 Atu3531(fabG) Atu3813(fabG) Atu4595 Atu4877 Atu5122(fabG) ATC: AGR_C_1817 AGR_C_2026 AGR_L_2039 AGR_L_2601 AGR_L_28 AGR_L_2975 AGR_L_561 AGR_pAT_178 BME: BMEI0026 BMEI0032 BMEI1250 BMEI1477 BMEII0063 BMEII0514 BMS: BR0458(fabG) BR2039 BRA0030 BJA: bll1230 bll2747(fabG) bll3913(fabG) bll4020 bll6359 bll7782 bll7880 bll7886 blr1495 blr1893(fabG) blr3403 blr4083(fabG) blr5634 blr6288 blr7888 RPA: RPA0109 RPA0479(fabG1) RPA0895 RPA0896 RPA1110 RPA1683 RPA1684 RPA1757 RPA2072 RPA2160 RPA3074(fabG2) RPA3304(fabG3) RPA3474(fabG4) RPA3631 RPA4596(fabG5) RPA4633(fixR2) RPA4657(kduD) BHE: BH05350(fabG) BQU: BQ04530(fabG) CCR: CC1675 CC2836 BSU: BG11535(fabG) BG13173(yjdA) BG13429(ymfI) BG13870(ytkK) BG14030(yusR) BG14031(yusS) BG14063(yvaG) BG14144(yvrD) BHA: BH0506 BH0932 BH1842 BH2391 BH2491(fabG) BH3182 BH3896 BAN: BA3385 BA3440 BA3610 BA3921 BA3989(fabG) BA4874 BAR: GBAA3385 GBAA3440 GBAA3610 GBAA3921 GBAA3989(fabG) GBAA4874 BAA: BA_0755 BA_3884 BA_3937 BA_4102 BA_4392 BA_4460 BA_5295 BAT: BAS0174 BAS3138 BAS3188 BAS3349 BAS3635 BAS3702 BAS4522 BCE: BC0195 BC1062 BC1958 BC3327 BC3382 BC3556 BC3785 BC3849 BC4624 BCA: BCE0194 BCE3355 BCE3570 BCE3820 BCE3893(fabG) BCE4759 BCZ: BTZK0164(fabG) BTZK1209(phaB) BTZK1775(fabG) BTZK3032 BTZK3090 BTZK3264 BTZK3545(fabG) BTZK3610(fabG) BTZK4369(fabG) BTK: BT9727_0164 BT9727_1793(fabG) BT9727_3125 BT9727_3169 BT9727_3314 BT9727_3527(fabG) BT9727_3592(fabG) BT9727_4358(fabG) BLI: BL00414(ytkK) BL00741(yvrD) BL02315(fabG) BL02426 BL03119(yvaG) BL03573 BLD: BLi00319 BLi03500 OIH: OB0671 OB1524(fabG) OB1618 OB1843 OB2792 OB3475 SAU: SA1074(fabG) SA1123 SAV: SAV1231(fabG) SAV1280 SAM: MW1114(fabG) MW1163 SAR: SAR1207(fabG) SAR1256 SAS: SAS1165 SAS1214 SEP: SE0324 SE0906 SE0957 LMO: lmo1394 lmo1807(fabG) lmo2815 LMF: LMOf2365_1413 LMOf2365_1835(fabG) LMOf2365_2806 LIN: lin1431 lin1921(fabG) lin2948 LLA: L0185(fabG1) L1530(yiaB) L27694(fabG2) SPY: SPy0440 SPy1749(fabG) SPM: spyM18_0483 spyM18_1821 SPG: SpyM3_0309 SpyM3_1523(fabG) SPS: SPs0343 SPs1548 SPA: M6_Spy0383 M6_Spy1484 SPN: SP0421 SP0793 SPR: spr0381(fabG) spr0701(fabG) SAG: SAG0348(fabG) SAG0664(cylG) SAG1544 SAN: gbs0335 gbs0646(cylG) gbs1600 SMU: SMU.1740(fabG) LPL: lp_0159 lp_1674(fabG1) lp_2764 LJO: LJ0836 EFA: EF1667 EF1773 EF2881(fabG) CAC: CAC2626(fabG) CAC3462(fabG) CAC3574(fabG) CPE: CPE1070(fabG) CPE1927 CTC: CTC00130 CTC00798 TTE: TTE0051(fabG) TTE1472(fabG3) TTE2234(fabG5) TTE2709(fabG6) MTU: Rv0769 Rv1350(fabG2) Rv1483(fabG1) Rv3502c Rv3559c MTC: MT0793 MT1393 MT1530 MT3606 MT3664 MBO: Mb0248c(fabG4) Mb1385(fabG2) Mb1519(fabG1) Mb3532c Mb3589c MLE: ML1807(fabG1) MPA: MAP0508 MAP0561 MAP0603 MAP1209(fabG1) MAP2408c(fabG2_2) MAP3328c CGL: NCgl0281(Cgl0286) NCgl0315(Cgl0321) CEF: CE2778 SCO: SCO0330(SCF12.09) SCO1346(2SCG61.28c) SCO1815(SCI28.09c) SCO1831(SCI8.16) SCO4681(SCD31.06) SMA: SAV2387 SAV3653(fabG2) SAV5872(fabG5) SAV6197 SAV6435 SAV6462(fabG1) SAV7008(fabG3) TWH: TW313(fabG) TWS: TW459(fabG) LXX: Lxx11740(fabG) PAC: PPA1533 PPA1815 BLO: BL0512 STH: STH1990 STH577 STH805 STH968 FNU: FN0216 FN0494 FN0899 RBA: RB11488 RB316(fabG) RB3657 RB4981 RB6240(fabG) RB8029 RB8871(fabG) RB9574(fabG) CTR: CT237(fabG) CMU: TC0508 CPN: CPn0296 CPA: CP0462 CPJ: CPj0296(fabG) CPT: CpB0305 CCA: CCA00486(fabG) PCU: pc1718(fabG) TDE: TDE0598(fabG) LIL: LA0020 LA0225 LA0971 LA1427 LA1975 LA2303 LA2324 LA2621 LA3484 LA4052 LB034 LB041 LB082 LB113 LB121 LB291 LIC: LIC10019 LIC10194 LIC10700 LIC11364(dltE) LIC11618 LIC11634(csgA) LIC11929 LIC12320 LIC12682 LIC13232 LIC20026 LIC20031 LIC20064(fabG) LIC20091 LIC20097 LIC20225 BTH: BT3771 PGI: PG1239(fabG) SYN: slr0886(fabG1) slr1994(phaB) SYW: SYNW1852(fabG) SYC: syc0845_c(fabG) TEL: tlr1502 GVI: glr3506 ANA: alr1894(fabG) PMA: Pro0452(fabG) PMM: PMM0453(fabG) PMT: PMT1333(fabG) CTE: CT2116(fabG) DRA: DR0822 DR1943 TTH: TTC0047 TTC0394 TTC1861 AAE: aq_1716(fabG) TMA: TM1169 TM1724 MAC: MA2687(fabG1) HAL: VNG1341G(fabG) VNG2158G(oxrA) HMA: pNG7030(fabG3) pNG7072(fabG7) pNG7335(fabG5) rrnAC0904(fabG1) rrnAC1984(fabG4) rrnAC3004(fabG6) TAC: Ta0251 Ta0822 TVO: TVG0720035 TVG1417421 PTO: PTO0990 PTO1324 PHO: PH1901 PAB: PAB1085(fabG) PAB2177 PFU: PF0149 PF1899 APE: APE0912 APE2503 SSO: SSO0975(fabG-1) SSO2276(fabG-5) SSO2289(fabG-6) SSO2500(fabG-7) SSO3114(fabG-10) STO: ST0070 ST1109 ST1299 ST1868 ST2239 PAI: PAE0797 PAE2832 NEQ: NEQ306 DISEASE MIM: 600212 Fatty acid synthase MOTIF PS: PS00012 [DEQGSTALMKRH]-[LIVMFYSTAC]-[GNQ]-[LIVMFYAG]-[DNEKHS]- S-[LIVMST]-{PCFY}-[STAGCPQLIVMF]-[LIVMATN]- [DENQGTAKRHLM]-[LIVMWSTA]-[LIVGSTACR]-x(2)-[LIVMFA] PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] PS: PS00606 G-x(4)-[LIVMFTAP]-x(2)-[AGC]-C-[STA](2)-[STAG]-x(3)- [LIVMF] PS: PS50075 Acyl carrier protein phosphopantetheine domain profile STRUCTURES PDB: 1I01 1O5I 1Q7B 1Q7C 1ULS REFERENCE 1 [PMID:4561013] Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269-311. 2 [PMID:6756317] Shimakata, T. and Stumpf, P.K. Purification and characterizations of beta-ketoacyl-[acyl-carrier-protein] reductase, beta-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves. Arch. Biochem. Biophys. 218 (1982) 77-91. 3 [PMID:4381013] Toomey, R.E. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli. Biochim. Biophys. Acta 116 (1966) 189-197. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.100 ExPASy - ENZYME nomenclature database: 1.1.1.100 ERGO genome analysis and discovery system: 1.1.1.100 BRENDA, the Enzyme Database: 1.1.1.100 CAS: 37250-34-3 /// ENTRY EC 1.1.1.101 NAME acylglycerone-phosphate reductase palmitoyldihydroxyacetone-phosphate reductase palmitoyl dihydroxyacetone phosphate reductase palmitoyl-dihydroxyacetone-phosphate reductase acyldihydroxyacetone phosphate reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 1-palmitoylglycerol-3-phosphate:NADP+ oxidoreductase REACTION 1-palmitoylglycerol 3-phosphate + NADP+ = palmitoylglycerone phosphate + NADPH + H+ SUBSTRATE 1-palmitoylglycerol 3-phosphate NADP+ PRODUCT palmitoylglycerone phosphate NADPH H+ COMMENT Also acts on alkylglycerone 3-phosphate and alkylglycerol 3-phosphate. REFERENCE 1 [PMID:4403490] LaBelle, E.F., Jr. and Hajira, A.K. Enzymatic reduction of alkyl and acyl derivatives of dihydroxyacetone phosphate by reduced pyridine nucleotides. J. Biol. Chem. 247 (1972) 5825-5834. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.101 ExPASy - ENZYME nomenclature database: 1.1.1.101 ERGO genome analysis and discovery system: 1.1.1.101 BRENDA, the Enzyme Database: 1.1.1.101 CAS: 37250-35-4 /// ENTRY EC 1.1.1.102 NAME 3-dehydrosphinganine reductase D-3-dehydrosphinganine reductase D-3-oxosphinganine reductase DSR 3-oxosphinganine reductase 3-oxosphinganine:NADPH oxidoreductase D-3-oxosphinganine:B-NADPH oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-erythro-dihydrosphingosine:NADP+ 3-oxidoreductase REACTION sphinganine + NADP+ = 3-dehydrosphinganine + NADPH + H+ SUBSTRATE sphinganine NADP+ PRODUCT 3-dehydrosphinganine NADPH H+ PATHWAY PATH: map00600 Glycosphingolipid metabolism ORTHOLOG KO: K04708 3-dehydrosphinganine reductase GENES SCE: YBR265W(TSC10) AGO: AEL164C(AEL164Cp) TAC: Ta0191 REFERENCE 1 [PMID:4386961] Stoffel, W., Le Kim, D. and Sticht, G. Biosynthesis of dihydrosphingosine in vitro. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 664-670. 2 [PMID:4387676] Stoffel, W., Le Kim, D. and Sticht, G. Metabolism of sphingosine bases. 8. Distribution, isolation and properties of D-3-oxosphinganine reductase. Stereospecificity of the NADPH-dependent reaction of 3-oxodihydrospingosine (2-amino-1-hydroxyoctadecane-3-one). Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1637-1644. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.102 ExPASy - ENZYME nomenclature database: 1.1.1.102 ERGO genome analysis and discovery system: 1.1.1.102 BRENDA, the Enzyme Database: 1.1.1.102 CAS: 37250-36-5 /// ENTRY EC 1.1.1.103 NAME L-threonine 3-dehydrogenase L-threonine dehydrogenase threonine 3-dehydrogenase threonine dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-threonine:NAD+ oxidoreductase REACTION L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+ SUBSTRATE L-threonine NAD+ PRODUCT L-2-amino-3-oxobutanoate NADH H+ COMMENT The product spontaneously decarboxylates to aminoacetone. PATHWAY PATH: map00260 Glycine, serine and threonine metabolism ORTHOLOG KO: K00060 threonine 3-dehydrogenase GENES MMU: 58865(Tdh) CME: CMR237C ECO: b3616(tdh) ECJ: JW3591(tdh) ECE: Z5043(tdh) ECS: ECs4494 ECC: c4443(tdh) STY: STY4087(tdh) STT: t3811(tdh) STM: STM3708(tdh) YPE: YPO0060(tdh) YPK: y0080(tdh) YPM: YP0061(tdh1) YPS: YPTB0057(tdh) SFL: SF3656(tdh) SFX: S4111(tdh) ECA: ECA0168(tdh) PLU: plu4845(tdh) XCC: XCC0945(tdh) XAC: XAC1022(tdh) VCH: VCA0885 VVU: VV21485 VVY: VVA0305 VPA: VPA1509 PPR: PBPRA1730 SON: SO4673(tdh) CBU: CBU0112(tdh) CVI: CV1651(tdh) BMA: BMAA0006(tdh) BPS: BPSS0006(tdh) MLO: mlr8299 SME: SMc01564(tdh) BSU: BG12685(tdh) BLI: BL03658(tdh) TTE: TTE2405(tdh3) SCO: SCO6799(tdh) SMA: SAV1628(tdh) PAC: PPA0402 STH: STH1873 PCU: pc0810(tdh) DRA: DR1662 TTH: TTC0201 PHO: PH0655 PAB: PAB2382 PFU: PF0991 MOTIF PS: PS00059 G-H-E-x(2)-G-x(5)-[GA]-x(2)-[IVSAC] REFERENCE 1 Green, M.L. and Elliott, W.H. The enzymic formation of aminoacetone from threonine and its further metabolism. Biochem. J. 92 (1964) 537-549. 2 Hartshorne, D. and Greenberg, D.M. Studies on liver threonine dehydrogenase. Arch. Biochem. Biophys. 105 (1964) 173-178. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.103 ExPASy - ENZYME nomenclature database: 1.1.1.103 ERGO genome analysis and discovery system: 1.1.1.103 BRENDA, the Enzyme Database: 1.1.1.103 CAS: 9067-99-6 /// ENTRY EC 1.1.1.104 NAME 4-oxoproline reductase hydroxy-L-proline oxidase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 4-hydroxy-L-proline:NAD+ oxidoreductase REACTION 4-hydroxy-L-proline + NAD+ = 4-oxoproline + NADH + H+ SUBSTRATE 4-hydroxy-L-proline NAD+ PRODUCT 4-oxoproline NADH H+ PATHWAY PATH: map00330 Arginine and proline metabolism REFERENCE 1 Smith, T.E. and Mitoma, C. Partial purification and some properties of 4-ketoproline reductase. J. Biol. Chem. 237 (1962) 1177-1180. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.104 ExPASy - ENZYME nomenclature database: 1.1.1.104 ERGO genome analysis and discovery system: 1.1.1.104 BRENDA, the Enzyme Database: 1.1.1.104 CAS: 37250-37-6 /// ENTRY EC 1.1.1.105 NAME retinol dehydrogenase retinol (vitamin A1) dehydrogenase MDR microsomal retinol dehydrogenase all-trans retinol dehydrogenase retinal reductase retinene reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME retinol:NAD+ oxidoreductase REACTION retinol + NAD+ = retinal + NADH + H+ SUBSTRATE retinol NAD+ PRODUCT retinal NADH H+ PATHWAY PATH: map00830 Retinol metabolism ORTHOLOG KO: K00061 retinol dehydrogenase GENES HSA: 5959(RDH5) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] REFERENCE 1 [PMID:5972368] Koen, A.L. and Shaw, C.R. Retinol and alcohol dehydrogenases in retina and liver. Biochim. Biophys. Acta 128 (1966) 48-54. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.105 ExPASy - ENZYME nomenclature database: 1.1.1.105 ERGO genome analysis and discovery system: 1.1.1.105 BRENDA, the Enzyme Database: 1.1.1.105 CAS: 9033-53-8 /// ENTRY EC 1.1.1.106 NAME pantoate 4-dehydrogenase pantoate dehydrogenase pantothenase D-pantoate:NAD+ 4-oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-pantoate:NAD+ 4-oxidoreductase REACTION (R)-pantoate + NAD+ = (R)-4-dehydropantoate + NADH + H+ SUBSTRATE (R)-pantoate NAD+ PRODUCT (R)-4-dehydropantoate NADH H+ PATHWAY PATH: map00770 Pantothenate and CoA biosynthesis REFERENCE 1 [PMID:4287370] Goodhue, C.T. and Snell, E.E. The bacterial degradation of pantothenic acid. 3. Enzymatic formation of aldopantoic acid. Biochemistry 5 (1966) 403-408. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.106 ExPASy - ENZYME nomenclature database: 1.1.1.106 ERGO genome analysis and discovery system: 1.1.1.106 BRENDA, the Enzyme Database: 1.1.1.106 CAS: 37250-38-7 /// ENTRY EC 1.1.1.107 NAME pyridoxal 4-dehydrogenase pyridoxal dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME pyridoxal:NAD+ 4-oxidoreductase REACTION pyridoxal + NAD+ = 4-pyridoxolactone + NADH + H+ SUBSTRATE pyridoxal NAD+ PRODUCT 4-pyridoxolactone NADH H+ COMMENT The enzyme acts on the hemiacetal form of the substrate. PATHWAY PATH: map00750 Vitamin B6 metabolism REFERENCE 1 [PMID:4306030] Burg, R.W. and Snell, E.E. The bacterial oxidation of vitamin B6. VI. Pyridoxal dehydrogenase and 4-pyridoxolactonase. J. Biol. Chem. 244 (1969) 2585-2589. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.107 ExPASy - ENZYME nomenclature database: 1.1.1.107 ERGO genome analysis and discovery system: 1.1.1.107 BRENDA, the Enzyme Database: 1.1.1.107 CAS: 37250-39-8 /// ENTRY EC 1.1.1.108 NAME carnitine 3-dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME carnitine:NAD+ 3-oxidoreductase REACTION carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+ SUBSTRATE carnitine NAD+ PRODUCT 3-dehydrocarnitine NADH H+ REFERENCE 1 [PMID:4302217] Aurich, H., Kleber, H.-P., Sorger, H. and Tauchert, H. Reinigung und Eigenschaften der Carnitindehydrogenase aus Pseudomonas aeruginosa. Eur. J. Biochem. 6 (1968) 196-201. 2 [PMID:4310279] Schopp, W., Sorger, H., Kleber, H.-P. and Aurich, H. Kinetische Untersuchungen zum Reaktionmechanisms der Carnitindehydrogenase aus Pseudomonas aeruginosa. Eur. J. Biochem. 10 (1969) 56-60. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.108 ExPASy - ENZYME nomenclature database: 1.1.1.108 ERGO genome analysis and discovery system: 1.1.1.108 BRENDA, the Enzyme Database: 1.1.1.108 CAS: 9045-45-8 /// ENTRY EC 1.1.1.109 Obsolete NAME Transferred to 1.3.1.28 CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Transferred entry: now EC 1.3.1.28 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 1.1.1.109 created 1972, deleted 1976) DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.109 ExPASy - ENZYME nomenclature database: 1.1.1.109 ERGO genome analysis and discovery system: 1.1.1.109 BRENDA, the Enzyme Database: 1.1.1.109 /// ENTRY EC 1.1.1.110 NAME indolelactate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME indolelactate:NAD+ oxidoreductase REACTION indolelactate + NAD+ = indolepyruvate + NADH + H+ SUBSTRATE indolelactate NAD+ PRODUCT indolepyruvate NADH H+ PATHWAY PATH: map00380 Tryptophan metabolism REFERENCE 1 [PMID:4384683] Jean, M. and DeMoss, R.D. Indolelactate dehydrogenase from Clostridium sporogenes. Can. J. Microbiol. 14 (1968) 429-435. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.110 ExPASy - ENZYME nomenclature database: 1.1.1.110 ERGO genome analysis and discovery system: 1.1.1.110 BRENDA, the Enzyme Database: 1.1.1.110 CAS: 37250-41-2 /// ENTRY EC 1.1.1.111 NAME 3-(imidazol-5-yl)lactate dehydrogenase imidazol-5-yl lactate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S)-3-(imidazol-5-yl)lactate:NAD(P)+ oxidoreductase REACTION (S)-3-(imidazol-5-yl)lactate + NAD(P)+ = 3-(imidazol-5-yl)pyruvate + NAD(P)H + H+ SUBSTRATE (S)-3-(imidazol-5-yl)lactate NAD+ NADP+ PRODUCT 3-(imidazol-5-yl)pyruvate NADH NADPH H+ REFERENCE 1 [PMID:4303364] Coote, J.G. and Hassall, H. The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide phosphate oxidoreductase and histidine-2-oxoglutarate aminotransferase in the degradation of imidazol-5-yl-lactate by Pseudomonas acidovorans. Biochem. J. 111 (1969) 237-239. 2 [PMID:4237631] Cortese, R., Brevet, J., Hedegaard, J. and Roche, J. [Identification and purification of an alpha-ketoacid aromatic reductase of Escherichia coli B]. C.R. Seances Soc. Biol. Fil. 162 (1968) 390-395. [French] DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.111 ExPASy - ENZYME nomenclature database: 1.1.1.111 ERGO genome analysis and discovery system: 1.1.1.111 BRENDA, the Enzyme Database: 1.1.1.111 CAS: 37250-42-3 /// ENTRY EC 1.1.1.112 NAME indanol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME indan-1-ol:NAD(P)+ 1-oxidoreductase REACTION indan-1-ol + NAD(P)+ = indanone + NAD(P)H + H+ SUBSTRATE indan-1-ol NAD+ NADP+ PRODUCT indanone NADH NADPH H+ COMMENT 3(20)alpha-Hydroxysteroids are also oxidized, more slowly. REFERENCE 1 [PMID:4397102] Billings, R.E., Sullivan, H.R. and McMahon, R.E. The dehydrogenation of 1-indanol by a soluble oxidoreductase from bovine liver. J. Biol. Chem. 246 (1971) 3512-3517. 2 [PMID:2559080] Hara, A., Nakagawa, M., Taniguchi, H. and Sawada, H. 3(20)alpha-Hydroxysteroid dehydrogenase activity of monkey liver indanol dehydrogenase. J. Biochem. (Tokyo) 106 (1989) 900-903. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.112 ExPASy - ENZYME nomenclature database: 1.1.1.112 ERGO genome analysis and discovery system: 1.1.1.112 BRENDA, the Enzyme Database: 1.1.1.112 CAS: 37250-43-4 /// ENTRY EC 1.1.1.113 NAME L-xylose 1-dehydrogenase L-xylose dehydrogenase NADPH-xylose reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-xylose:NADP+ 1-oxidoreductase REACTION L-xylose + NADP+ = L-xylono-1,4-lactone + NADPH + H+ SUBSTRATE L-xylose NADP+ PRODUCT L-xylono-1,4-lactone NADPH H+ COMMENT Also oxidizes D-arabinose and D-lyxose. REFERENCE 1 Uehara, K. and Takeda, M. L-Xylose dehydrogenase in bakers' yeast. J. Biochem. (Tokyo) 52 (1962) 461-463. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.113 ExPASy - ENZYME nomenclature database: 1.1.1.113 ERGO genome analysis and discovery system: 1.1.1.113 BRENDA, the Enzyme Database: 1.1.1.113 CAS: 37250-44-5 /// ENTRY EC 1.1.1.114 NAME apiose 1-reductase D-apiose reductase D-apiitol reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-apiitol:NAD+ 1-oxidoreductase REACTION D-apiitol + NAD+ = D-apiose + NADH + H+ SUBSTRATE D-apiitol NAD+ PRODUCT D-apiose NADH H+ REFERENCE 1 Hanna, R., Picken, M. and Mendicino, J. Purification of a specific D-apiitol dehydrogenase from a Micrococcus isolated from the surface of germinating parsley seeds. Biochim. Biophys. Acta 315 (1973) 259-271. 2 [PMID:4314545] Neal, D.L. and Kindel, P.K. D-Apiose reductase from Aerobacter aerogenes. J. Bacteriol. 101 (1970) 910-915. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.114 ExPASy - ENZYME nomenclature database: 1.1.1.114 ERGO genome analysis and discovery system: 1.1.1.114 BRENDA, the Enzyme Database: 1.1.1.114 CAS: 37250-45-6 /// ENTRY EC 1.1.1.115 NAME ribose 1-dehydrogenase (NADP+) D-ribose dehydrogenase (NADP+) NADP-pentose-dehydrogenase ribose 1-dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-ribose:NADP+ 1-oxidoreductase REACTION D-ribose + NADP+ + H2O = D-ribonate + NADPH + H+ SUBSTRATE D-ribose NADP+ H2O PRODUCT D-ribonate NADPH H+ COMMENT Also acts, more slowly, on D-xylose and other pentoses. REFERENCE 1 [PMID:4381350] Scher, B.M. and Horecker, B.L. Pentose metabolism in Candida. 3. The triphosphopyridine nucleotide-specific polyol dehydrogenase of Candida utilis. Arch. Biochem. Biophys. 116 (1966) 117-128. 2 [PMID:4393642] Schiwara, H.W., Domschke, W. and Domagk, G.F. Uber die Zucker-Dehydrogenase in der Saugetierleber. I. Differenzierung verschiedener Zucker-Dehydrogenasen in der Schweineleber durch Disk-Elektrophorese und Ionenaustausch-chromatographie. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1575-1581. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.115 ExPASy - ENZYME nomenclature database: 1.1.1.115 ERGO genome analysis and discovery system: 1.1.1.115 BRENDA, the Enzyme Database: 1.1.1.115 CAS: 37250-46-7 /// ENTRY EC 1.1.1.116 NAME D-arabinose 1-dehydrogenase NAD-pentose-dehydrogenase arabinose(fucose)dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-arabinose:NAD+ 1-oxidoreductase REACTION D-arabinose + NAD+ = D-arabinono-1,4-lactone + NADH + H+ SUBSTRATE D-arabinose NAD+ PRODUCT D-arabinono-1,4-lactone NADH H+ GENES SCE: YBR149W(ARA1) REFERENCE 1 Palleroni, N.J. and Doudoroff, M. Metabolism of carbohydrates by Pseudomonas saccharophilla. III. Oxidation of D-arabinose. J. Bacteriol. 74 (1957) 180-185. 2 [PMID:4393642] Schiwara, H.W., Domschke, W. and Domagk, G.F. Uber die Zucker-Dehydrogenase in der Saugetierleber. I. Differenzierung verschiedener Zucker-Dehydrogenasen in der Schweineleber durch Disk-Elektrophorese und Ionenaustausch-chromatographie. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1575-1581. [German] DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.116 ExPASy - ENZYME nomenclature database: 1.1.1.116 ERGO genome analysis and discovery system: 1.1.1.116 BRENDA, the Enzyme Database: 1.1.1.116 CAS: 37250-47-8 /// ENTRY EC 1.1.1.117 NAME D-arabinose 1-dehydrogenase [NAD(P)+] D-arabinose 1-dehydrogenase [NAD(P)] CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-arabinose:NAD(P)+ 1-oxidoreductase REACTION D-arabinose + NAD(P)+ = D-arabinono-1,4-lactone + NAD(P)H + H+ SUBSTRATE D-arabinose NAD+ NADP+ PRODUCT D-arabinono-1,4-lactone NADH NADPH H+ COMMENT Also acts on L-galactose, 6-deoxy- and 3,6-dideoxy-L-galactose. GENES SCE: YBR149W(ARA1) MOTIF PS: PS00062 [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY] PS: PS00063 [LIVM]-[PAIV]-[KR]-[ST]-x(4)-R-x(2)-[GSTAEQK]-[NSL]- x(2)-[LIVMFA] PS: PS00798 G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGC]-[AS]-x(5)-E-x(2)- [LIVM]-G REFERENCE 1 [PMID:5845847] Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a psuedomonad. J. Biol. Chem. 240 (1965) 4488-4492. 2 [PMID:5845848] Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493-4497. 3 [PMID:5845849] Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498-4502. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.117 ExPASy - ENZYME nomenclature database: 1.1.1.117 ERGO genome analysis and discovery system: 1.1.1.117 BRENDA, the Enzyme Database: 1.1.1.117 CAS: 37250-48-9 /// ENTRY EC 1.1.1.118 NAME glucose 1-dehydrogenase (NAD+) D-glucose:NAD oxidoreductase D-aldohexose dehydrogenase glucose 1-dehydrogenase (NAD) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-glucose:NAD+ 1-oxidoreductase REACTION D-glucose + NAD+ = D-glucono-1,5-lactone + NADH + H+ SUBSTRATE D-glucose NAD+ PRODUCT D-glucono-1,5-lactone NADH H+ REFERENCE 1 Hu, A.S.L. and Cline, A.L. The regulation of some sugar dehydrogenases in a pseuudomonad. Biochim. Biophys. Acta 93 (1964) 237-245. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.118 ExPASy - ENZYME nomenclature database: 1.1.1.118 ERGO genome analysis and discovery system: 1.1.1.118 BRENDA, the Enzyme Database: 1.1.1.118 CAS: 37250-49-0 /// ENTRY EC 1.1.1.119 NAME glucose 1-dehydrogenase (NADP+) nicotinamide adenine dinucleotide phosphate-linked aldohexose $dehydrogenase NADP-linked aldohexose dehydrogenase NADP-dependent glucose dehydrogenase glucose 1-dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-glucose:NADP+ 1-oxidoreductase REACTION D-glucose + NADP+ = D-glucono-1,4-lactone + NADPH + H+ SUBSTRATE D-glucose NADP+ PRODUCT D-glucono-1,4-lactone NADPH H+ COMMENT Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose. REFERENCE 1 Adachi, O. and Ameyama, M. D-Glucose dehydrogenase from Gluconobacter suboxydans. Methods Enzymol. 89 (1982) 159-163. 2 [PMID:4384672] Avigad, G., Alroy, Y. and Englard, S. Purification and properties of a nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase from Gluconobacter cerinus. J. Biol. Chem. 243 (1968) 1936-1941. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.119 ExPASy - ENZYME nomenclature database: 1.1.1.119 ERGO genome analysis and discovery system: 1.1.1.119 BRENDA, the Enzyme Database: 1.1.1.119 CAS: 37250-50-3 /// ENTRY EC 1.1.1.120 NAME galactose 1-dehydrogenase (NADP+) D-galactose dehydrogenase (NADP+) galactose 1-dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-galactose:NADP+ 1-oxidoreductase REACTION D-galactose + NADP+ = D-galactonolactone + NADPH + H+ SUBSTRATE D-galactose NADP+ PRODUCT D-galactonolactone NADPH H+ COMMENT Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose. PATHWAY PATH: map00052 Galactose metabolism REFERENCE 1 [PMID:5845847] Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a psuedomonad. J. Biol. Chem. 240 (1965) 4488-4492. 2 [PMID:5845848] Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493-4497. 3 [PMID:5845849] Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498-4502. 4 [PMID:4387016] Schiwara, H.W. and Domagk, G.F. Uber den Abbau der Desoxyzucker durch Bakterienenzyme. V. Anreicherung und Charakterisierung einer NADP-abhangigen Abequosedehydrogenase aus Pseudomonas putida. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1321-1329. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.120 ExPASy - ENZYME nomenclature database: 1.1.1.120 ERGO genome analysis and discovery system: 1.1.1.120 BRENDA, the Enzyme Database: 1.1.1.120 CAS: 37250-51-4 /// ENTRY EC 1.1.1.121 NAME aldose 1-dehydrogenase aldose dehydrogenase dehydrogenase, D-aldohexose CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-aldose:NAD+ 1-oxidoreductase REACTION D-aldose + NAD+ = D-aldonolactone + NADH + H+ SUBSTRATE D-aldose NAD+ PRODUCT D-aldonolactone NADH H+ COMMENT Acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose, 6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose. REFERENCE 1 [PMID:5845847] Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4488-4492. 2 [PMID:5845848] Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493-4497. 3 [PMID:5845849] Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498-4502. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.121 ExPASy - ENZYME nomenclature database: 1.1.1.121 ERGO genome analysis and discovery system: 1.1.1.121 BRENDA, the Enzyme Database: 1.1.1.121 CAS: 9076-61-3 /// ENTRY EC 1.1.1.122 NAME D-threo-aldose 1-dehydrogenase L-fucose dehydrogenase (2S,3R)-aldose dehydrogenase dehydrogenase, L-fucose L-fucose (D-arabinose) dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-threo-aldose:NAD+ 1-oxidoreductase REACTION a D-threo-aldose + NAD+ = a D-threo-aldono-1,5-lactone + NADH + H+ SUBSTRATE D-threo-aldose NAD+ PRODUCT D-threo-aldono-1,5-lactone NADH H+ COMMENT Acts on L-fucose, D-arabinose and L-xylose; the animal enzyme was also shown to act on L-arabinose, and the enzyme from Pseudomonas caryophylli on L-glucose. PATHWAY PATH: map00053 Ascorbate and aldarate metabolism ORTHOLOG KO: K00064 D-threo-aldose 1-dehydrogenase GENES ECA: ECA0250 XCC: XCC0141 XAC: XAC0158 PST: PSPTO3075 MLO: mll8482 mlr3332 SME: SMa1403 SMc02775 ATU: Atu3528 ATC: AGR_L_2607 BJA: blr1124 BAN: BA3463 BA5079 BAR: GBAA3463 GBAA5079 BAA: BA_3961 BA_5496 BAT: BAS3210 BAS4717 BCE: BC3410 BCZ: BTZK3116(fdh) BTK: BT9727_3188(fdh) OIH: OB0307 RBA: RB5820(fucO) REFERENCE 1 [PMID:40609] Sasajima, K.-I. and Sinskey, A.J. Oxidation of L-glucose by a Pseudomonad. Biochim. Biophys. Acta 571 (1979) 120-126. 2 [PMID:4309152] Schachter, H., Sarney, J., McGuire, E.J. and Roseman, S. Isolation of diphosphopyridine nucleotide-dependent L-fucose dehydrogenase from pork liver. J. Biol. Chem. 244 (1969) 4785-4792. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.122 ExPASy - ENZYME nomenclature database: 1.1.1.122 ERGO genome analysis and discovery system: 1.1.1.122 BRENDA, the Enzyme Database: 1.1.1.122 CAS: 9082-70-6 /// ENTRY EC 1.1.1.123 NAME sorbose 5-dehydrogenase (NADP+) 5-ketofructose reductase 5-keto-D-fructose reductase sorbose (nicotinamide adenine dinucleotide phosphate) dehydrogenase reduced nicotinamide adenine dinucleotide phosphate-linked reductase sorbose 5-dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-sorbose:NADP+ 5-oxidoreductase REACTION L-sorbose + NADP+ = 5-dehydro-D-fructose + NADPH + H+ SUBSTRATE L-sorbose NADP+ PRODUCT 5-dehydro-D-fructose NADPH H+ REFERENCE 1 [PMID:4392628] Englard, S., Kaysen, G. and Avigad, G. 5-keto-D-Fructose. VI. A specific reduced nicotinamide adenine dinucleotide phosphate-linked reductase from yeast. J. Biol. Chem. 245 (1970) 1311-1318. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.123 ExPASy - ENZYME nomenclature database: 1.1.1.123 ERGO genome analysis and discovery system: 1.1.1.123 BRENDA, the Enzyme Database: 1.1.1.123 CAS: 37250-52-5 /// ENTRY EC 1.1.1.124 NAME fructose 5-dehydrogenase (NADP+) 5-ketofructose reductase (NADP) 5-keto-D-fructose reductase (NADP+) fructose 5-(nicotinamide adenine dinucleotide phosphate) $dehydrogenase D-(-)fructose:(NADP+) 5-oxidoreductase fructose 5-dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-fructose:NADP+ 5-oxidoreductase REACTION D-fructose + NADP+ = 5-dehydro-D-fructose + NADPH + H+ SUBSTRATE D-fructose NADP+ PRODUCT 5-dehydro-D-fructose NADPH H+ REFERENCE 1 Ameyama, M., Matsushita, K., Shinagawa, E. and Adachi, O. 5-keto-D-Fructose reductase of Gluconobacter industrius - Purification, crystallization and properties. Agric. Biol. Chem. 45 (1981) 863-869. 2 [PMID:4379259] Avigad, G., Englard, S. and Pifco, S. 5-keto-D-Fructose. IV. A specific reduced nicotinamide adenine dinucleotide phosphate-linked reductase from Gluconobacter cerinus. J. Biol. Chem. 241 (1966) 373-378. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.124 ExPASy - ENZYME nomenclature database: 1.1.1.124 ERGO genome analysis and discovery system: 1.1.1.124 BRENDA, the Enzyme Database: 1.1.1.124 CAS: 37250-53-6 /// ENTRY EC 1.1.1.125 NAME 2-deoxy-D-gluconate 3-dehydrogenase 2-deoxygluconate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 2-deoxy-D-gluconate:NAD+ 3-oxidoreductase REACTION 2-deoxy-D-gluconate + NAD+ = 3-dehydro-2-deoxy-D-gluconate + NADH + H+ SUBSTRATE 2-deoxy-D-gluconate NAD+ PRODUCT 3-dehydro-2-deoxy-D-gluconate NADH H+ PATHWAY PATH: map00040 Pentose and glucuronate interconversions ORTHOLOG KO: K00065 2-deoxy-D-gluconate 3-dehydrogenase GENES CAL: orf19.5763 orf19.6322(ARD1) ECO: b2842(kduD) ECJ: JW2810(kduD) ECE: Z4162(kduD) ECS: ECs3699 ECC: c3439(kduD) STY: STY3162(kduD) STT: t2927(kduD) STM: STM3017(kduD) YPE: YPO0839(kduD2) YPO1724(kduD1) YPK: y1886(kduD) y3224(kduD) YPM: YP1749(kduD) YP3535(kduD2) YPS: YPTB2357(kduD1) YPTB3083(kduD2) SFL: SF2852(kduD) SFX: S3050(kduD) ECA: ECA2401(kduD) XCC: XCC0152(kduD) XAC: XAC0169(kduD) VVU: VV20914 VV21093 VVY: VV0552 VVA1401 VVA1616 VPA: VPA0077 PPR: PBPRB0149(kduD) PBPRB1737 BMA: BMAA1811(kduD) NEU: NE1567(kduD) MLO: mll4054 SME: SMb21348 ATU: Atu3141(kduD) ATC: AGR_L_3337 BME: BMEII0316 BMS: BRA0981 BJA: bll1082(kduD) bll4353(kduD) RPA: RPA4786(rhlG) CCR: CC1492 BSU: BG11400(kduD) BHA: BH2167(kduD) BLI: BL02435(kduD) OIH: OB2814 CAC: CAC0361(kduD) MTU: Rv1714 Rv1928c MTC: MT1753.1 SCO: SCO3476(SCE65.12c) TTH: TTP0037 AFU: AF1207(kduD) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] REFERENCE 1 Eichhorn, M.M. and Cynkin, M.A. Microbial metabolism of 2-deoxyglucose; 2-deoxyglucose acid dehydrogenase. Biochemistry 4 (1965) 159-165. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.125 ExPASy - ENZYME nomenclature database: 1.1.1.125 ERGO genome analysis and discovery system: 1.1.1.125 BRENDA, the Enzyme Database: 1.1.1.125 CAS: 37250-54-7 /// ENTRY EC 1.1.1.126 NAME 2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase 2-keto-3-deoxy-D-gluconate dehydrogenase 2-keto-3-deoxygluconate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 2-dehydro-3-deoxy-D-gluconate:NADP+ 6-oxidoreductase REACTION 2-dehydro-3-deoxy-D-gluconate + NADP+ = (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + NADPH + H+ SUBSTRATE 2-dehydro-3-deoxy-D-gluconate NADP+ PRODUCT (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate NADPH H+ REFERENCE 1 Preiss, J. and Ashwell, G. Alginic acid metabolism in bacteria. II. The enzymatic reduction of 4-deoxy-L-erythro-5-hexoseulose uronic acid to 2-keto-3-deoxy-D-gluconic acid. J. Biol. Chem. 237 (1962) 317-321. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.126 ExPASy - ENZYME nomenclature database: 1.1.1.126 ERGO genome analysis and discovery system: 1.1.1.126 BRENDA, the Enzyme Database: 1.1.1.126 CAS: 37250-55-8 /// ENTRY EC 1.1.1.127 NAME 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase 2-keto-3-deoxygluconate 5-dehydrogenase 2-keto-3-deoxy-D-gluconate dehydrogenase 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide $(phosphate)) dehydrogenase 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic $acid) dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 2-dehydro-3-deoxy-D-gluconate:NAD+ 5-oxidoreductase REACTION 2-dehydro-3-deoxy-D-gluconate + NAD+ = (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH + H+ SUBSTRATE 2-dehydro-3-deoxy-D-gluconate NAD+ PRODUCT (4S)-4,6-dihydroxy-2,5-dioxohexanoate NADH H+ COMMENT The enzyme from Pseudomonas acts equally well on NAD+ or NADP+, while that from Erwinia chrysanthemi and Escherichia coli is more specific for NAD+. PATHWAY PATH: map00040 Pentose and glucuronate interconversions REFERENCE 1 Condemine, G., Hugouvieux-Cotte-Pattat, N. and Robert-Baudouy, J. An enzyme in the pectolytic pathway of Erwinia chrysanthemi: 3-keto-3-deoxygluconate oxidoreductase. J. Gen. Microbiol. 130 (1984) 2839-2844. 2 Preiss, J. and Ashwell, G. Polygalacturonic acid metabolism in bacteria. II. Formation and metabolism of 3-deoxy-D-glycero-2,5-hexodiulosonic acid. J. Biol. Chem. 238 (1963) 1577-1583. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.127 ExPASy - ENZYME nomenclature database: 1.1.1.127 ERGO genome analysis and discovery system: 1.1.1.127 BRENDA, the Enzyme Database: 1.1.1.127 CAS: 37250-56-9 /// ENTRY EC 1.1.1.128 NAME L-idonate 2-dehydrogenase 5-ketogluconate 2-reductase 5-keto-D-gluconate 2-reductase L-idonate dehydrogenase reductase, 5-ketogluconate 5- (L-idonate-forming) 5KGR 5-ketoglucono-idono-reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-idonate:NADP+ 2-oxidoreductase REACTION L-idonate + NADP+ = 5-dehydro-D-gluconate + NADPH + H+ SUBSTRATE L-idonate NADP+ PRODUCT 5-dehydro-D-gluconate NADPH H+ REFERENCE 1 Takagi, Y. A new enzyme, 5-ketoglucono-idono-reductase. Agric. Biol. Chem. 26 (1962) 719-720. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.128 ExPASy - ENZYME nomenclature database: 1.1.1.128 ERGO genome analysis and discovery system: 1.1.1.128 BRENDA, the Enzyme Database: 1.1.1.128 CAS: 37250-57-0 /// ENTRY EC 1.1.1.129 NAME L-threonate 3-dehydrogenase threonate dehydrogenase L-threonic acid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-threonate:NAD+ 3-oxidoreductase REACTION L-threonate + NAD+ = 3-dehydro-L-threonate + NADH + H+ SUBSTRATE L-threonate NAD+ PRODUCT 3-dehydro-L-threonate NADH H+ PATHWAY PATH: map00053 Ascorbate and aldarate metabolism REFERENCE 1 Aspen, A.J. and Jakoby, W.B. L-Threonic acid dehydrogenase: purification and properties. J. Biol. Chem. 239 (1964) 710-713. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.129 ExPASy - ENZYME nomenclature database: 1.1.1.129 ERGO genome analysis and discovery system: 1.1.1.129 BRENDA, the Enzyme Database: 1.1.1.129 CAS: 37250-59-2 /// ENTRY EC 1.1.1.130 NAME 3-dehydro-L-gulonate 2-dehydrogenase 3-keto-L-gulonate dehydrogenase 3-ketogulonate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3-dehydro-L-gulonate:NAD(P)+ 2-oxidoreductase REACTION 3-dehydro-L-gulonate + NAD(P)+ = (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H + H+ SUBSTRATE 3-dehydro-L-gulonate NAD+ NADP+ PRODUCT (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate NADH NADPH H+ PATHWAY PATH: map00040 Pentose and glucuronate interconversions REFERENCE 1 Volk, W.A. and Larsen, J.L. beta-Keto-L-gulonic acid as an intermediate in the bacterial metabolism of ascorbic acid. J. Biol. Chem. 237 (1962) 2454-2457. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.130 ExPASy - ENZYME nomenclature database: 1.1.1.130 ERGO genome analysis and discovery system: 1.1.1.130 BRENDA, the Enzyme Database: 1.1.1.130 CAS: 37250-61-6 /// ENTRY EC 1.1.1.131 NAME mannuronate reductase mannonate dehydrogenase mannonate (nicotinamide adenine dinucleotide $(phosphate))dehydrogenase mannonate dehydrogenase (NAD(P)+) D-mannonate:nicotinamide adenine dinucleotide (phosphate $oxidoreductase (D-mannuronate-forming)) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-mannonate:NAD(P)+ 6-oxidoreductase REACTION D-mannonate + NAD(P)+ = D-mannuronate + NAD(P)H + H+ SUBSTRATE D-mannonate NAD+ NADP+ PRODUCT D-mannuronate NADH NADPH H+ REFERENCE 1 [PMID:4388117] Farmer, J.J., III and Eagon, R.G. Aldohexuronic acid catabolism by a soil Aeromonas. J. Bacteriol. 97 (1969) 97-106. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.131 ExPASy - ENZYME nomenclature database: 1.1.1.131 ERGO genome analysis and discovery system: 1.1.1.131 BRENDA, the Enzyme Database: 1.1.1.131 CAS: 37250-62-7 /// ENTRY EC 1.1.1.132 NAME GDP-mannose 6-dehydrogenase guanosine diphosphomannose dehydrogenase GDP-mannose dehydrogenase guanosine diphospho-D-mannose dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME GDP-D-mannose:NAD+ 6-oxidoreductase REACTION GDP-D-mannose + 2 NAD+ + H2O = GDP-D-mannuronate + 2 NADH + 2 H+ SUBSTRATE GDP-D-mannose NAD+ H2O PRODUCT GDP-D-mannuronate NADH H+ COMMENT Also acts on the corresponding deoxynucleoside diphosphate derivative as a substrate. PATHWAY PATH: map00051 Fructose and mannose metabolism ORTHOLOG KO: K00066 GDPmannose 6-dehydrogenase GENES PAE: PA3540(algD) PPU: PP1288(algD) PST: PSPTO1243(algD) ACI: ACIAD0087 BJA: blr6296 BTK: BT9727_4949 SCO: SCO0382(SCF62.08) STRUCTURES PDB: 1MFZ 1MUU 1MV8 REFERENCE 1 Preiss, J. Sugar nucleotide reaction in Arthrobacter. II. Biosynthesis of guanosine diphosphomannuronate. J. Biol. Chem. 239 (1964) 3127-3132. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.132 ExPASy - ENZYME nomenclature database: 1.1.1.132 ERGO genome analysis and discovery system: 1.1.1.132 BRENDA, the Enzyme Database: 1.1.1.132 CAS: 37250-63-8 /// ENTRY EC 1.1.1.133 NAME dTDP-4-dehydrorhamnose reductase dTDP-4-keto-L-rhamnose reductase reductase, thymidine diphospho-4-ketorhamnose dTDP-4-ketorhamnose reductase TDP-4-keto-rhamnose reductase thymidine diphospho-4-ketorhamnose reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME dTDP-6-deoxy-L-mannose:NADP+ 4-oxidoreductase REACTION dTDP-6-deoxy-L-mannose + NADP+ = dTDP-4-dehydro-6-deoxy-L-mannose + NADPH + H+ SUBSTRATE dTDP-6-deoxy-L-mannose NADP+ PRODUCT dTDP-4-dehydro-6-deoxy-L-mannose NADPH H+ COMMENT In the reverse direction, reduction on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyses epimerization at C-3 and C-5; the complex has been referred to as dTDP-L-rhamnose synthase. PATHWAY PATH: map00520 Nucleotide sugars metabolism PATH: map00521 Streptomycin biosynthesis PATH: map00523 Polyketide sugar unit biosynthesis ORTHOLOG KO: K00067 dTDP-4-dehydrorhamnose reductase GENES ECO: b2040(rfbD) ECJ: JW2025(rfbD) STY: STY2306(rfbD) STT: t0776(rfbD) STM: STM2096(rfbD) SFL: SF2103(rfbD) SFX: S2226(rfbD) ECA: ECA1440(rfbD) XFA: XF0258 XFT: PD0211(rmlD) XCC: XCC0624(rmlD) XAC: XAC3582(rmlD) VVY: VV0302 PAE: PA5162(rmlD) PPU: PP1784(rmlD) PST: PSPTO1080(rfbD) ACI: ACIAD0078(rmlD) SON: SO1653(rfbD) MCA: MCA1285(rfbD) NME: NMB0756 NMA: NMA0967(rfbD) CVI: CV4011(rfbD) RSO: RS01588(rfbD) BMA: BMA1987(rfbD) BPS: BPSL2683(rmlD) BPE: BP0108(rfbD) BPA: BPP0172(rfbD) BBR: BB0174(rfbD) NEU: NE1023(rfbD) GSU: GSU2247 GSU2365(rfbD) DVU: DVU1363(rfbD) DPS: DP2222 RPR: RP332 RTY: RT0322(rmlD) RCO: RC0456 MLO: mlr7553 SME: SMb21327(expA10) ATU: Atu4616(rfbD) ATC: AGR_L_531 RPA: RPA0119(rmlD) CCR: CC1140 CC3615 BSU: BG10619(spsK) BHA: BH3365(spsK) BAN: BA1231(rfbD) BAR: GBAA1231(rfbD) BAA: BA_1766 BAT: BAS1138 BCE: BC1215 BCA: BCE1338(rfbD) BCZ: BTZK1112(rbfD) BTK: BT9727_1118(rbfD) OIH: OB1128 LMO: lmo1084 LLA: L320(rmlC) SPY: SPy0784(rmlD) SPM: spyM18_0843 SPG: SpyM3_0521(rmlD) SPS: SPs1333 SPA: M6_Spy0619 SPR: spr0323(cpsO) SAG: SAG1424(rfbD) SAN: gbs1494(rmlD) SMU: SMU.824 LPL: lp_1190(rfbD) LJO: LJ1052 EFA: EF2191 CAC: CAC2315 CAP0122 CPE: CPE0618(rfbD) MTU: Rv3266c(rmlD) MTC: MT3366 MBO: Mb3294c(rmlD) MLE: ML0751(rmlD) MPA: MAP3380c(rmlD) CGL: NCgl0326(Cgl0333) CEF: CE0343 CDI: DIP0361 TWH: TW029(rmlD) TWS: TW032 LXX: Lxx04900(strL) BLO: BL0228 FNU: FN1685 FN1698 FN1847 PCU: pc0125(rfbD) LIL: LA1660(rmlD) LIC: LIC12125(rfbD) BTH: BT1730 PGI: PG1561(rfbD) SYN: sll1395(rfbD) SYW: SYNW0647(rfbD) SYC: syc1994_c(rfbD) TEL: tlr0951(rfbD) GVI: glr3234(rfbD) ANA: alr4490(rfbD) PMM: PMM1233(rfbD) PMT: PMT0114(rfbD) CTE: CT0307(rfbD) DRA: DRA0044 MAC: MA3778(rfbD) MMA: MM1168 MTH: MTH1792 TVO: TVG0949121 PTO: PTO0308 PHO: PH0417 PAB: PAB0789 APE: APE1179 SSO: SSO0832(rfbD-1) SSO1783(rfbD-2) SSO2161(rfbD-3) STO: ST1970 STRUCTURES PDB: 1KBZ 1KC1 1KC3 1N2S REFERENCE 1 [PMID:4384782] Melo, A. and Glaser, L. The mechanism of 6-deoxyhexose synthesis. II. Conversion of deoxythymidine diphosphate 4-keto-6-deoxy-D-glucose to deoxythymidine diphosphate L-rhamnose. J. Biol. Chem. 243 (1968) 1475-1478. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.133 ExPASy - ENZYME nomenclature database: 1.1.1.133 ERGO genome analysis and discovery system: 1.1.1.133 BRENDA, the Enzyme Database: 1.1.1.133 CAS: 37250-64-9 /// ENTRY EC 1.1.1.134 NAME dTDP-6-deoxy-L-talose 4-dehydrogenase thymidine diphospho-6-deoxy-L-talose dehydrogenase TDP-6-deoxy-L-talose dehydrogenase dTDP-6-deoxy-L-talose dehydrogenase (4-reductase) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME dTDP-6-deoxy-L-talose:NADP+ 4-oxidoreductase REACTION dTDP-6-deoxy-L-talose + NADP+ = dTDP-4-dehydro-6-deoxy-L-mannose + NADPH + H+ SUBSTRATE dTDP-6-deoxy-L-talose NADP+ PRODUCT dTDP-4-dehydro-6-deoxy-L-mannose NADPH H+ COMMENT Oxidation on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyses epimerization at C-3 and C-5. PATHWAY PATH: map00520 Nucleotide sugars metabolism REFERENCE 1 [PMID:4199258] Gaugler, R.W. and Gabriel, O. Biological mechanisms involved in the formation of deoxy sugars. VII. Biosynthesis of 6-deoxy-L-talose. J. Biol. Chem. 248 (1973) 6041-6049. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.134 ExPASy - ENZYME nomenclature database: 1.1.1.134 ERGO genome analysis and discovery system: 1.1.1.134 BRENDA, the Enzyme Database: 1.1.1.134 CAS: 37250-65-0 /// ENTRY EC 1.1.1.135 NAME GDP-6-deoxy-D-talose 4-dehydrogenase guanosine diphospho-6-deoxy-D-talose dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME GDP-6-deoxy-D-talose:NAD(P)+ 4-oxidoreductase REACTION GDP-6-deoxy-D-talose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+ SUBSTRATE GDP-6-deoxy-D-talose NAD+ NADP+ PRODUCT GDP-4-dehydro-6-deoxy-D-mannose NADH NADPH H+ PATHWAY PATH: map00051 Fructose and mannose metabolism REFERENCE 1 Markovitz, A. Biosynthesis of guanosine diphosphate D-rhamnose and guanosine diphosphate D-talomethylose from guanosine diphosphate alpha-D-mannose. J. Biol. Chem. 239 (1964) 2091-2098. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.135 ExPASy - ENZYME nomenclature database: 1.1.1.135 ERGO genome analysis and discovery system: 1.1.1.135 BRENDA, the Enzyme Database: 1.1.1.135 CAS: 37250-66-1 /// ENTRY EC 1.1.1.136 NAME UDP-N-acetylglucosamine 6-dehydrogenase uridine diphosphoacetylglucosamine dehydrogenase UDP-acetylglucosamine dehydrogenase UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase UDP-GLcNAc dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME UDP-N-acetyl-D-glucosamine:NAD+ 6-oxidoreductase REACTION UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O = UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+ SUBSTRATE UDP-N-acetyl-D-glucosamine NAD+ H2O PRODUCT UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate NADH H+ PATHWAY PATH: map00530 Aminosugars metabolism REFERENCE 1 [PMID:4312076] Fan, D.-F., John, C.E., Zalitis, J. and Feingold, D.S. UDPacetylglucosamine dehydrogenase from Achromobacter georgiopolitanum. Arch. Biochem. Biophys. 135 (1969) 45-49. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.136 ExPASy - ENZYME nomenclature database: 1.1.1.136 ERGO genome analysis and discovery system: 1.1.1.136 BRENDA, the Enzyme Database: 1.1.1.136 CAS: 9054-83-5 /// ENTRY EC 1.1.1.137 NAME ribitol-5-phosphate 2-dehydrogenase dehydrogenase, ribitol 5-phosphate CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-ribitol-5-phosphate:NAD(P)+ 2-oxidoreductase REACTION D-ribitol 5-phosphate + NAD(P)+ = D-ribulose 5-phosphate + NAD(P)H + H+ SUBSTRATE D-ribitol 5-phosphate NAD+ NADP+ PRODUCT D-ribulose 5-phosphate NADH NADPH H+ PATHWAY PATH: map00040 Pentose and glucuronate interconversions ORTHOLOG KO: K05352 ribitol-5-phosphate 2-dehydrogenase GENES LPL: lp_1817 REFERENCE 1 Glaser, L. Ribitol-5-phosphate from Lactobacillus plantarum. Biochim. Biophys. Acta 67 (1963) 525-530. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.137 ExPASy - ENZYME nomenclature database: 1.1.1.137 ERGO genome analysis and discovery system: 1.1.1.137 BRENDA, the Enzyme Database: 1.1.1.137 CAS: 37250-67-2 /// ENTRY EC 1.1.1.138 NAME mannitol 2-dehydrogenase (NADP+) mannitol 2-dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-mannitol:NADP+ 2-oxidoreductase REACTION D-mannitol + NADP+ = D-fructose + NADPH + H+ SUBSTRATE D-mannitol NADP+ PRODUCT D-fructose NADPH H+ PATHWAY PATH: map00051 Fructose and mannose metabolism MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] STRUCTURES PDB: 1H5Q REFERENCE 1 Edmundowicz, J.M. and Wriston, J.C., Jr. Mannitol dehydrogenase from Agaricus campestris. J. Biol. Chem. 238 (1963) 3539-3541. 2 Strobel, G.A. and Kosuge, T. Polyol metabolism in Diplodia viticola Desm. Arch. Biochem. Biophys. 109 (1965) 622-626. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.138 ExPASy - ENZYME nomenclature database: 1.1.1.138 ERGO genome analysis and discovery system: 1.1.1.138 BRENDA, the Enzyme Database: 1.1.1.138 CAS: 37250-68-3 /// ENTRY EC 1.1.1.139 Obsolete NAME Deleted entry CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Deleted entry: - polyol dehydrogenase (NADP+). Now included with EC 1.1.1.21 aldehyde reductase (EC 1.1.1.139 created 1972, deleted 1978) DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.139 ExPASy - ENZYME nomenclature database: 1.1.1.139 ERGO genome analysis and discovery system: 1.1.1.139 BRENDA, the Enzyme Database: 1.1.1.139 /// ENTRY EC 1.1.1.140 NAME sorbitol-6-phosphate 2-dehydrogenase ketosephosphate reductase D-sorbitol 6-phosphate dehydrogenase D-sorbitol-6-phosphate dehydrogenase sorbitol-6-P-dehydrogenase D-glucitol-6-phosphate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-sorbitol-6-phosphate:NAD+ 2-oxidoreductase REACTION D-sorbitol 6-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+ SUBSTRATE D-sorbitol 6-phosphate NAD+ PRODUCT D-fructose 6-phosphate NADH H+ PATHWAY PATH: map00051 Fructose and mannose metabolism ORTHOLOG KO: K00068 sorbitol-6-phosphate 2-dehydrogenase GENES ECO: b2705(srlD) ECJ: JW2674(srlD) ECE: Z4012(srlD) Z5618 ECS: ECs3561 ECs5003 ECC: c3259(srlD) c4986 STY: STY2956(srlD) STT: t2736(srlD) STM: STM2835(srlD) SFL: SF2728(srlD) SF4093 SFX: S2919(srlD) S3637(sorD) PMU: PM1968 CVI: CV2258 BLI: BL02488 BLD: BLi03863 SMU: SMU.308 LPL: lp_3623(srlD1) lp_3657(srlD2) EFA: EF3310 MMY: MSC_0020(srlD) HMA: rrnAC0917(sorD) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] REFERENCE 1 [PMID:4318899] Du Toit, P.J. and Kotze, J.P. The isolation and characterization of sorbitol-6-phosphate dehydrogenase from Clostridium pasteurianum. Biochim. Biophys. Acta 206 (1970) 333-342. 2 Liss, M., Horwitz, S.B. and Kaplan, N.O. D-Mannitol 1-phosphate dehydrogenase and D-sorbitol 6-phosphate dehydrogenase in Aerobacter aerogenes. J. Biol. Chem. 237 (1962) 1342-1350. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.140 ExPASy - ENZYME nomenclature database: 1.1.1.140 ERGO genome analysis and discovery system: 1.1.1.140 BRENDA, the Enzyme Database: 1.1.1.140 CAS: 37250-69-4 /// ENTRY EC 1.1.1.141 NAME 15-hydroxyprostaglandin dehydrogenase (NAD+) NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I) PGDH 11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase 15-OH-PGDH 15-hydroxyprostaglandin dehydrogenase 15-hydroxyprostanoic dehydrogenase NAD-specific 15-hydroxyprostaglandin dehydrogenase prostaglandin dehydrogenase 15-hydroxyprostaglandin dehydrogenase (NAD) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ $15-oxidoreductase REACTION (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NAD+ = (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADH + H+ SUBSTRATE (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate NAD+ PRODUCT (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate NADH H+ COMMENT Acts on prostaglandin E2, F2alpha and B1, but not on prostaglandin D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+). GENES HSA: 3248(HPGD) RNO: 79242(Hpgd) DISEASE MIM: 601688 Hydroxyprostaglandin dehydrogenase 15-(NAD) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] REFERENCE 1 Anggard, E. and Samuelsson, B. Purification and properties of a 15-hydroxyprostaglandin dehydrogenase from swine lung. Prostaglandins and related factors. Ark. Kemi 25 (1966) 293-300. 2 [PMID:1117007] Braithwaite, S.S. and Jarabak, J. Studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Purification and partial characterization. J. Biol. Chem. 250 (1975) 2315-2318. 3 [PMID:234431] Lee, S.-C. and Levine, L. Prostaglandin metabolism. II. Identification of two 15-hydroxyprostaglandin dehydrogenase types. J. Biol. Chem. 250 (1975) 548-552. 4 [PMID:803247] Lee, S.-C., Pong, S.-S., Katzen, D., Wu, K.-Y. and Levine, L. Distribution of prostaglandin E 9-ketoreductase and types I and II 15-hydroxyprostaglandin dehydrogenase in swine kidney medulla and cortex. Biochemistry 14 (1975) 142-145. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.141 ExPASy - ENZYME nomenclature database: 1.1.1.141 ERGO genome analysis and discovery system: 1.1.1.141 BRENDA, the Enzyme Database: 1.1.1.141 CAS: 9030-87-9 /// ENTRY EC 1.1.1.142 NAME D-pinitol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 5D-5-O-methyl-chiro-inositol:NADP+ oxidoreductase REACTION 5D-5-O-methyl-chiro-inositol + NADP+ = 5D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADPH + H+ SUBSTRATE 5D-5-O-methyl-chiro-inositol NADP+ PRODUCT 5D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone NADPH H+ REFERENCE 1 [PMID:4389340] Ruis, H. and Hoffmann-Ostenhof, O. Enzymic epimerization of sequoyitol to D-pinitol in Trifolium incarnatum. Eur. J. Biochem. 7 (1969) 442-448. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.142 ExPASy - ENZYME nomenclature database: 1.1.1.142 ERGO genome analysis and discovery system: 1.1.1.142 BRENDA, the Enzyme Database: 1.1.1.142 CAS: 37250-71-8 /// ENTRY EC 1.1.1.143 NAME sequoyitol dehydrogenase D-pinitol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 5-O-methyl-myo-inositol:NAD+ oxidoreductase REACTION 5-O-methyl-myo-inositol + NAD+ = 5D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+ SUBSTRATE 5-O-methyl-myo-inositol NAD+ PRODUCT 5D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone NADH H+ REFERENCE 1 [PMID:4389340] Ruis, H. and Hoffmann-Ostenhof, O. Enzymic epimerization of sequoyitol to D-pinitol in Trifolium incarnatum. Eur. J. Biochem. 7 (1969) 442-448. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.143 ExPASy - ENZYME nomenclature database: 1.1.1.143 ERGO genome analysis and discovery system: 1.1.1.143 BRENDA, the Enzyme Database: 1.1.1.143 CAS: 37250-72-9 /// ENTRY EC 1.1.1.144 NAME perillyl-alcohol dehydrogenase perillyl alcohol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME perillyl-alcohol:NAD+ oxidoreductase REACTION perillyl alcohol + NAD+ = perillyl aldehyde + NADH + H+ SUBSTRATE perillyl alcohol NAD+ PRODUCT perillyl aldehyde NADH H+ COMMENT Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic. PATHWAY PATH: map00903 Limonene and pinene degradation REFERENCE 1 [PMID:4289759] Ballal, N.R., Bhattacharyya, P.K. and Rangachari, P.N. Perillyl alcohol dehydrogenase from a soil pseudomonad. Biochem. Biophys. Res. Commun. 23 (1966) 473-478. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.144 ExPASy - ENZYME nomenclature database: 1.1.1.144 ERGO genome analysis and discovery system: 1.1.1.144 UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.144 BRENDA, the Enzyme Database: 1.1.1.144 CAS: 37250-73-0 /// ENTRY EC 1.1.1.145 NAME 3beta-hydroxy-delta5-steroid dehydrogenase progesterone reductase delta5-3beta-hydroxysteroid dehydrogenase 3beta-hydroxy-5-ene steroid dehydrogenase 3beta-hydroxy steroid dehydrogenase/isomerase 3beta-hydroxy-delta5-C27-steroid dehydrogenase/isomerase 3beta-hydroxy-delta5-C27-steroid oxidoreductase 3beta-hydroxy-5-ene-steroid oxidoreductase steroid-delta5-3beta-ol dehydrogenase 3beta-HSDH 5-ene-3-beta-hydroxysteroid dehydrogenase 3beta-hydroxy-5-ene-steroid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3beta-hydroxy-delta5-steroid:NAD+ 3-oxidoreductase REACTION a 3beta-hydroxy-delta5-steroid + NAD+ = a 3-oxo-delta5-steroid + NADH + H+ SUBSTRATE 3beta-hydroxy-delta5-steroid NAD+ PRODUCT 3-oxo-delta5-steroid NADH H+ COMMENT Acts on 3beta-hydroxyandrost-5-en-17-one to form androst-4-ene-3,17-dione and on 3beta-hydroxypregn-5-en-20-one to form progesterone. PATHWAY PATH: map00140 C21-Steroid hormone metabolism PATH: map00150 Androgen and estrogen metabolism ORTHOLOG KO: K00070 3beta-hydroxy-delta5-steroid dehydrogenase GENES HSA: 3283(HSD3B1) 3284(HSD3B2) MMU: 15492(Hsd3b1) 15493(Hsd3b2) 15495(Hsd3b4) 15496(Hsd3b5) 15497(Hsd3b6) RNO: 24470(Hsd3b) 29632(Hsd3b1) SCE: YGL001C(ERG26) AGO: AFR001W(AFR001Wp) CAL: orf19.2909(ERG26) SPO: SPBC3F6.02c RBA: RB993 DISEASE MIM: 201810 Hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid REFERENCE 1 [PMID:4226148] Cheatum, S.G. and Warren, J.C. Purification and properties of 3-beta-hydroxysteroid dehydrogenase and delta-5-3-ketosteroid isomerase from bovine corpora lutea. Biochim. Biophys. Acta 122 (1966) 1-13. 2 Koritz, S.B. The conversion of prepnenolone to progesterone by small particle from rat adrenal. Biochemistry 3 (1964) 1098-1102. 3 Neville, A.M., Orr, J.C. and Engel, L.L. delta5-3beta-Hydroxy steroid dehydrogenase activities of bovine adrenal cortex. Biochem. J. 107 (1968) 20P. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.145 ExPASy - ENZYME nomenclature database: 1.1.1.145 ERGO genome analysis and discovery system: 1.1.1.145 BRENDA, the Enzyme Database: 1.1.1.145 CAS: 9044-85-3 /// ENTRY EC 1.1.1.146 NAME 11beta-hydroxysteroid dehydrogenase corticosteroid 11beta-dehydrogenase beta-hydroxysteroid dehydrogenase 11beta-hydroxy steroid dehydrogenase corticosteroid 11-reductase dehydrogenase, 11beta-hydroxy steroid CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 11beta-hydroxysteroid:NADP+ 11-oxidoreductase REACTION an 11beta-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH + H+ SUBSTRATE 11beta-hydroxysteroid NADP+ PRODUCT 11-oxosteroid NADPH H+ PATHWAY PATH: map00140 C21-Steroid hormone metabolism PATH: map00150 Androgen and estrogen metabolism ORTHOLOG KO: K00071 11beta-hydroxysteroid dehydrogenase GENES HSA: 3290(HSD11B1) 3291(HSD11B2) MMU: 15483(Hsd11b1) 15484(Hsd11b2) RNO: 25116(Hsd11b1) 25117(Hsd11b2) TTH: TTC1745 DISEASE MIM: 218030 Hydroxysteroid (11-beta) dehydrogenase 2 MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] STRUCTURES PDB: 1XSE 1XU7 1XU9 REFERENCE 1 [PMID:2808402] Agarwal, A.K., Monder, C., Eckstein, B. and White, P.C. Cloning and expression of rat cDNA encoding corticosteroid 11beta-dehydrogenase. J. Biol. Chem. 264 (1989) 18939-18943. 2 [PMID:4384445] Bush, I.E., Hunter, S.A. and Meigs, R.A. Metabolism of 11-oxygenated steroids. Metabolism in vitro by preparations of liver. Biochem. J. 107 (1968) 239-258. 3 [PMID:3139396] Lakshmi, V. and Monder, C. Purification and characterization of the corticosteroid 11beta-dehydrogenase component of the rat liver 11beta-hydroxysteroid dehydrogenase complex. Endocrinology 123 (1988) 2390-2398. 4 [PMID:2661206] Phillips, D.M., Lakshmi, V. and Monder, C. Corticosteroid 11beta-dehydrogenase in rat testis. Endocrinology 125 (1989) 209-216. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.146 ExPASy - ENZYME nomenclature database: 1.1.1.146 ERGO genome analysis and discovery system: 1.1.1.146 BRENDA, the Enzyme Database: 1.1.1.146 CAS: 9041-46-7 /// ENTRY EC 1.1.1.147 NAME 16alpha-hydroxysteroid dehydrogenase 16alpha-hydroxy steroid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 16alpha-hydroxysteroid:NAD(P)+ 16-oxidoreductase REACTION a 16alpha-hydroxysteroid + NAD(P)+ = a 16-oxosteroid + NAD(P)H + H+ SUBSTRATE 16alpha-hydroxysteroid NAD+ NADP+ PRODUCT 16-oxosteroid NADH NADPH H+ REFERENCE 1 [PMID:4380686] Meigs, R.A. and Ryan, K.J. 16-alpha-Hydroxysteroid dehydrogenase of rat kidney. Purification, assay, and properties. J. Biol. Chem. 241 (1966) 4011-4015. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.147 ExPASy - ENZYME nomenclature database: 1.1.1.147 ERGO genome analysis and discovery system: 1.1.1.147 BRENDA, the Enzyme Database: 1.1.1.147 CAS: 37250-74-1 /// ENTRY EC 1.1.1.148 NAME estradiol 17alpha-dehydrogenase 17alpha-estradiol dehydrogenase 17alpha-hydroxy steroid dehydrogenase 17alpha-hydroxy steroid oxidoreductase 17alpha-hydroxysteroid oxidoreductase estradiol 17alpha-oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 17alpha-hydroxysteroid:NAD(P)+ 17-oxidoreductase REACTION estradiol-17alpha + NAD(P)+ = estrone + NAD(P)H + H+ SUBSTRATE estradiol-17alpha NAD+ NADP+ PRODUCT estrone NADH NADPH H+ PATHWAY PATH: map00150 Androgen and estrogen metabolism REFERENCE 1 [PMID:4383682] Renwick, A.G.C. and Engel, L.L. The partial purification of 17alpha- and 17beta-estradiol dehydrogenase activities from chicken liver. Biochim. Biophys. Acta 146 (1967) 336-348. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.148 ExPASy - ENZYME nomenclature database: 1.1.1.148 ERGO genome analysis and discovery system: 1.1.1.148 BRENDA, the Enzyme Database: 1.1.1.148 CAS: 9044-91-1 /// ENTRY EC 1.1.1.149 NAME 20alpha-hydroxysteroid dehydrogenase 20alpha-hydroxy steroid dehydrogenase 20alpha-HSD 20alpha-HSDH CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 20alpha-hydroxysteroid:NAD(P)+ 20-oxidoreductase REACTION 17alpha,20alpha-dihydroxypregn-4-en-3-one + NAD(P)+ = 17alpha-hydroxyprogesterone + NAD(P)H + H+ SUBSTRATE 17alpha,20alpha-dihydroxypregn-4-en-3-one NAD+ NADP+ PRODUCT 17alpha-hydroxyprogesterone NADH NADPH H+ COMMENT A-specific with respect to NAD(P)+ (cf. EC 1.1.1.62 estradiol 17beta-dehydrogenase). PATHWAY PATH: map00140 C21-Steroid hormone metabolism ORTHOLOG KO: K05295 20alpha-hydroxysteroid dehydrogenase GENES MMU: 105349(Akr1c18) RNO: 171516(LOC171516) MOTIF PS: PS00062 [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY] PS: PS00063 [LIVM]-[PAIV]-[KR]-[ST]-x(4)-R-x(2)-[GSTAEQK]-[NSL]- x(2)-[LIVMFA] PS: PS00798 G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGC]-[AS]-x(5)-E-x(2)- [LIVM]-G STRUCTURES PDB: 1MRQ 1Q13 1Q5M REFERENCE 1 [PMID:4382486] Shikita, M., Inano, H. and Tamaoki, B. Further studies on 20alpha-hydroxysteroid dehydrogenase of rat testes. Biochemistry 6 (1967) 1760-1764. 2 [PMID:6935192] Strickler, R.C., Tobias, B. and Covey, D.F. Human placental 17beta-estradiol dehydrogenase and 20alpha-hydroxysteroid dehydrogenase. Two activities at a single enzyme active site. J. Biol. Chem. 256 (1981) 316-321. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.149 ExPASy - ENZYME nomenclature database: 1.1.1.149 ERGO genome analysis and discovery system: 1.1.1.149 BRENDA, the Enzyme Database: 1.1.1.149 CAS: 9040-08-8 /// ENTRY EC 1.1.1.150 NAME 21-hydroxysteroid dehydrogenase (NAD+) 21-hydroxysteroid dehydrogenase (NAD) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 21-hydroxysteroid:NAD+ 21-oxidoreductase REACTION pregnan-21-ol + NAD+ = pregnan-21-al + NADH + H+ SUBSTRATE pregnan-21-ol NAD+ PRODUCT pregnan-21-al NADH H+ COMMENT Acts on a number of 21-hydroxycorticosteroids. REFERENCE 1 Monder, C. and White, A. The 21-hydroxysteroid dehydrogenases of liver. A nicotinamide adenine dinucleotide phosphate dehydrogenase and two nicotinamide adenine dinucleotide dehydrogenases. J. Biol. Chem. 240 (1965) 71-77. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.150 ExPASy - ENZYME nomenclature database: 1.1.1.150 ERGO genome analysis and discovery system: 1.1.1.150 BRENDA, the Enzyme Database: 1.1.1.150 CAS: 37250-75-2 /// ENTRY EC 1.1.1.151 NAME 21-hydroxysteroid dehydrogenase (NADP+) 21-hydroxy steroid dehydrogenase 21-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) $dehydrogenase 21-hydroxy steroid dehydrogenase (nicotinamide adenine dinucleotide $phosphate) NADP-21-hydroxysteroid dehydrogenase 21-hydroxysteroid dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 21-hydroxysteroid:NADP+ 21-oxidoreductase REACTION pregnan-21-ol + NADP+ = pregnan-21-al + NADPH + H+ SUBSTRATE pregnan-21-ol NADP+ PRODUCT pregnan-21-al NADPH H+ COMMENT Acts on a number of 21-hydroxycorticosteroids. REFERENCE 1 Monder, C. and White, A. The 21-hydroxysteroid dehydrogenases of liver. A nicotinamide adenine dinucleotide phosphate dehydrogenase and two nicotinamide adenine dinucleotide dehydrogenases. J. Biol. Chem. 240 (1965) 71-77. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.151 ExPASy - ENZYME nomenclature database: 1.1.1.151 ERGO genome analysis and discovery system: 1.1.1.151 BRENDA, the Enzyme Database: 1.1.1.151 CAS: 37250-76-3 /// ENTRY EC 1.1.1.152 NAME 3alpha-hydroxy-5beta-androstan-17-one 3alpha-dehydrogenase etiocholanolone 3alpha-dehydrogenase 3alpha-hydroxy-5beta-steroid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3alpha-hydroxy-5beta-steroid:NAD+ 3-oxidoreductase REACTION 3alpha-hydroxy-5beta-androstan-17-one + NAD+ = 5beta-androstane-3,17-dione + NADH + H+ SUBSTRATE 3alpha-hydroxy-5beta-androstan-17-one NAD+ PRODUCT 5beta-androstane-3,17-dione NADH H+ PATHWAY PATH: map00150 Androgen and estrogen metabolism REFERENCE 1 [PMID:5365796] Roe, C.R. and Kaplan, N.O. Purification and substrate specificities of bacterial hydroxysteroid dehydrogenases. Biochemistry 8 (1969) 5093-5103. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.152 ExPASy - ENZYME nomenclature database: 1.1.1.152 ERGO genome analysis and discovery system: 1.1.1.152 BRENDA, the Enzyme Database: 1.1.1.152 CAS: 37250-77-4 /// ENTRY EC 1.1.1.153 NAME sepiapterin reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 7,8-dihydrobiopterin:NADP+ oxidoreductase REACTION 7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+ SUBSTRATE 7,8-dihydrobiopterin NADP+ PRODUCT sepiapterin NADPH H+ PATHWAY PATH: map00790 Folate biosynthesis ORTHOLOG KO: K00072 sepiapterin reductase GENES HSA: 6697(SPR) MMU: 20751(Spr) DME: CG12117-PA(CG12117) SYN: sll0330 ANA: all0968(fabG) DISEASE MIM: 182125 Sepiapterin reductase STRUCTURES PDB: 1NAS 1OAA 1SEP REFERENCE 1 Katoh, S. Sepiapterin reductase from horse liver: purification and properties of the enzyme. Arch. Biochem. Biophys. 146 (1971) 202-214. 2 [PMID:5969298] Matsubara, M., Katoh, S., Akino, M. and Kaufman, S. Sepiapterin reductase. Biochim. Biophys. Acta 122 (1966) 202-212. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.153 ExPASy - ENZYME nomenclature database: 1.1.1.153 ERGO genome analysis and discovery system: 1.1.1.153 BRENDA, the Enzyme Database: 1.1.1.153 CAS: 9059-48-7 /// ENTRY EC 1.1.1.154 NAME ureidoglycolate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S)-ureidoglycolate:NAD(P)+ oxidoreductase REACTION (S)-ureidoglycolate + NAD(P)+ = oxalureate + NAD(P)H + H+ SUBSTRATE (S)-ureidoglycolate NAD+ NADP+ PRODUCT oxalureate NADH NADPH H+ PATHWAY PATH: map00230 Purine metabolism ORTHOLOG KO: K00073 ureidoglycolate dehydrogenase GENES ECO: b0517(allD) ECJ: JW0505(ylbC) ECE: Z0672(ylbC) ECS: ECs0579 ECC: c0631 c3753 STY: STY0576(allD) STT: t2333(allD) STM: STM0528(allD) BLI: BL01097 BL01098 BLD: BLi01129 EFA: EF0388(allD) STRUCTURES PDB: 1XRH REFERENCE 1 [PMID:4399430] van der Drift, C., van Helvoort, P.E.M. and Vogels, G.D. S-Ureidoglycolate dehydrogenase: purification and properties. Arch. Biochem. Biophys. 145 (1971) 465-469. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.154 ExPASy - ENZYME nomenclature database: 1.1.1.154 ERGO genome analysis and discovery system: 1.1.1.154 BRENDA, the Enzyme Database: 1.1.1.154 CAS: 62213-62-1 /// ENTRY EC 1.1.1.155 Obsolete NAME Deleted entry CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Deleted entry: the enzyme is identical to EC 1.1.1.87, homoisocitrate dehydrogenase (EC 1.1.1.155 created 1976, deleted 2004) PATHWAY PATH: map00300 Lysine biosynthesis DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.155 ExPASy - ENZYME nomenclature database: 1.1.1.155 ERGO genome analysis and discovery system: 1.1.1.155 BRENDA, the Enzyme Database: 1.1.1.155 /// ENTRY EC 1.1.1.156 NAME glycerol 2-dehydrogenase (NADP+) dihydroxyacetone reductase dihydroxyacetone (reduced nicotinamide adenine dinucleotide $phosphate) reductase dihydroxyacetone reductase (NADPH) DHA oxidoreductase glycerol 2-dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME glycerol:NADP+ 2-oxidoreductase (glycerone-forming) REACTION glycerol + NADP+ = glycerone + NADPH + H+ SUBSTRATE glycerol NADP+ PRODUCT glycerone NADPH H+ PATHWAY PATH: map00561 Glycerolipid metabolism REFERENCE 1 [PMID:4146296] Ben-Amotz, A. and Avron, M. NADP specific dihydroxyacetone reductase from Dunaliella parva. FEBS Lett. 29 (1973) 153-155. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.156 ExPASy - ENZYME nomenclature database: 1.1.1.156 ERGO genome analysis and discovery system: 1.1.1.156 BRENDA, the Enzyme Database: 1.1.1.156 CAS: 39342-20-6 /// ENTRY EC 1.1.1.157 NAME 3-hydroxybutyryl-CoA dehydrogenase beta-hydroxybutyryl coenzyme A dehydrogenase L(+)-3-hydroxybutyryl-CoA dehydrogenase BHBD dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine $dinucleotide phosphate) L-(+)-3-hydroxybutyryl-CoA dehydrogenase beta-hydroxybutyryl-CoA dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase REACTION (S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+ SUBSTRATE (S)-3-hydroxybutanoyl-CoA NADP+ PRODUCT 3-acetoacetyl-CoA NADPH H+ PATHWAY PATH: map00632 Benzoate degradation via CoA ligation PATH: map00650 Butanoate metabolism ORTHOLOG KO: K00074 3-hydroxybutyryl-CoA dehydrogenase GENES ATH: At3g15290(K7L4.9) CME: CMC137C ECO: b1395(paaH) ECJ: JW1390(paaH) ECC: c2467 PAE: PA1628 PA3590 PPU: PP3282(paaC) PP3755(paaH) ACI: ACIAD1690(dcaH) LPN: lpg1942 CVI: CV2086(paaH) RSO: RS00676(paaH1) RS03581(paaH2) BPE: BP0217 BP3310(paaH) BPA: BPP0416 BPP1372 BPP2104 BPP2341 BPP4112(paaH) BBR: BB0418 BB1500 BB1792 BB2438 BB4583(paaH) BBA: Bd1850 MLO: mlr3490 mlr6793 SME: SMc00727(hbdA) ATU: Atu3597(hbdA) ATC: AGR_L_2460 BME: BMEI0099 BMEII0215 BMEII1020 BMS: BR1969(hbd) BRA0223 BRA1086 BJA: bll6223(hbdA) blr1379(hbdA) blr6087 RPA: RPA4748(hbdA) CCR: CC0715 BSU: BG11320(mmgB) BHA: BH0204(hbd) BH1995 BH3800(mmgB) BAN: BA5588 BAR: GBAA5588 BAA: BA_0444 BAT: BAS5192 BCE: BC5343 BCA: BCE5474 BCZ: BTZK5043(hbd) BLI: BL03926(mmgB) OIH: OB3012 CAC: CAC2708(hbd) CPE: CPE2297 CTC: CTC02423 TTE: TTE0548(fadB) MTU: Rv1715(fadB3) MTC: MT1754 MBO: Mb0477(fadB2) Mb1742(fadB3a) Mb1743(fadB3b) CEF: CE0323 CE2775 SCO: SCO3834(SCH69.04c) SCO5385(2SC6G5.29) SMA: SAV2870(fadC3) SAV4359(paaH) BLO: BL0058 STH: STH214 STH2584 STH2912 FNU: FN1019 TDE: TDE0610 PGI: PG1080 DRA: DR1068 TTH: TTC0898 TAC: Ta0947 TVO: TVG1148597 PTO: PTO1021 PTO1504 SSO: SSO0647(hdb-1) SSO2871(hdb-2) SSO2996(hdb-3) STO: ST1507 ST2094 MOTIF PS: PS00067 [DNE]-x(2)-[GA]-F-[LIVMFY]-x-[NT]-R-x(3)-[PA]- [LIVMFY](2)-x(5)-[LIVMFYCT]-[LIVMFY]-x(2)-[GV] REFERENCE 1 [PMID:4405720] Madan, V.K., Hillmer, P. and Gottschalk, G. Purification and properties of NADP-dependent L(+)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri. Eur. J. Biochem. 32 (1973) 51-56. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.157 ExPASy - ENZYME nomenclature database: 1.1.1.157 ERGO genome analysis and discovery system: 1.1.1.157 BRENDA, the Enzyme Database: 1.1.1.157 CAS: 39319-78-3 /// ENTRY EC 1.1.1.158 NAME UDP-N-acetylmuramate dehydrogenase MurB reductase UDP-N-acetylenolpyruvoylglucosamine reductase UDP-N-acetylglucosamine-enoylpyruvate reductase UDP-GlcNAc-enoylpyruvate reductase uridine diphosphoacetylpyruvoylglucosamine reductase uridine diphospho-N-acetylglucosamine-enolpyruvate reductase uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O- $lactylglucose:NADP-oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME UDP-N-acetylmuramate:NADP+ oxidoreductase REACTION UDP-N-acetylmuramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH + H+ SUBSTRATE UDP-N-acetylmuramate NADP+ PRODUCT UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine NADPH H+ COMMENT A flavoprotein (FAD). Sodium dithionite, sodium borohydride and, to a lesser extent, NADH, can replace NADPH. PATHWAY PATH: map00530 Aminosugars metabolism ORTHOLOG KO: K00075 UDP-N-acetylmuramate dehydrogenase GENES ECO: b3972(murB) ECJ: JW3940(murB) ECE: Z5543(murB) ECS: ECs4899 ECC: c4931(murB) STY: STY3742(murB) STT: t3489(murB) STM: STM4137(murB) YPE: YPO3760(murB) YPK: y0471(murB) YPM: YP3288(murB) YPS: YPTB0272(murB) SFL: SF4050(murB) SFX: S3690(murB) ECA: ECA0213(murB) PLU: plu4733(murB) BUC: BU045(murB) BAS: BUsg042(murB) BAB: bbp046(murB) WBR: Wbr0241(murB) BFL: Bfl183(murB) HIN: HI0268(murB) HDU: HD0081(murB) PMU: PM1589(murB) MSU: MS0028(murB) XFA: XF2572 XFT: PD1953(murB) XCC: XCC1787(murB) XAC: XAC1804(murB) VCH: VC0318 VVU: VV11197 VVY: VV3170 VPA: VP2932 PPR: PBPRA3446 PAE: PA2977(murB) PPU: PP1904(murB) PST: PSPTO3842(murB) ACI: ACIAD1945(murB) SON: SO0213(murB) CBU: CBU0137(murB) LPN: lpg2613(murB) MCA: MCA2427(murB) NME: NMB0811 NMA: NMA1021(murB) CVI: CV1592(murB) RSO: RS00729(murB) BMA: BMA0374(murB) BPS: BPSL0868(murB) BPE: BP2510(murB) BPA: BPP3497(murB) BBR: BB3945(murB) NEU: NE0993 HPY: HP1418(murB) HPJ: jhp1313 HHE: HH0439(murB) WSU: WS1488(murB) CJE: Cj1676(murB) GSU: GSU3067(murB) DVU: DVU2502(murB) BBA: Bd3233(murB) DPS: DP2896(murB) RPR: RP248(murB) RTY: RT0240(murB) RCO: RC0332(murB) WOL: WD0541(murB) MLO: mll1552 SME: SMc01868(murB) ATU: Atu2092(murB) ATC: AGR_C_3794 BME: BMEI0581 BMS: BR1429(murB) BJA: bll6600(murB) RPA: RPA3528(murB) BHE: BH11220(murB) BQU: BQ08840(murB) CCR: CC2545 BSU: BG10228(murB) BHA: BH2564(murB) BAN: BA4048(murB-1) BA5315(murB-2) BAR: GBAA4048(murB-1) GBAA5315(murB-2) BAA: BA_0174(murB) BA_4518(murB) BAT: BAS3760 BAS4937 BCE: BC3909 BC5063 BCA: BCE3955(murB) BCE5212(murB) BCZ: BTZK3668(murB) BTZK4798(murB) BTK: BT9727_3651(murB) BT9727_4778(murB) BLI: BL02244(murB) OIH: OB0556 SAU: SA0693 SAV: SAV0738 SAM: MW0700 SAR: SAR0792(murB) SAS: SAS0703 SEP: SE0520 LMO: lmo1420 LMF: LMOf2365_1439(murB) LIN: lin1459 LLA: L173881(murB) SPY: SPy1101(murB) SPM: spyM18_1063(murB) SPG: SpyM3_0763(murB) SPS: SPs0963 SPA: M6_Spy0823 SPN: SP1390 SPR: spr1247(murB) SAG: SAG1112(murB) SAN: gbs1179 SMU: SMU.972(murB) LPL: lp_0814(murB) LJO: LJ0887 EFA: EF2489 EF2733(murB) CAC: CAC0510(murB) CPE: CPE0353(murB) CTC: CTC02496 TTE: TTE1836(murB) MTU: Rv0482(murB) MTC: MT0500 MBO: Mb0492(murB) MLE: ML2447(murB) MPA: MAP3975(murB) CGL: NCgl0346(Cgl0353) NCgl0386(Cgl0397) CEF: CE0417 CDI: DIP0384 SCO: SCO4643(SCD82.14) SMA: SAV4905(murB) TWH: TW718(murB) TWS: TW734(murB) LXX: Lxx02830(murB) PAC: PPA1894 BLO: BL1561(murB) STH: STH1211 STH692 FNU: FN1455 RBA: RB2661(murB) CTR: CT831(murB) CMU: TC0218 CPN: CPn0988 CPA: CP0867 CPJ: CPj0988(murB) CPT: CpB1024 CCA: CCA00773(murB) PCU: pc1624(murB) BBU: BB0598(murB) TPA: TP0090 TDE: TDE0093 LIL: LA3930(murB) LIC: LIC13138(murB) BTH: BT1368 PGI: PG1342(murB) SYN: slr1424 SYW: SYNW0028(murB) SYC: syc2351_d(murB) TEL: tll0370 GVI: gll1780 glr2317 ANA: alr5066 PMA: Pro0021(murB) PMM: PMM0021(murB) PMT: PMT0026(murB) DRA: DR0628 TTH: TTC0721 AAE: aq_520(murB1) TMA: TM1714 STRUCTURES PDB: 1HSK 1MBB 1MBT 1UXY 2MBR REFERENCE 1 [PMID:4717533] Taku, A. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. IV. Activation of uridine diphospho-N-acetylenolpyruvylglucosamine reductase by monovalent cations. J. Biol. Chem. 248 (1973) 4971-1976. 2 [PMID:4394163] Taku, A., Gunetileke, K.G. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3. Purification and properties of uridine diphospho-N-acetylenolpyruvyl-glucosamine reductase. J. Biol. Chem. 245 (1970) 5012-5016. 3 [PMID:11699883] van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.158 ExPASy - ENZYME nomenclature database: 1.1.1.158 ERGO genome analysis and discovery system: 1.1.1.158 BRENDA, the Enzyme Database: 1.1.1.158 CAS: 39307-28-3 /// ENTRY EC 1.1.1.159 NAME 7alpha-hydroxysteroid dehydrogenase 7alpha-hydroxy steroid dehydrogenase 7alpha-HSDH CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 7alpha-hydroxysteroid:NAD+ 7-oxidoreductase REACTION 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NAD+ = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+ SUBSTRATE 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate NAD+ PRODUCT 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate NADH H+ COMMENT Catalyses the oxidation of the 7alpha-hydroxyl group of bile acids and alcohols both in their free and conjugated forms. The Bacteroides fragilis and Clostridium enzymes can also utilize NADP+. GENES ECO: b1619(hdhA) ECJ: JW1611(hdhA) ECE: Z2624(hdhA) ECS: ECs2327 ECC: c2011(hdhA) SFL: SF1644(hdhA) HPY: HP1014(hdhA) HPJ: jhp0409 HHE: HH1627 WSU: WS2222 BME: BMEI0405 BMEI0406 BMS: BR1618 MTU: Rv0927c MTC: MT0954 MBO: Mb0950c MPA: MAP0871c MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] STRUCTURES PDB: 1AHH 1AHI 1FMC REFERENCE 1 [PMID:786279] Haslewood, E.S. and Haslewood, G.A.D. The specificity of a 7alpha-hydroxy steroid dehydrogenase from Escherichia coli. Biochem. J. 157 (1976) 207-210. 2 [PMID:6945134] Macdonald, I.A. and Roach, P.D. Bile induction of 7alpha- and 7beta-hydroxysteroid dehydrogenases in Clostridium absonum. Biochim. Biophys. Acta 665 (1981) 262-269. 3 [PMID:4581498] Macdonald, I.A., Williams, C.N. and Mahony, D.E. 7alpha-Hydroxysteroid dehydrogenase from Escherichia coli B: preliminary studies. Biochim. Biophys. Acta 309 (1973) 243-253. 4 [PMID:236764] Macdonald, I.A., Williams, C.N., Mahony, D.E. and Christie, W.M. NAD- and NADP-dependent 7alpha-hydroxysteroid dehydrogenases from Bacteroides fragilis. Biochim. Biophys. Acta 384 (1975) 12-24. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.159 ExPASy - ENZYME nomenclature database: 1.1.1.159 ERGO genome analysis and discovery system: 1.1.1.159 BRENDA, the Enzyme Database: 1.1.1.159 CAS: 39361-64-3 /// ENTRY EC 1.1.1.160 NAME dihydrobunolol dehydrogenase bunolol reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (+/-)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1- $naphthol:NADP+ oxidoreductase REACTION (+/-)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1- $naphthol + NADP+ = (+/-)-5-[(tert-butylamino)-2'-hydroxypropoxy]- $3,4-dihydro-1(2H)-naphthalenone + NADPH + H+ SUBSTRATE (+/-)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1- $naphthol NADP+ PRODUCT (+/-)-5-[(tert-butylamino)-2'-hydroxypropoxy]-3,4-dihydro-1(2H)- $naphthalenone NADPH H+ COMMENT Also acts, more slowly, with NAD+. REFERENCE 1 [PMID:4560367] Leinweber, F.-J., Greenough, R.C., Schwender, C.F., Kaplan, H.R. and DiCarlo, F.J. Bunolol metabolism by cell-free preparations of human liver: biosynthesis of dihydrobunolol. Xenobiotica 2 (1972) 191-202. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.160 ExPASy - ENZYME nomenclature database: 1.1.1.160 ERGO genome analysis and discovery system: 1.1.1.160 BRENDA, the Enzyme Database: 1.1.1.160 CAS: 62213-61-0 /// ENTRY EC 1.1.1.161 NAME cholestanetetraol 26-dehydrogenase cholestanetetrol 26-dehydrogenase 5beta-cholestane-3alpha,7alpha,12alpha,26-tetrol dehydrogenase TEHC-NAD oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol:NAD+ $26-oxidoreductase REACTION 5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NAD+ = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + NADH + H+ SUBSTRATE 5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol NAD+ PRODUCT 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al NADH H+ PATHWAY PATH: map00120 Bile acid biosynthesis REFERENCE 1 [PMID:5914340] Masui, T., Herman, R. and Staple, E. The oxidation of 5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol to 5beta-cholestane-3alpha,7alpha,12alpha-triol-26-oic acid via 5beta-cholestane-3alpha,7alpha,12alpha-triol-26-al by rat liver. Biochim. Biophys. Acta 117 (1966) 266-268. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.161 ExPASy - ENZYME nomenclature database: 1.1.1.161 ERGO genome analysis and discovery system: 1.1.1.161 BRENDA, the Enzyme Database: 1.1.1.161 CAS: 62213-60-9 /// ENTRY EC 1.1.1.162 NAME erythrulose reductase D-erythrulose reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME erythritol:NADP+ oxidoreductase REACTION erythritol + NADP+ = D-erythrulose + NADPH + H+ SUBSTRATE erythritol NADP+ PRODUCT D-erythrulose NADPH H+ COMMENT NAD+ is also utilized, more slowly. REFERENCE 1 [PMID:4152124] Uehara, K., Tanimoto, T. and Sato, H. Studies on D-tetrose metabolism. IV. Purification and some properties of D-erythrulose reductase from beef liver. J. Biochem. (Tokyo) 75 (1974) 333-345. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.162 ExPASy - ENZYME nomenclature database: 1.1.1.162 ERGO genome analysis and discovery system: 1.1.1.162 BRENDA, the Enzyme Database: 1.1.1.162 CAS: 52064-49-0 /// ENTRY EC 1.1.1.163 NAME cyclopentanol dehydrogenase cyclopentanol:NADP+ oxidoreductase (incorrect) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME cyclopentanol:NAD+ oxidoreductase REACTION cyclopentanol + NAD+ = cyclopentanone + NADH + H+ SUBSTRATE cyclopentanol NAD+ PRODUCT cyclopentanone NADH H+ COMMENT 4-Methylcyclohexanol and cyclohexanol can also act as substrates. REFERENCE 1 [PMID:4349113] Griffin, M. and Trudgill, P.W. The metabolism of cyclopentanol by Pseudomonas N.C.I.B. 9872. Biochem. J. 129 (1972) 595-603. 2 [PMID:12406764] Iwaki, H., Hasegawa, Y., Wang, S., Kayser, M.M. and Lau, P.C. Cloning and characterization of a gene cluster involved in cyclopentanol metabolism in Comamonas sp. strain NCIMB 9872 and biotransformations effected by Escherichia coli-expressed cyclopentanone 1,2-monooxygenase. Appl. Environ. Microbiol. 68 (2002) 5671-5684; 69 (2003) 2414 (only). DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.163 ExPASy - ENZYME nomenclature database: 1.1.1.163 ERGO genome analysis and discovery system: 1.1.1.163 BRENDA, the Enzyme Database: 1.1.1.163 CAS: 37364-12-8 /// ENTRY EC 1.1.1.164 NAME hexadecanol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME hexadecanol:NAD+ oxidoreductase REACTION hexadecanol + NAD+ = hexadecanal + NADH + H+ SUBSTRATE hexadecanol NAD+ PRODUCT hexadecanal NADH H+ COMMENT The liver enzyme acts on long-chain alcohols from C8 to C16. The Euglena enzyme also oxidizes the corresponding aldehydes to fatty acids. REFERENCE 1 [PMID:4313936] Kolattukuday, P.E. Reduction of fatty acids to alcohols by cell-free preparations of Euglena gracilis. Biochemistry 9 (1970) 1095-1102. 2 [PMID:5432753] Stoffel, W., Le Kim, D. and Heyn, G. Metabolism of sphingosine bases. XIV. Sphinganine (dihydrosphingosine), an effective donor of the alk-1-enyl chain of plasmalogens. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 875-883. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.164 ExPASy - ENZYME nomenclature database: 1.1.1.164 ERGO genome analysis and discovery system: 1.1.1.164 BRENDA, the Enzyme Database: 1.1.1.164 CAS: 62213-59-6 /// ENTRY EC 1.1.1.165 NAME 2-alkyn-1-ol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 2-butyne-1,4-diol:NAD+ 1-oxidoreductase REACTION 2-butyne-1,4-diol + NAD+ = 4-hydroxy-2-butynal + NADH + H+ SUBSTRATE 2-butyne-1,4-diol NAD+ PRODUCT 4-hydroxy-2-butynal NADH H+ COMMENT Acts on a variety of 2-alkyn-1-ols, and also on 1,4-butanediol. NADP+ also acts as acceptor, but more slowly. REFERENCE 1 Miyoshi, T., Sato, H. and Harada, T. Purification and characterization of 2-alkyne-1-ol dehydrogenase induced by 2-butene-1,4-diol in Fusarium merismoides B11. Biochim. Biophys. Acta 358 (1974) 231-239. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.165 ExPASy - ENZYME nomenclature database: 1.1.1.165 ERGO genome analysis and discovery system: 1.1.1.165 BRENDA, the Enzyme Database: 1.1.1.165 CAS: 54576-94-2 /// ENTRY EC 1.1.1.166 NAME hydroxycyclohexanecarboxylate dehydrogenase dihydroxycyclohexanecarboxylate dehydrogenase (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate-NAD oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate:NAD+ $3-oxidoreductase REACTION (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate + NAD+ = (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate + NADH + H+ SUBSTRATE (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate NAD+ PRODUCT (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate NADH H+ COMMENT Acts on hydroxycyclohexanecarboxylates that have an equatorial carboxy group at C-1, an axial hydroxy group at C-3 and an equatorial hydroxy or carbonyl group at C-4, including (-)-quinate and (-)-shikimate. REFERENCE 1 [PMID:4375976] Whiting, G.C. and Coggins, R.A. A new nicotinamide-adenine dinucleotide-dependent hydroaromatic dehydrogenase of Lactobacillus plantarum and its role in formation of (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate. Biochem. J. 141 (1974) 35-42. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.166 ExPASy - ENZYME nomenclature database: 1.1.1.166 ERGO genome analysis and discovery system: 1.1.1.166 BRENDA, the Enzyme Database: 1.1.1.166 CAS: 55467-53-3 /// ENTRY EC 1.1.1.167 NAME hydroxymalonate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME hydroxymalonate:NAD+ oxidoreductase REACTION hydroxymalonate + NAD+ = oxomalonate + NADH + H+ SUBSTRATE hydroxymalonate NAD+ PRODUCT oxomalonate NADH H+ REFERENCE 1 Jukova, N.I., Klunova, S.M. and Philippovich, Y.B. In: Biochemistry of Insects, issue 17, V.I. Lenin State Pedagogical Institute, Moscow, 1971, p. 56. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.167 ExPASy - ENZYME nomenclature database: 1.1.1.167 ERGO genome analysis and discovery system: 1.1.1.167 BRENDA, the Enzyme Database: 1.1.1.167 CAS: 58693-60-0 /// ENTRY EC 1.1.1.168 NAME 2-dehydropantolactone reductase (A-specific) 2-oxopantoyl lactone reductase ketopantoyl lactone reductase 2-ketopantoyl lactone reductase 2-dehydropantoyl-lactone reductase (A-specific) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-pantolactone:NADP+ oxidoreductase (A-specific) REACTION (R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+ SUBSTRATE (R)-pantolactone NADP+ PRODUCT 2-dehydropantolactone NADPH H+ COMMENT The yeast enzyme differs from that from Escherichia coli [EC 1.1.1.214 2-dehydropantolactone reductase (B-specific)], which is specific for the B-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase. REFERENCE 1 King, H.L., Jr. and Wilken, D.R. Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase. J. Biol. Chem. 247 (1972) 4689-4695. 2 [PMID:234966] Wilken, D.R., King, H.L., Jr. and Dyar, R.E. Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate. J. Biol. Chem. 250 (1975) 2311-2314. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.168 ExPASy - ENZYME nomenclature database: 1.1.1.168 ERGO genome analysis and discovery system: 1.1.1.168 BRENDA, the Enzyme Database: 1.1.1.168 CAS: 37211-75-9 /// ENTRY EC 1.1.1.169 NAME 2-dehydropantoate 2-reductase 2-oxopantoate reductase 2-ketopantoate reductase 2-ketopantoic acid reductase ketopantoate reductase ketopantoic acid reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-pantoate:NADP+ 2-oxidoreductase REACTION (R)-pantoate + NADP+ = 2-dehydropantoate + NADPH + H+ SUBSTRATE (R)-pantoate NADP+ PRODUCT 2-dehydropantoate NADPH H+ PATHWAY PATH: map00770 Pantothenate and CoA biosynthesis ORTHOLOG KO: K00077 2-dehydropantoate 2-reductase GENES SCE: YHR063C(PAN5) AGO: AAL044C(AAL044Cp) CAL: orf19.4006(PAN5) SPO: SPBPB2B2.09c ECO: b0425(apbA) ECJ: JW0415(apbA) ECE: Z0528(apbA) ECS: ECs0479 ECC: c0536(apbA) STY: STY0473(apbA) STY2819 STT: t0284 t2430(apbA) STM: STM0434(apbA) STM2573 YPE: YPO3171(apbA) YPK: y1014(apbA) YPM: YP0760(apbA) YPS: YPTB0945(panE) SFL: SF0362(apbA) SFX: S0370(apbA) ECA: ECA1136(panE) ECA1579 PLU: plu3882(apbA) WBR: Wbr0629(apbA) VCH: VC2307 VVU: VV11810 VVY: VV2602 VPA: VP2363 PPR: PBPRA0812(apbA) PAE: PA4397 PPU: PP1351 PP2998 PST: PSPTO4394(panE-2) SON: SO3817(panE) MCA: MCA2523(panE) BMA: BMA0348(panE-1) BMA1471(panE-2) BMA2264(panE-3) BPE: BP1360 BBR: BB2814 GSU: GSU2683(panE) DPS: DP0071 MLO: mll6982 BJA: bll3147 bll6396 blr0117 blr0589 RPA: RPA1943(panE) RPA4562(apbA) CCR: CC0261 BSU: BG13369(ylbQ) BHA: BH2579(apbA) BAN: BA1884 BA4059 BAR: GBAA1884 GBAA4059 BAA: BA_2386(apbA) BA_4530(apbA) BAT: BAS1746 BAS3771 BCE: BC1806 BC3920 BCA: BCE1964 BCE3966 BCZ: BTZK1696(panE) BTZK3679(panE) BTK: BT9727_1723(panE) BT9727_3662(panE) BLI: BL05158(panE) OIH: OB3273 SAU: SA2232 SA2393 SAV: SAV2443 SAV2600 SAM: MW2367 MW2519 SAR: SAR2533 SAR2678 SAS: SAS2335 SAS2485 SEP: SE2009 SE2142 LMO: lmo2046 LMF: LMOf2365_2077(panE) LIN: lin2152 LLA: L157055(panE) SPY: SPy0852(apbA) SPM: spyM18_0911(apbA) SPG: SpyM3_0577(apbA) SPS: SPs1277 SPA: M6_Spy0678 SAG: SAG1351 SAN: gbs1421 LPL: lp_2532(panE1) lp_2788(panE2) EFA: EF0517 EF1655 EF2445 CAC: CAC2937 CPE: CPE0786(apbA) MTU: Rv2573 MTC: MT2649 MBO: Mb2603 MPA: MAP1062c MAP4016c CGL: NCgl1044(Cgl1089) CEF: CE1145 SCO: SCO6562(SC4B5.12c) SMA: SAV1833 RBA: RB12638(apbA) RB3312 LIL: LA2190(panE1) LA3613(panE2) LIC: LIC10594(panE2) LIC11735(apbA) ANA: all1319 AAE: aq_1727 MMP: MMP0672 AFU: AF1695(apbA) HAL: VNG0730C HMA: rrnAC3068(panE) PHO: PH1390 PAB: PAB0512(apbA) PFU: PF1396 APE: APE0677 PAI: PAE3409 STRUCTURES PDB: 1KS9 REFERENCE 1 King, H.L., Jr. and Wilken, D.R. Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase. J. Biol. Chem. 247 (1972) 4689-4695. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.169 ExPASy - ENZYME nomenclature database: 1.1.1.169 ERGO genome analysis and discovery system: 1.1.1.169 BRENDA, the Enzyme Database: 1.1.1.169 CAS: 37211-74-8 /// ENTRY EC 1.1.1.170 NAME sterol-4alpha-carboxylate 3-dehydrogenase (decarboxylating) 3beta-hydroxy-4beta-methylcholestenecarboxylate 3-dehydrogenase $(decarboxylating) 3beta-hydroxy-4beta-methylcholestenoate dehydrogenase sterol 4alpha-carboxylic decarboxylase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha- $carboxylate:NAD(P)+ 3-oxidoreductase (decarboxylating) REACTION 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + NAD(P)+ = 4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NAD(P)H SUBSTRATE 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate NAD+ NADP+ PRODUCT 4alpha-methyl-5alpha-cholest-7-en-3-one CO2 NADH NADPH COMMENT Also acts on 3beta-hydroxy-5alpha-cholest-7-ene-4alpha-carboxylate. REFERENCE 1 [PMID:7430141] Brady, D.R., Crowder, R.D. and Hayes, W.J. Mixed function oxidases in sterol metabolism. Source of reducing equivalents. J. Biol. Chem. 255 (1980) 10624-10629. 2 [PMID:4401584] Rahimtula, A.D. and Gaylor, J.L. Partial purification of a microsomal sterol 4alpha-carboxylic acid decarboxylase. J. Biol. Chem. 247 (1972) 9-15. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.170 ExPASy - ENZYME nomenclature database: 1.1.1.170 ERGO genome analysis and discovery system: 1.1.1.170 BRENDA, the Enzyme Database: 1.1.1.170 CAS: 71822-23-6 /// ENTRY EC 1.1.1.171 Obsolete NAME Transferred to 1.5.1.20 CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Transferred entry: now EC 1.5.1.20 methylenetetrahydrofolate reductase (NADPH) (EC 1.1.1.171 created 1978, deleted 1984) DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.171 ExPASy - ENZYME nomenclature database: 1.1.1.171 ERGO genome analysis and discovery system: 1.1.1.171 BRENDA, the Enzyme Database: 1.1.1.171 /// ENTRY EC 1.1.1.172 NAME 2-oxoadipate reductase 2-ketoadipate reductase alpha-ketoadipate reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 2-hydroxyadipate:NAD+ 2-oxidoreductase REACTION 2-hydroxyadipate + NAD+ = 2-oxoadipate + NADH + H+ SUBSTRATE 2-hydroxyadipate NAD+ PRODUCT 2-oxoadipate NADH H+ REFERENCE 1 [PMID:185965] Suda, T., Robinson, J.C. and Fjellstedt, T.A. Purification and properties of alpha-ketoadipate reductase, a newly discovered enzyme from human placenta. Arch. Biochem. Biophys. 176 (1976) 610-620. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.172 ExPASy - ENZYME nomenclature database: 1.1.1.172 ERGO genome analysis and discovery system: 1.1.1.172 BRENDA, the Enzyme Database: 1.1.1.172 CAS: 61116-21-0 /// ENTRY EC 1.1.1.173 NAME L-rhamnose 1-dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-rhamnofuranose:NAD+ 1-oxidoreductase REACTION L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+ SUBSTRATE L-rhamnofuranose NAD+ PRODUCT L-rhamno-1,4-lactone NADH H+ PATHWAY PATH: map00051 Fructose and mannose metabolism REFERENCE 1 Rigo, L.U., Marechal, L.R., Vieira, M.M. and Veiga, L.A. Oxidative pathway for L-rhamnose degradation in Pallularia pullulans. Can. J. Microbiol. 31 (1985) 817-822. 2 [PMID:8142] Rigo, L.U., Nakano, M., Veiga, L.A. and Feingold, D.S. L-Rhamnose dehydrogenase of Pullularia pullulans. Biochim. Biophys. Acta 445 (1976) 286-293. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.173 ExPASy - ENZYME nomenclature database: 1.1.1.173 ERGO genome analysis and discovery system: 1.1.1.173 BRENDA, the Enzyme Database: 1.1.1.173 CAS: 52227-67-5 /// ENTRY EC 1.1.1.174 NAME cyclohexane-1,2-diol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME trans-cyclohexane-1,2-diol:NAD+ 1-oxidoreductase REACTION trans-cyclohexane-1,2-diol + NAD+ = 2-hydroxycyclohexan-1-one + NADH + H+ SUBSTRATE trans-cyclohexane-1,2-diol NAD+ PRODUCT 2-hydroxycyclohexan-1-one NADH H+ COMMENT Also oxidizes, more slowly, the cis isomer and 2-hydroxy-cyclohexanone. PATHWAY PATH: map00930 Caprolactam degradation REFERENCE 1 [PMID:856571] Davey, J.F. and Trudgill, P.W. The metabolism of trans-cyclohexan-1,2-diol by an Acinetobacter species. Eur. J. Biochem. 74 (1977) 115-127. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.174 ExPASy - ENZYME nomenclature database: 1.1.1.174 ERGO genome analysis and discovery system: 1.1.1.174 BRENDA, the Enzyme Database: 1.1.1.174 CAS: 62628-27-7 /// ENTRY EC 1.1.1.175 NAME D-xylose 1-dehydrogenase NAD-D-xylose D-xylose dehydrogenase (NAD)-linked D-xylose dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-xylose:NAD+ 1-oxidoreductase REACTION D-xylose + NAD+ = D-xylonolactone + NADH + H+ SUBSTRATE D-xylose NAD+ PRODUCT D-xylonolactone NADH H+ PATHWAY PATH: map00040 Pentose and glucuronate interconversions REFERENCE 1 Yamanaka, K., Gino, M. and Kaneda, R. A specific NAD-D-xylose dehydrogenase from Arthrobacter sp. Agric. Biol. Chem. 41 (1977) 1493-1499. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.175 ExPASy - ENZYME nomenclature database: 1.1.1.175 ERGO genome analysis and discovery system: 1.1.1.175 BRENDA, the Enzyme Database: 1.1.1.175 CAS: 62931-20-8 /// ENTRY EC 1.1.1.176 NAME 12alpha-hydroxysteroid dehydrogenase 12alpha-hydroxy steroid dehydrogenase NAD-dependent 12alpha-hydroxysteroid dehydrogenase NADP-12alpha-hydroxysteroid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 12alpha-hydroxysteroid:NADP+ 12-oxidoreductase REACTION 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NADP+ = 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADPH + H+ SUBSTRATE 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate NADP+ PRODUCT 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate NADPH H+ COMMENT Catalyses the oxidation of the 12alpha-hydroxy group of bile acids, both in their free and conjugated form. Also acts on bile alcohols. REFERENCE 1 [PMID:201289] Macdonald, I.A., Mahony, D.E., Jellett, J.F. and Meier, C.E. NAD-dependent 3alpha- and 12alpha-hydroxysteroid dehydrogenase activities from Eubacterium lentum ATCC no. 25559. Biochim. Biophys. Acta 489 (1977) 466-476. 2 [PMID:921266] Mahony, D.E., Meier, C.E., Macdonald, I.A. and Holdeman, L.V. Bile salt degradation by nonfermentative clostridia. Appl. Environ. Microbiol. 34 (1977) 419-423. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.176 ExPASy - ENZYME nomenclature database: 1.1.1.176 ERGO genome analysis and discovery system: 1.1.1.176 BRENDA, the Enzyme Database: 1.1.1.176 CAS: 61642-40-8 /// ENTRY EC 1.1.1.177 NAME glycerol-3-phosphate 1-dehydrogenase (NADP+) glycerol phosphate (nicotinamide adenine dinucleotide phosphate) $dehydrogenase L-glycerol 3-phosphate:NADP oxidoreductase glycerin-3-phosphate dehydrogenase NADPH-dependent glycerin-3-phosphate dehydrogenase glycerol-3-phosphate 1-dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME sn-glycerol-3-phosphate:NADP+ 1-oxidoreductase REACTION sn-glycerol 3-phosphate + NADP+ = D-glyceraldehyde 3-phosphate + NADPH + H+ SUBSTRATE sn-glycerol 3-phosphate NADP+ PRODUCT D-glyceraldehyde 3-phosphate NADPH H+ REFERENCE 1 Glushankov, P.E., Epifanova, V.E. and Kolotilova, A.I. Pentose phosphate pathway of carbohydrate metabolism and NADP-dependent glycerol 3-phosphate dehydrogenase activity in some white rat tissues. [in Russian] Biokhimiya 41 (1976) 1788-1790. 2 [PMID:4152128] Wood, T. Catalysis of pentose phosphate pathway reactions by cytoplasmic fractions from muscle, uterus and liver of the rat, and the presence of a reduced nicotinamide-adenine dinucleotide phosphate-triose phosphate oxidoreductase in rat muscle. Biochem. J. 138 (1974) 71-76. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.177 ExPASy - ENZYME nomenclature database: 1.1.1.177 ERGO genome analysis and discovery system: 1.1.1.177 BRENDA, the Enzyme Database: 1.1.1.177 CAS: 37213-46-0 /// ENTRY EC 1.1.1.178 NAME 3-hydroxy-2-methylbutyryl-CoA dehydrogenase 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase 2-methyl-3-hydroxy-butyryl CoA dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA:NAD+ oxidoreductase REACTION (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH + H+ SUBSTRATE (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA NAD+ PRODUCT 2-methylacetoacetyl-CoA NADH H+ COMMENT Also acts, more slowly, on (2S,3S)-2-hydroxy-3-methylpentanoyl-CoA. PATHWAY PATH: map00280 Valine, leucine and isoleucine degradation REFERENCE 1 [PMID:4150713] Conrad, R.S., Massey, L.K. and Sokatch, J.R. D- and L-isoleucine metabolism and regulation of their pathways in Pseudomonas putida. J. Bacteriol. 118 (1974) 103-111. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.178 ExPASy - ENZYME nomenclature database: 1.1.1.178 ERGO genome analysis and discovery system: 1.1.1.178 BRENDA, the Enzyme Database: 1.1.1.178 CAS: 52227-66-4 /// ENTRY EC 1.1.1.179 NAME D-xylose 1-dehydrogenase (NADP+) D-xylose (nicotinamide adenine dinucleotide phosphate) dehydrogenase D-xylose-NADP dehydrogenase D-xylose:NADP+ oxidoreductase D-xylose 1-dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-xylose:NADP+ 1-oxidoreductase REACTION D-xylose + NADP+ = D-xylono-1,5-lactone + NADPH + H+ SUBSTRATE D-xylose NADP+ PRODUCT D-xylono-1,5-lactone NADPH H+ COMMENT Also acts, more slowly, on L-arabinose and D-ribose. GENES CAL: orf19.4317(GRE3) BME: BMEI2003 REFERENCE 1 Wissler, J.H. D-Xylose:NADP oxidoreductase of arterial vessels and eye lens: a new enzyme and a final link in ATP-independent cycling of reducing eqivalents in aldose-polyol-ketose interconversion. Hoppe-Seyler's Z. Physiol. Chem. 358 (1977) 1300-1301. 2 Wissler, J.H. Direct spectrophotometric and specific quantitative determination of free and bound D-xylose by analytical application of a new enzyme, D-xylose:NADP-oxidoreductase. Fresenius' Z. Anal. Chem. 290 (1978) 179-180. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.179 ExPASy - ENZYME nomenclature database: 1.1.1.179 ERGO genome analysis and discovery system: 1.1.1.179 BRENDA, the Enzyme Database: 1.1.1.179 CAS: 83534-37-6 /// ENTRY EC 1.1.1.180 Obsolete NAME Deleted entry CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Deleted entry: mannonate dehydrogenase (NAD(P)+). Now included with EC 1.1.1.131 mannuronate reductase (EC 1.1.1.180 created 1983, deleted 1984) DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.180 ExPASy - ENZYME nomenclature database: 1.1.1.180 ERGO genome analysis and discovery system: 1.1.1.180 BRENDA, the Enzyme Database: 1.1.1.180 /// ENTRY EC 1.1.1.181 NAME cholest-5-ene-3beta,7alpha-diol 3beta-dehydrogenase 3beta-hydroxy-delta5-C27-steroid oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME Cholest-5-ene-3beta,7alpha-diol:NAD+ 3-oxidoreductase REACTION cholest-5-ene-3beta,7alpha-diol + NAD+ = 7alpha-hydroxycholest-4-en-3-one + NADH + H+ SUBSTRATE cholest-5-ene-3beta,7alpha-diol NAD+ PRODUCT 7alpha-hydroxycholest-4-en-3-one NADH H+ COMMENT Highly specific for 3beta-hydroxy-C27-steroids with delta5-double bond. PATHWAY PATH: map00120 Bile acid biosynthesis REFERENCE 1 [PMID:6937465] Wikvall, K. Purification and properties of a 3beta-hydroxy-delta5-C27-steroid oxidoreductase from rabbit liver microsomes. J. Biol. Chem. 256 (1981) 3376-3380. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.181 ExPASy - ENZYME nomenclature database: 1.1.1.181 ERGO genome analysis and discovery system: 1.1.1.181 BRENDA, the Enzyme Database: 1.1.1.181 CAS: 56626-16-5 /// ENTRY EC 1.1.1.182 Obsolete NAME Deleted entry CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Deleted entry: fenchol dehydrogenase. Now included with EC 1.1.1.198 (+)-borneol dehydrogenase, EC 1.1.1.227 (-)-borneol dehydrogenase and EC 1.1.1.228 (+)-sabinol dehydrogenase (EC 1.1.1.182 created 1983, deleted 1990) DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.182 ExPASy - ENZYME nomenclature database: 1.1.1.182 ERGO genome analysis and discovery system: 1.1.1.182 BRENDA, the Enzyme Database: 1.1.1.182 /// ENTRY EC 1.1.1.183 NAME geraniol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME geraniol:NADP+ oxidoreductase REACTION geraniol + NADP+ = geranial + NADPH + H+ SUBSTRATE geraniol NADP+ PRODUCT geranial NADPH H+ COMMENT Also acts, more slowly, on nerol, farnesol and citronellol. REFERENCE 1 Potty, V.H. and Bruemmer, J.H. Oxidation of geraniol by an enzyme system from orange. Phytochemistry 9 (1970) 1001-1007. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.183 ExPASy - ENZYME nomenclature database: 1.1.1.183 ERGO genome analysis and discovery system: 1.1.1.183 BRENDA, the Enzyme Database: 1.1.1.183 CAS: 56802-96-1 /// ENTRY EC 1.1.1.184 NAME carbonyl reductase (NADPH) aldehyde reductase 1 prostaglandin 9-ketoreductase xenobiotic ketone reductase NADPH2-dependent carbonyl reductase ALR3 carbonyl reductase nonspecific NADPH-dependent carbonyl reductase carbonyl reductase (NADPH2) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME secondary-alcohol:NADP+ oxidoreductase REACTION R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+ SUBSTRATE R-CHOH-R' NADP+ PRODUCT R-CO-R' NADPH H+ COMMENT Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin and prostaglandins E and F, reducing them to the corresponding alcohol. B-specific with respect to NADPH [cf. EC 1.1.1.2 alcohol dehydrogenase (NADP+)]. PATHWAY PATH: map00590 Prostaglandin and leukotriene metabolism ORTHOLOG KO: K00079 carbonyl reductase (NADPH) GENES HSA: 873(CBR1) 874(CBR3) MMU: 12408(Cbr1) 12409(Cbr2) RNO: 29224(Cbr1) CEL: R11D1.11 CAL: orf19.2896(SOU1) orf19.2897(SOU2) orf19.6322(ARD1) orf19.732(SPS22) RSO: RS05193 BME: BMEII0062 DISEASE MIM: 603608 Carbonyl reductase 3 MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] STRUCTURES PDB: 1CYD REFERENCE 1 [PMID:31888] Ahmed, N.K., Felsted, R.L. and Bachur, N.R. Heterogeneity of anthracycline antibiotic carbonyl reductases in mammalian livers. Biochem. Pharmacol. 27 (1978) 2713-2719. 2 [PMID:666816] Lin, Y.M. and Jarabak, J. Isolation of two proteins with 9-ketoprostaglandin reductase and NADP-linked 15-hydroxyprostaglandin dehydrogenase activities and studies on their inhibition. Biochem. Biophys. Res. Commun. 81 (1978) 1227-1234. 3 [PMID:7005231] Wermuth, B. Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. 256 (1981) 1206-1213. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.184 ExPASy - ENZYME nomenclature database: 1.1.1.184 ERGO genome analysis and discovery system: 1.1.1.184 BRENDA, the Enzyme Database: 1.1.1.184 CAS: 89700-36-7 /// ENTRY EC 1.1.1.185 NAME L-glycol dehydrogenase glycol (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase L-(+)-glycol:NAD(P) oxidoreductase L-glycol:NAD(P) dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME L-glycol:NAD(P)+ oxidoreductase REACTION an L-glycol + NAD(P)+ = a 2-hydroxycarbonyl compound + NAD(P)H + H+ SUBSTRATE L-glycol NAD+ NADP+ PRODUCT 2-hydroxycarbonyl compound NADH NADPH H+ COMMENT The 2-hydroxycarbonyl compound formed can be further oxidized to a vicinal dicarbonyl compound. In the reverse direction, vicinal diketones, glyceraldehyde, glyoxal, methylglyoxal, 2-oxo-hydroxyketones and 2-ketoacid esters can be reduced. REFERENCE 1 [PMID:7018582] Bernardo, A., Burgos, J. and Martin, R. Purification and some properties of L-glycol dehydrogenase from hen's muscle. Biochim. Biophys. Acta 659 (1981) 189-198. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.185 ExPASy - ENZYME nomenclature database: 1.1.1.185 ERGO genome analysis and discovery system: 1.1.1.185 BRENDA, the Enzyme Database: 1.1.1.185 CAS: 77967-75-0 /// ENTRY EC 1.1.1.186 NAME dTDP-galactose 6-dehydrogenase thymidine-diphosphate-galactose dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME dTDP-D-galactose:NADP+ 6-oxidoreductase REACTION dTDP-D-galactose + 2 NADP+ + H2O = dTDP-D-galacturonate + 2 NADPH + 2 H+ SUBSTRATE dTDP-D-galactose NADP+ H2O PRODUCT dTDP-D-galacturonate NADPH H+ PATHWAY PATH: map00520 Nucleotide sugars metabolism REFERENCE 1 [PMID:4381717] Katan, R. and Avigad, G. NADP dependent oxidation of TDP-glucose by an enzyme system from sugar beets. Biochem. Biophys. Res. Commun. 24 (1966) 18-24. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.186 ExPASy - ENZYME nomenclature database: 1.1.1.186 ERGO genome analysis and discovery system: 1.1.1.186 BRENDA, the Enzyme Database: 1.1.1.186 /// ENTRY EC 1.1.1.187 NAME GDP-4-dehydro-D-rhamnose reductase GDP-4-keto-6-deoxy-D-mannose reductase GDP-4-keto-D-rhamnose reductase guanosine diphosphate-4-keto-D-rhamnose reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME GDP-6-deoxy-D-mannose:NAD(P)+ 4-oxidoreductase REACTION GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+ SUBSTRATE GDP-6-deoxy-D-mannose NAD+ NADP+ PRODUCT GDP-4-dehydro-6-deoxy-D-mannose NADH NADPH H+ COMMENT In the reverse reaction, a mixture of GDP-D-rhamnose and its C-4 epimer is formed. PATHWAY PATH: map00051 Fructose and mannose metabolism ORTHOLOG KO: K00080 GDP-4-dehydro-D-rhamnose reductase GENES DME: CG3495-PA(CG3495) REFERENCE 1 [PMID:4386238] Barber, G.A. The synthesis of guanosine 5'-diphosphate D-rhamnose by enzymes of a higher plant. Biochim. Biophys. Acta 165 (1968) 68-75. 2 [PMID:4398966] Winkler, N.W. and Markovitz, A. Guanosine diphosphate-4-keto-D-rhamnose reductase. A non-stereoselective enzyme. J. Biol. Chem. 246 (1971) 5868-5876. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.187 ExPASy - ENZYME nomenclature database: 1.1.1.187 ERGO genome analysis and discovery system: 1.1.1.187 BRENDA, the Enzyme Database: 1.1.1.187 CAS: 9075-56-3 /// ENTRY EC 1.1.1.188 NAME prostaglandin-F synthase prostaglandin-D2 11-reductase reductase, 15-hydroxy-11-oxoprostaglandin PGD2 11-ketoreductase PGF2alpha synthetase prostaglandin 11-ketoreductase prostaglandin delta2-ketoreductase prostaglandin F synthase prostaglandin F synthetase synthetase, prostaglandin F2alpha PGF synthetase NADPH-dependent prostaglandin D2 11-keto reductase prostaglandin 11-keto reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13- $dienoate:NADP+ 11-oxidoreductase REACTION (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+ SUBSTRATE (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate NADP+ PRODUCT (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate NADPH H+ COMMENT Reduces prostaglandin D2 and prostaglandin H2 to prostaglandin F2; prostaglandin D2 is not an intermediate in the reduction of prostaglandin H2. Also catalyses the reduction of a number of carbonyl compounds, such as 9,10-phenanthroquinone and 4-nitro-acetophenone. PATHWAY PATH: map00590 Prostaglandin and leukotriene metabolism ORTHOLOG KO: K04119 prostaglandin-F synthase GENES HSA: 8644(AKR1C3) MOTIF PS: PS00062 [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY] PS: PS00063 [LIVM]-[PAIV]-[KR]-[ST]-x(4)-R-x(2)-[GSTAEQK]-[NSL]- x(2)-[LIVMFA] PS: PS00798 G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGC]-[AS]-x(5)-E-x(2)- [LIVM]-G STRUCTURES PDB: 1RY0 1RY8 1XF0 REFERENCE 1 [PMID:7248318] Reingold, D.F., Kawasaki, A. and Needleman, P. A novel prostaglandin 11-keto reductase found in rabbit liver. Biochim. Biophys. Acta 659 (1981) 179-188. 2 Watanabe, K., Shimizu, T. and Hayaishi, O. Enzymatic conversion of prostaglandin-D2 to prostaglandin-F2alpha in the rat lung. Biochem. Int. 2 (1981) 603-610. 3 [PMID:3858278] Watanabe, K., Yoshida, R., Shimizu, T. and Hayaishi, O. Enzymatic formation of prostaglandin F2alpha from prostaglandin H2 and D2. Purification and properties of prostaglandin F synthetase from bovine lung. J. Biol. Chem. 260 (1985) 7035-7041. 4 [PMID:7248317] Wong, P.Y.-K. Purification and partial characterization of prostaglandin D2 11-keto reductase in rabbit liver. Biochim. Biophys. Acta 659 (1981) 169-178. 5 [PMID:7132748] Wong, P.Y.-K. Purification of PGD2 11-ketoreductase from rabbit liver. Methods Enzymol. 86 (1982) 117-125. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.188 ExPASy - ENZYME nomenclature database: 1.1.1.188 ERGO genome analysis and discovery system: 1.1.1.188 BRENDA, the Enzyme Database: 1.1.1.188 CAS: 55976-95-9 /// ENTRY EC 1.1.1.189 NAME prostaglandin-E2 9-reductase PGE2-9-OR reductase, 15-hydroxy-9-oxoprostaglandin 9-keto-prostaglandin E2 reductase 9-ketoprostaglandin reductase PGE-9-ketoreductase PGE2 9-oxoreductase PGE2-9-ketoreductase prostaglandin 9-ketoreductase prostaglandin E 9-ketoreductase prostaglandin E2-9-oxoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13- $dienoate:NADP+ 9-oxidoreductase REACTION (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH + H+ SUBSTRATE (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate NADP+ PRODUCT (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate NADPH H+ COMMENT Reduces prostaglandin E2 to prostaglandin F2alpha. A number of other 9-oxo- and 15-oxo-prostaglandin derivatives can also be reduced to the corresponding hydroxy compounds. May be identical with EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+). PATHWAY PATH: map00590 Prostaglandin and leukotriene metabolism ORTHOLOG KO: K00081 prostaglandin-E2 9-reductase GENES HSA: 873(CBR1) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] PS: PS00062 [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY] PS: PS00063 [LIVM]-[PAIV]-[KR]-[ST]-x(4)-R-x(2)-[GSTAEQK]-[NSL]- x(2)-[LIVMFA] PS: PS00798 G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGC]-[AS]-x(5)-E-x(2)- [LIVM]-G STRUCTURES PDB: 1Q13 1Q5M REFERENCE 1 [PMID:166995] Lee, S.-C. and Levine, L. Purification and regulatory properties of chicken heart prostaglandin E 9-ketoreductase. J. Biol. Chem. 250 (1975) 4549-4555. 2 [PMID:6586494] Schlegel, W., Kruger, S. and Korte, K. Purification of prostaglandin E2 9-oxoreductase from human decidua vera. FEBS Lett. 171 (1984) 141-144. 3 [PMID:7132747] Tai, H.-H. and Yuan, B. Purification and assay of 9-hydroxyprostaglandin dehydrogenase from rat kidney. Methods Enzymol. 86 (1982) 113-117. 4 [PMID:3901124] Watkins, J.D. and Jarabak, J. The effect of NaCl intake on 9-ketoprostaglandin reductase activity in the rabbit kidney. Prostaglandins 30 (1985) 335-349. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.189 ExPASy - ENZYME nomenclature database: 1.1.1.189 ERGO genome analysis and discovery system: 1.1.1.189 BRENDA, the Enzyme Database: 1.1.1.189 CAS: 42613-35-4 /// ENTRY EC 1.1.1.190 NAME indole-3-acetaldehyde reductase (NADH) indoleacetaldehyde reductase indole-3-acetaldehyde reductase (NADH2) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME indole-3-ethanol:NAD+ oxidoreductase REACTION indole-3-ethanol + NAD+ = indole-3-acetaldehyde + NADH + H+ SUBSTRATE indole-3-ethanol NAD+ PRODUCT indole-3-acetaldehyde NADH H+ PATHWAY PATH: map00380 Tryptophan metabolism REFERENCE 1 [PMID:2607] Brown, H.M. and Purves, W.K. Isolation and characterization of indole-3-acetaldehyde reductases from Cucumis sativus. J. Biol. Chem. 251 (1976) 907-913. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.190 ExPASy - ENZYME nomenclature database: 1.1.1.190 ERGO genome analysis and discovery system: 1.1.1.190 BRENDA, the Enzyme Database: 1.1.1.190 CAS: 58875-06-2 /// ENTRY EC 1.1.1.191 NAME indole-3-acetaldehyde reductase (NADPH) indoleacetaldehyde (reduced nicotinamide adenine dinucleotide $phosphate) reductase indole-3-acetaldehyde reductase (NADPH2) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME indole-3-ethanol:NADP+ oxidoreductase REACTION indole-3-ethanol + NADP+ = indole-3-acetaldehyde + NADPH + H+ SUBSTRATE indole-3-ethanol NADP+ PRODUCT indole-3-acetaldehyde NADPH H+ PATHWAY PATH: map00380 Tryptophan metabolism REFERENCE 1 [PMID:2607] Brown, H.M. and Purves, W.K. Isolation and characterization of indole-3-acetaldehyde reductases from Cucumis sativus. J. Biol. Chem. 251 (1976) 907-913. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.191 ExPASy - ENZYME nomenclature database: 1.1.1.191 ERGO genome analysis and discovery system: 1.1.1.191 BRENDA, the Enzyme Database: 1.1.1.191 CAS: 58875-05-1 /// ENTRY EC 1.1.1.192 NAME long-chain-alcohol dehydrogenase long-chain alcohol dehydrogenase fatty alcohol oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME long-chain-alcohol:NAD+ oxidoreductase REACTION a long-chain alcohol + 2 NAD+ + H2O = a long-chain carboxylate + 2 NADH + 2 H+ SUBSTRATE long-chain alcohol NAD+ H2O PRODUCT long-chain carboxylate NADH H+ COMMENT Hexadecanol is a good substrate. PATHWAY PATH: map00071 Fatty acid metabolism REFERENCE 1 [PMID:34610] Lee, T.-C. Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver. J. Biol. Chem. 254 (1979) 2892-2896. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.192 ExPASy - ENZYME nomenclature database: 1.1.1.192 ERGO genome analysis and discovery system: 1.1.1.192 BRENDA, the Enzyme Database: 1.1.1.192 CAS: 76774-36-2 /// ENTRY EC 1.1.1.193 NAME 5-amino-6-(5-phosphoribosylamino)uracil reductase aminodioxyphosphoribosylaminopyrimidine reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 5-amino-6-(5-phosphoribitylamino)uracil:NADP+ 1'-oxidoreductase REACTION 5-amino-6-(5-phosphoribitylamino)uracil + NADP+ = 5-amino-6-(5-phosphoribosylamino)uracil + NADPH + H+ SUBSTRATE 5-amino-6-(5-phosphoribitylamino)uracil NADP+ PRODUCT 5-amino-6-(5-phosphoribosylamino)uracil NADPH H+ PATHWAY PATH: map00740 Riboflavin metabolism ORTHOLOG KO: K00082 5-amino-6-(5-phosphoribosylamino)uracil reductase GENES ATH: At3g47390(T21L8.140) At4g20960(T13K14.120) CME: CMQ053C CMS352C SCE: YBR153W(RIB7) AGO: AER037C(AER037Cp) CAL: orf19.6341(RIB7) SPO: SPBC21C3.10c ECO: b0414(ribD) ECJ: JW0404(ribD) ECE: Z0515(ribD) ECS: ECs0467 ECC: c0524(ribD) STY: STY0455(ribD) STT: t2447(ribD) STM: STM0416(ribD) YPE: YPO3183(ribD) YPK: y1000(ribD) YPM: YP0748(ribD) YPS: YPTB0934(ribD) SFL: SF0351(ribD) SFX: S0359(ribD) ECA: ECA1126(ribD) PLU: plu3899(ribD) BUC: BU462(ribD2) BAS: BUsg446(ribD2) BAB: bbp408(ribD) WBR: Wbr0297(ribD) BFL: Bfl234(ribD) HIN: HI0944(ribD) HDU: HD1161(ribD) PMU: PM0749(ribD) XFA: XF0950 XFT: PD1747(ribD) XCC: XCC0693(ribD) XAC: XAC0746(ribD) VCH: VC2271 VVU: VV10323 VVY: VV0861 VPA: VP0679 PPR: PBPRA0797 PAE: PA4056(ribD) PPU: PP0514(ribD) PST: PSPTO0690(ribD) ACI: ACIAD0247(ribD) SON: SO3469(ribD) CBU: CBU0643(ribD) NME: NMB1817 NMA: NMA0644(ribD) CVI: CV1290(ribD) RSO: RS05138(ribD) BPS: BPSL2624(ribD) BPE: BP2948 BPA: BPP3871 BBR: BB4344 NEU: NE0793(ribD) HPY: HP1505(ribG) HPJ: jhp1398 HHE: HH0838(ribD) WSU: WS2019(ribD) CJE: Cj1622(ribD) GSU: GSU1688(ribD) DVU: DVU1201(ribD) BBA: Bd3542(ribD) DPS: DP2785(ribD) WOL: WD0710(ribD) MLO: mlr8405 SME: SMc01772(ribD) ATU: Atu1167(ribD*) Atu1168(ribD*) ATC: AGR_C_2159 BME: BMEI1189 BMS: BR0767(ribD) BJA: bll5031(ribD) RPA: RPA2726(ribD) BHE: BH07560(ribD) BQU: BQ05410(ribD) CCR: CC0885 BSU: BG10518(ribG) BHA: BH1554(ribG) BAN: BA4331(ribD) BAR: GBAA4331(ribD) BAA: BA_4789 BAT: BAS4018 BCE: BC3387 BC4109 BCA: BCE4179(ribD) BCZ: BTZK3096(ribD) BTZK3865(ribD) BTK: BT9727_3851(ribD) BLI: BL01891(ribD) OIH: OB0423 SAU: SA1589(ribD) SAV: SAV1771(ribD) SAM: MW1711(ribD) SAR: SAR1853(ribD) SAS: SAS1694 SEP: SE1441 LLA: L0163(ribG) SPN: SP0178 SPR: spr0164(ribD) SAG: SAG0746(ribD) SAN: gbs0767 CAC: CAC0590(ribD) CPE: CPE0566(ribB) CTC: CTC00671 MTU: Rv1409(ribG) Rv2671(ribD) MTC: MT1453 MT2745 MBO: Mb1444(ribG) Mb2690(ribD) MLE: ML0555(ribG) ML1340 MPA: MAP1136(ribG) MAP2791(ribD) CGL: NCgl1535(Cgl1597) CEF: CE1716(ribD) CDI: DIP1319(ribD) SCO: SCO2688(SCC61A.09) SCO4106(SCD17.10) SCO6058(SC9B1.05) SMA: SAP1_36 SAV2208 SAV4119(ribG) TWH: TW687(ribG) TWS: TW706(ribD) LXX: Lxx04370(ribD) PAC: PPA1752 FNU: FN1506 RBA: RB6126(ribD) CTR: CT730(ribD) CMU: TC0103 CPN: CPn0871 CPA: CP0998 CPJ: CPj0871(ribD) CPT: CpB0900 CCA: CCA00896(ribD) PCU: pc1042(ribD) LIL: LA1144(ribD1) LA4019(ribD2) LIC: LIC12536(ribD) LIC13208 BTH: BT3728(ribD) PGI: PG0155(ribD) SYN: slr0066(ribD) SYW: SYNW1590(ribD) SYNW2200 SYC: syc0364_c(RibG) syc1308_d(ribD) TEL: tlr2152(ribD) GVI: gll1250(ribD) glr3534 ANA: all0082(ribD) all4103(ribG) PMA: Pro0126(ribD) Pro1339(ribD) PMM: PMM0105(ribG) PMM1265(ribD) PMT: PMT0165(ribG) PMT0375(ribD) CTE: CT0747(ribD) DRA: DR0153 TTH: TTC0699(ribD) AAE: aq_138(ribD1) aq_436(ribD2) TMA: TM1828 MJA: MJ0671 MAC: MA4092(ribD) MA4367(ribD) MMA: MM0826 MM1058 MTH: MTH235 MKA: MK0098(ribD) AFU: AF2007(ribG) HAL: VNG1256G(ribG) PFU: PF0062 APE: APE1279 SSO: SSO2097(ribD) STO: ST0285 PAI: PAE2985 MOTIF PS: PS00903 [CH]-[AGV]-E-x(2)-[LIVMFGAT]-[LIVM]-x(17,33)-P-C- x(2,8)-C-x(3)-[LIVM] REFERENCE 1 [PMID:30756] Burrows, R.B. and Brown, G.M. Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin. J. Bacteriol. 136 (1978) 657-667. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.193 ExPASy - ENZYME nomenclature database: 1.1.1.193 ERGO genome analysis and discovery system: 1.1.1.193 BRENDA, the Enzyme Database: 1.1.1.193 CAS: 69020-28-6 /// ENTRY EC 1.1.1.194 NAME coniferyl-alcohol dehydrogenase CAD CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME coniferyl-alcohol:NADP+ oxidoreductase REACTION coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+ SUBSTRATE coniferyl alcohol NADP+ PRODUCT coniferyl aldehyde NADPH H+ COMMENT Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol. PATHWAY PATH: map00940 Stilbene, coumarine and lignin biosynthesis REFERENCE 1 Mansell, R.L., Babbel, G.R. and Zenk, M.H. Multiple forms and specificity of coniferyl alcohol dehydrogenase from cambial regions of higher plants. Phytochemistry 15 (1976) 1849-1853. 2 [PMID:1250] Wyrambik, D. and Grisebach, H. Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 59 (1975) 9-15. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.194 ExPASy - ENZYME nomenclature database: 1.1.1.194 ERGO genome analysis and discovery system: 1.1.1.194 BRENDA, the Enzyme Database: 1.1.1.194 CAS: 37250-27-4 /// ENTRY EC 1.1.1.195 NAME cinnamyl-alcohol dehydrogenase cinnamyl alcohol dehydrogenase CAD CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME cinnamyl-alcohol:NADP+ oxidoreductase REACTION cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+ SUBSTRATE cinnamyl alcohol NADP+ PRODUCT cinnamaldehyde NADPH H+ COMMENT Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194 coniferyl-alcohol dehydrogenase). PATHWAY PATH: map00940 Stilbene, coumarine and lignin biosynthesis ORTHOLOG KO: K00083 cinnamyl-alcohol dehydrogenase GENES ATH: At3g19450(MLD14.30) At4g34230(F28A23.10) CAL: orf19.2581 orf19.3150(GRP4) orf19.3151(GRP6) orf19.4309(GRP3) orf19.4781(GRP1) orf19.5611(GRE2) orf19.6868(GRP5) orf19.7009(GRP8) CHO: Chro.50271 MOTIF PS: PS00059 G-H-E-x(2)-G-x(5)-[GA]-x(2)-[IVSAC] REFERENCE 1 [PMID:6365550] Sarni, F., Grand, C. and Baudet, A.M. Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase from poplar stems (Populus X euramericana). Eur. J. Biochem. 139 (1984) 259-265. 2 [PMID:1250] Wyrambik, D. and Grisebach, H. Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 59 (1975) 9-15. 3 [PMID:572771] Wyrambik, D. and Grisebach, H. Enzymic synthesis of lignin precursors. Further studies on cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 97 (1979) 503-509. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.195 ExPASy - ENZYME nomenclature database: 1.1.1.195 ERGO genome analysis and discovery system: 1.1.1.195 BRENDA, the Enzyme Database: 1.1.1.195 CAS: 55467-36-2 /// ENTRY EC 1.1.1.196 NAME 15-hydroxyprostaglandin-D dehydrogenase (NADP+) prostaglandin-D 15-dehydrogenase (NADP) dehydrogenase, prostaglandin D2 NADP-PGD2 dehydrogenase dehydrogenase, 15-hydroxyprostaglandin (nicotinamide adenine $dinucleotide phosphate) 15-hydroxy PGD2 dehydrogenase 15-hydroxyprostaglandin dehydrogenase (NADP) NADP-dependent 15-hydroxyprostaglandin dehydrogenase prostaglandin D2 dehydrogenase NADP-linked 15-hydroxyprostaglandin dehydrogenase NADP-specific 15-hydroxyprostaglandin dehydrogenase NADP-linked prostaglandin D2 dehydrogenase 15-hydroxyprostaglandin-D dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate:NADP+ $15-oxidoreductase REACTION (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADP+ = (5Z,13E)-9alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate + NADPH + H+ SUBSTRATE (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate NADP+ PRODUCT (5Z,13E)-9alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate NADPH H+ COMMENT Specific for prostaglandins D [cf. EC 1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+)]. PATHWAY PATH: map00590 Prostaglandin and leukotriene metabolism REFERENCE 1 [PMID:7354056] Watanabe, K., Shimizu, T., Iguchi, S., Wakatsuka, H., Hayashi, M. and Hayaishi, O. An NADP-linked prostaglandin D dehydrogenase in swine brain. J. Biol. Chem. 255 (1980) 1779-1882. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.196 ExPASy - ENZYME nomenclature database: 1.1.1.196 ERGO genome analysis and discovery system: 1.1.1.196 BRENDA, the Enzyme Database: 1.1.1.196 CAS: 84399-95-1 /// ENTRY EC 1.1.1.197 NAME 15-hydroxyprostaglandin dehydrogenase (NADP+) NADP-dependent 15-hydroxyprostaglandin dehydrogenase NADP-linked 15-hydroxyprostaglandin dehydrogenase NADP-specific 15-hydroxyprostaglandin dehydrogenase type II 15-hydroxyprostaglandin dehydrogenase 15-hydroxyprostaglandin dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate:NADP+ $15-oxidoreductase REACTION (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ = (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH + H+ SUBSTRATE (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate NADP+ PRODUCT (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate NADPH H+ COMMENT Acts on prostaglandins E2, F2alpha and B1, but not on prostaglandin D2 [cf. EC 1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+) and EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+)]. May be identical with EC 1.1.1.189 prostaglandin-E2 9-reductase. GENES HSA: 873(CBR1) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] REFERENCE 1 [PMID:234431] Lee, S.-C. and Levine, L. Prostaglandin metabolism. II. Identification of two 15-hydroxyprostaglandin dehydrogenase types. J. Biol. Chem. 250 (1975) 548-552. 2 [PMID:803247] Lee, S.-C., Pong, S.-S., Katzen, D., Wu, K.-Y. and Levine, L. Distribution of prostaglandin E 9-ketoreductase and types I and II 15-hydroxyprostaglandin dehydrogenase in swine kidney medulla and cortex. Biochemistry 14 (1975) 142-145. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.197 ExPASy - ENZYME nomenclature database: 1.1.1.197 ERGO genome analysis and discovery system: 1.1.1.197 BRENDA, the Enzyme Database: 1.1.1.197 CAS: 54989-39-8 /// ENTRY EC 1.1.1.198 NAME (+)-borneol dehydrogenase bicyclic monoterpenol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (+)-borneol:NAD+ oxidoreductase REACTION (+)-borneol + NAD+ = (+)-camphor + NADH + H+ SUBSTRATE (+)-borneol NAD+ PRODUCT (+)-camphor NADH H+ COMMENT NADP+ can also act, but more slowly. REFERENCE 1 [PMID:677891] Croteau, R., Hooper, C.L. and Felton, M. Biosynthesis of monoterpenes. Partial purification and characterization of a bicyclic monoterpenol dehydrogenase from sage (Salvia officinalis). Arch. Biochem. Biophys. 188 (1978) 182-193. 2 [PMID:3310901] Dehal, S.S. and Croteau, R. Metabolism of monoterpenes: specificity of the dehydrogenases responsible for the biosynthesis of camphor, 3-thujone, and 3-isothujone. Arch. Biochem. Biophys. 258 (1987) 287-291. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.198 ExPASy - ENZYME nomenclature database: 1.1.1.198 ERGO genome analysis and discovery system: 1.1.1.198 BRENDA, the Enzyme Database: 1.1.1.198 CAS: 67185-75-5 /// ENTRY EC 1.1.1.199 NAME (S)-usnate reductase L-usnic acid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME reduced-(S)-usnate:NAD+ oxidoreductase (ether-bond-forming) REACTION in the reverse direction, (S)-usnate is reduced by NADH with cleavage of the ether bond to form a 7-hydroxy group REFERENCE 1 Estevez, M.P., Legaz, E., Olmeda, L., Perez, F.J. and Vincente, C. Purification and properties of a new enzyme from Evernia prunastri, which reduces L-usnic acid. Z. Naturforsch. C: Biosci. 36 (1981) 35-39. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.199 ExPASy - ENZYME nomenclature database: 1.1.1.199 ERGO genome analysis and discovery system: 1.1.1.199 BRENDA, the Enzyme Database: 1.1.1.199 CAS: 77237-99-1 /// ENTRY EC 1.1.1.200 NAME aldose-6-phosphate reductase (NADPH) aldose 6-phosphate reductase NADP-dependent aldose 6-phosphate reductase A6PR aldose-6-P reductase aldose-6-phosphate reductase alditol 6-phosphate:NADP 1-oxidoreductase aldose-6-phosphate reductase (NADPH2) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-aldose-6-phosphate:NADP+ 1-oxidoreductase REACTION D-sorbitol 6-phosphate + NADP+ = D-glucose 6-phosphate + NADPH + H+ SUBSTRATE D-sorbitol 6-phosphate NADP+ PRODUCT D-glucose 6-phosphate NADPH H+ COMMENT In the reverse reaction, acts also on D-galactose 6-phosphate and, more slowly, on D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate. GENES ATH: At2g21260(F3K23.2) MOTIF PS: PS00062 [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY] PS: PS00063 [LIVM]-[PAIV]-[KR]-[ST]-x(4)-R-x(2)-[GSTAEQK]-[NSL]- x(2)-[LIVMFA] PS: PS00798 G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGC]-[AS]-x(5)-E-x(2)- [LIVM]-G REFERENCE 1 Negm, F.B. and Loescher, W.H. Characterization and partial-purification of aldose-6-phosphate reductase (alditol-6-phosphate-NADP 1-oxidoreductase) from apple leaves. Plant Physiol. 67 (1981) 139-142. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.200 ExPASy - ENZYME nomenclature database: 1.1.1.200 ERGO genome analysis and discovery system: 1.1.1.200 BRENDA, the Enzyme Database: 1.1.1.200 CAS: 76901-04-7 /// ENTRY EC 1.1.1.201 NAME 7beta-hydroxysteroid dehydrogenase (NADP+) NADP-dependent 7beta-hydroxysteroid dehydrogenase 7beta-hydroxysteroid dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 7beta-hydroxysteroid:NADP+ 7-oxidoreductase REACTION A 7beta-hydroxysteroid + NADP+ = a 7-oxosteroid + NADPH + H+ SUBSTRATE 7beta-hydroxysteroid NADP+ PRODUCT 7-oxosteroid NADPH H+ COMMENT Catalyses the oxidation of the 7beta-hydroxy group of bile acids such as ursodeoxycholate. REFERENCE 1 [PMID:6954878] Hirano, S. and Masuda, N. Characterization of NADP-dependent 7beta-hydroxysteroid dehydrogenases from Peptostreptococcus productus and Eubacterium aerofaciens. Appl. Environ. Microbiol. 43 (1982) 1057-1063. 2 [PMID:6945134] Macdonald, I.A. and Roach, P.D. Bile induction of 7alpha- and 7beta-hydroxysteroid dehydrogenases in Clostridium absonum. Biochim. Biophys. Acta 665 (1981) 262-269. 3 [PMID:6758698] Macdonald, I.A., Rochon, Y.P., Hutchison, D.M. and Holdeman, L.V. Formation of ursodeoxycholic acid from chenodeoxycholic acid by a 7beta-hydroxysteroid dehydrogenase-elaborating Eubacterium aerofaciens strain cocultured with 7alpha-hydroxysteroid dehydrogenase-elaborating organisms. Appl. Environ. Microbiol. 44 (1982) 1187-1195. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.201 ExPASy - ENZYME nomenclature database: 1.1.1.201 ERGO genome analysis and discovery system: 1.1.1.201 BRENDA, the Enzyme Database: 1.1.1.201 CAS: 79393-83-2 /// ENTRY EC 1.1.1.202 NAME 1,3-propanediol dehydrogenase 3-hydroxypropionaldehyde reductase 1,3-PD:NAD+ oxidoreductase 1,3-propanediol:NAD+ oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME propane-1,3-diol:NAD+ 1-oxidoreductase REACTION propane-1,3-diol + NAD+ = 3-hydroxypropanal + NADH + H+ SUBSTRATE propane-1,3-diol NAD+ PRODUCT 3-hydroxypropanal NADH H+ PATHWAY PATH: map00561 Glycerolipid metabolism ORTHOLOG KO: K00086 1,3-propanediol dehydrogenase GENES BCE: BC2176 LPL: lp_3051(dhaT) CTC: CTC00506 LIL: LA2996(dhaT) LIC: LIC11070 AAE: aq_1145(dhaT) MOTIF PS: PS00060 [GSW]-x-[LIVTSACD]-[GH]-x(2)-[GSAE]-[GSHYQ]-x-[LIVTP]- [GAST]-[GAS]-x(3)-[LIVMT]-x-[HNS]-[GA]-x-[GTAC] PS: PS00913 [STALIV]-[LIVF]-x-[DE]-x(6,7)-P-x(4)-[ALIV]-x-[GST]- x(2)-D-[TAIVM]-[LIVMF]-x(4)-E REFERENCE 1 Abeles, R.H., Brownstein, A.M. and Randles, C.H. alpha-Hydroxypropionaldehyde, an intermediate in the formation of 1,3-propanediol by Aerobacter melanogaster. Biochim. Biophys. Acta 41 (1960) 530. 2 [PMID:7035429] Forage, R.G. and Foster, M.A. Glycerol fermentation in Klebsiella pneumoniae: functions of the coenzyme B12-dependent glycerol and diol dehydratases. J. Bacteriol. 149 (1982) 413-419. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.202 ExPASy - ENZYME nomenclature database: 1.1.1.202 ERGO genome analysis and discovery system: 1.1.1.202 BRENDA, the Enzyme Database: 1.1.1.202 CAS: 81611-70-3 /// ENTRY EC 1.1.1.203 NAME uronate dehydrogenase uronate: NAD-oxidoreductase uronic acid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME uronate:NAD+ 1-oxidoreductase REACTION D-galacturonate + NAD+ + H2O = D-galactarate + NADH + H+ SUBSTRATE D-galacturonate NAD+ H2O PRODUCT D-galactarate NADH H+ COMMENT Also acts on D-glucuronate. Formerly EC 1.2.1.35. REFERENCE 1 Kilgore, W.W. and Starr, M.P. Uronate oxidation by phytopathogenic pseudomonads. Nature (Lond.) 183 (1959) 1412-1413. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.203 ExPASy - ENZYME nomenclature database: 1.1.1.203 ERGO genome analysis and discovery system: 1.1.1.203 BRENDA, the Enzyme Database: 1.1.1.203 CAS: 37250-98-9 /// ENTRY EC 1.1.1.204 Obsolete NAME Transferred to 1.17.1.4 CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Transferred entry: now EC 1.17.1.4, xanthine dehydrogenase. The enzyme was incorrectly classified as acting on a CH-OH group (EC 1.1.1.204 created 1972 as EC 1.2.1.37, transferred 1984 to EC 1.1.1.204, modified 1989, deleted 2004) PATHWAY PATH: map00230 Purine metabolism MOTIF PS: PS00197 C-{C}-{C}-[GA]-{C}-C-[GAST]-{CPDEKRHFYW}-C PS: PS00559 [GA]-x(3)-[KRNQHT]-x(11,14)-[LIVMFYWS]-x(8)-[LIVMF]-x- C-x(2)-[DEN]-R-x(2)-[DE] STRUCTURES PDB: 1FO4 1JRO 1JRP 1N5X 1V97 DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.204 ExPASy - ENZYME nomenclature database: 1.1.1.204 ERGO genome analysis and discovery system: 1.1.1.204 BRENDA, the Enzyme Database: 1.1.1.204 /// ENTRY EC 1.1.1.205 NAME IMP dehydrogenase inosine-5'-phosphate dehydrogenase inosinic acid dehydrogenase inosinate dehydrogenase inosine 5'-monophosphate dehydrogenase inosine monophosphate dehydrogenase IMP oxidoreductase inosine monophosphate oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME IMP:NAD+ oxidoreductase REACTION inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+ SUBSTRATE inosine 5'-phosphate NAD+ H2O PRODUCT xanthosine 5'-phosphate NADH H+ COMMENT The enzyme acts on the hydroxy group of the hydrated derivative of the substrate. Formerly EC 1.2.1.14. PATHWAY PATH: map00230 Purine metabolism ORTHOLOG KO: K00088 IMP dehydrogenase GENES HSA: 3614(IMPDH1) 3615(IMPDH2) MMU: 23917(Impdh1) 23918(Impdh2) RNO: 301005(Impdh2) DME: CG1799-PA(CG1799) CG1799-PB(CG1799) CEL: T22D1.3 ATH: At1g16350(F3O9.15) At1g79470(T8K14.11) CME: CML243C SCE: YAR073W(IMD1) YHR216W(IMD2) YLR432W(IMD3) YML056C AGO: AER117W(AER117Wp) CAL: orf19.18(IMD3) SPO: SPBC2F12.14c PFA: PFI1020c ECO: b2508(guaB) ECJ: JW2492(guaB) ECE: Z3772(guaB) ECS: ECs3370 ECC: c3027(guaB) STY: STY2752(guaB) STT: t0346(guaB) STM: STM2511(guaB) YPE: YPO2871(guaB) YPK: y1362(guaB) YPM: YP2737(guaB) YPS: YPTB2833(guaB) SFL: SF2554(guaB) SFX: S2726(guaB) ECA: ECA3209(guaB) PLU: plu2713(guaB) WBR: Wbr0144(guaB) BFL: Bfl528(guaB) HIN: HI0221(guaB) HDU: HD1503(guaB) PMU: PM0295(guaB) XFA: XF2430 XFT: PD1448(guaB) XCC: XCC2184(guaB) XAC: XAC2288(guaB) VCH: VC0767 VVU: VV10419 VVY: VV0775 VPA: VP0616 PPR: PBPRA0780 PAE: PA3770(guaB) PPU: PP1031(guaB) PST: PSPTO1449(guaB) ACI: ACIAD3503(guaB) SON: SO3293(guaB) CBU: CBU1342(guaB) LPN: lpg1723(guaB) lpg2843 MCA: MCA0291(guaB) NME: NMB1201 NMA: NMA1372(guaB) CVI: CV1303(guaB) RSO: RS05263(guaB) BMA: BMA1524(guaB) BPS: BPSL2129(guaB) BPE: BP2625(guaB) BPA: BPP1258(guaB) BBR: BB2326(guaB) NEU: NE0095(guaB) NE0524 HPY: HP0829(guaB) HPJ: jhp0768 HHE: HH0702(guaB) WSU: WS1895(guaB) CJE: Cj1058c(guaB) GSU: GSU2195(guaB) DVU: DVU1044(guaB) BBA: Bd0921 Bd1779(guaB) Bd2081(guaB) DPS: DP0902 WOL: WD0089(guaB) MLO: mlr8350 SME: SMc00815(guaB) ATU: Atu0624(guaB) ATC: AGR_C_1108(guaB) BME: BMEII0896 BMS: BRA0352(guaB) BJA: blr3972(guaB) RPA: RPA2200(guaB) BHE: BH01800(guaB) BQU: BQ01690(guaB) CCR: CC1617 BSU: BG10073(guaB) BG11600(yhcV) BHA: BH0020(guaB) BAN: BA0008(guaB) BAR: GBAA0008(guaB) BAA: BA_0603 BAT: BAS0011 BCE: BC0013 BCA: BCE0009(guaB) BCZ: BTZK0009(guaB) BTK: BT9727_0009(guaB) BLI: BL02350(guaB) OIH: OB0010 SAU: SA0375(guaB) SAV: SAV0390(guaB) SAM: MW0366(guaB) SAR: SAR0408(guaB) SAS: SAS0366 SEP: SE2348 LMO: lmo0132 lmo2758(guaB) LMF: LMOf2365_0150 LMOf2365_2746(guaB) LIN: lin0179 lin2901(guaB) LLA: L21264(guaB) SPY: SPy2206(guaB) SPM: spyM18_2244(impd) SPG: SpyM3_1857(guaB) SPS: SPs1853 SPA: M6_Spy1875 SPN: SP2228 SPR: spr2033(imdH) SAG: SAG2159(guaB) SAN: gbs2118 SMU: SMU.2157(guaB) LPL: lp_3194(guaB) LJO: LJ0043 EFA: EF3293(guaB) CAC: CAC2701(guaB) CPE: CPE2276 CTC: CTC02410 TTE: TTE0582(guaB) MPE: MYPE3150(guaB) MFL: Mfl343 MTU: Rv1843c(guaB1) Rv3410c(guaB3) Rv3411c(guaB2) MTC: MT1891 MT3518 MT3519 MBO: Mb1874c(guaB1) Mb3444c(guaB3) Mb3445c(guaB2) MLE: ML0387(guaB2) ML0388(guaB3) ML2066(guaB1) MPA: MAP1556c(guaB1) MAP4278(guaB2) MAP4279(guaB3) CGL: NCgl0578(Cgl0603) NCgl0579(Cgl0604) NCgl2586(Cgl2679) CEF: CE0608(guaB) CE0609 CE2530 CDI: DIP0580(guaB) DIP0581 SCO: SCO1461(SCL6.18c) SCO4770(SCD63.02) SCO4771(SCD63.03) SMA: SAV5000(guaB1) SAV5001(guaB2) SAV6884(guaB3) TWH: TW075(guaB1) TW076(guaB2) TWS: TW085(guaB1) TW086(guaB2) LXX: Lxx19150(guaB) Lxx19840(guaB) Lxx19860(guaB) PAC: PPA0708 PPA1767 PPA1768 BLO: BL1500 BL1722(guaB) STH: STH2916 FNU: FN1231 RBA: RB11822(guaB) CMU: TC0443 CPN: CPn0172 CPJ: CPj0172(guaB) CPT: CpB0174 CCA: CCA00574 BBU: BBB17(guaB) TDE: TDE2665(guaB) LIL: LA1986 LIC: LIC11919(guaB) BTH: BT3845 PGI: PG0523(guaB) SYN: slr1722(guaB) SYW: SYNW0725(guaB) SYC: syc2263_d(guaB) TEL: tll2190 GVI: glr1603 ANA: alr0051 PMA: Pro1138(guaB) PMM: PMM1062(guaB) PMT: PMT1126(guaB) CTE: CT1293(guaB) DRA: DR1878 TTH: TTC0064 AAE: aq_2023(guaB) TMA: TM1347 MJA: MJ0188 MJ1616(guaB) MMP: MMP0133(guaB) MMP0287 MTH: MTH1282 MTH142 MKA: MK1600(guaB) AFU: AF0847(guaB-1) AF1259 AF2118(guaB-2) HAL: VNG0651G(imd1) VNG1001G(guaB) HMA: pNG7153(guaB1) rrnAC0267(imd1) rrnAC0748(guaB3) rrnAC1274(guaB2) rrnAC2139(imd3) rrnAC2699 rrnB0175(imd2) TAC: Ta0219 TVO: TVG1445839 PTO: PTO0470 PTO0540 PTO0859 PHO: PH0307 PAB: PAB1250 PFU: PF0285 APE: APE1507 DISEASE MIM: 146690 Inosine-5'-monophosphate dehydrogenase, type I MIM: 146691 Inosine-5'-monophosphate dehydrogenase, type II MOTIF PS: PS00487 [LIVM]-[RK]-[LIVM]-G-[LIVM]-G-x-G-S-[LIVM]-C-x-T STRUCTURES PDB: 1AK5 1B3O 1EEP 1JCN 1JR1 1LRT 1ME7 1ME8 1ME9 1MEH 1MEI 1MEW 1NF7 1NFB 1PVN 1ZFJ REFERENCE 1 Magasanik, B., Moyed, H.S. and Gehring, L.B. Enzymes essential for the biosynthesis of nucleic acid guanine; inosine 5'-phosphate dehydrogenase of Aerobacter aerogenes. J. Biol. Chem. 226 (1957) 339-350. 2 Turner, J.F. and King, J.E. Inosine 5-phosphate dehydrogenase of pea seeds. Biochem. J. 79 (1961) 147. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.205 ExPASy - ENZYME nomenclature database: 1.1.1.205 ERGO genome analysis and discovery system: 1.1.1.205 BRENDA, the Enzyme Database: 1.1.1.205 CAS: 9028-93-7 /// ENTRY EC 1.1.1.206 NAME tropine dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME tropine:NADP+ 3alpha-oxidoreductase REACTION tropine + NADP+ = tropinone + NADPH + H+ SUBSTRATE tropine NADP+ PRODUCT tropinone NADPH H+ COMMENT Also oxidizes other tropan-3alpha-ols, but not the corresponding beta-derivatives. PATHWAY PATH: map00960 Alkaloid biosynthesis II MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] REFERENCE 1 Koelen, K.J. and Gross, G.G. Partial purification and properties of tropine dehydrogenase from root cultures of Datura stramonium. Planta Med. 44 (1982) 227-230. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.206 ExPASy - ENZYME nomenclature database: 1.1.1.206 ERGO genome analysis and discovery system: 1.1.1.206 BRENDA, the Enzyme Database: 1.1.1.206 CAS: 118390-87-7 /// ENTRY EC 1.1.1.207 NAME (-)-menthol dehydrogenase monoterpenoid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (-)-menthol:NADP+ oxidoreductase REACTION (-)-menthol + NADP+ = (-)-menthone + NADPH + H+ SUBSTRATE (-)-menthol NADP+ PRODUCT (-)-menthone NADPH H+ COMMENT Not identical with EC 1.1.1.208 (+)-neomenthol dehydrogenase. Acts also on a number of other cyclohexanols and cyclohexenols. PATHWAY PATH: map00902 Monoterpenoid biosynthesis REFERENCE 1 Kjonaas, R., Martinkus-Taylor, C. and Croteau, R. Metabolism of monoterpenes: conversion of l-menthone to l-menthol and d-neomenthol by stereospecific dehydrogenases from peppermint (Mentha piperita) leaves. Plant Physiol. 69 (1982) 1013-1017. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.207 ExPASy - ENZYME nomenclature database: 1.1.1.207 ERGO genome analysis and discovery system: 1.1.1.207 BRENDA, the Enzyme Database: 1.1.1.207 CAS: 81811-46-3 /// ENTRY EC 1.1.1.208 NAME (+)-neomenthol dehydrogenase monoterpenoid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (+)-neomenthol:NADP+ oxidoreductase REACTION (+)-neomenthol + NADP+ = (-)-menthone + NADPH + H+ SUBSTRATE (+)-neomenthol NADP+ PRODUCT (-)-menthone NADPH H+ COMMENT Not identical with EC 1.1.1.207 (-)-menthol dehydrogenase. Acts also on a number of other cyclohexanols and cyclohexenols. PATHWAY PATH: map00902 Monoterpenoid biosynthesis REFERENCE 1 Kjonaas, R., Martinkus-Taylor, C. and Croteau, R. Metabolism of monoterpenes: conversion of l-menthone to l-menthol and d-neomenthol by stereospecific dehydrogenases from peppermint (Mentha piperita) leaves. Plant Physiol. 69 (1982) 1013-1017. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.208 ExPASy - ENZYME nomenclature database: 1.1.1.208 ERGO genome analysis and discovery system: 1.1.1.208 BRENDA, the Enzyme Database: 1.1.1.208 CAS: 81811-47-4 /// ENTRY EC 1.1.1.209 NAME 3(or 17)alpha-hydroxysteroid dehydrogenase 3(17)alpha-hydroxysteroid dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3(or 17)alpha-hydroxysteroid:NAD(P)+ oxidoreductase REACTION androsterone + NAD(P)+ = 5alpha-androstane-3,17-dione + NAD(P)H + H+ SUBSTRATE androsterone NAD+ NADP+ PRODUCT 5alpha-androstane-3,17-dione NADH NADPH H+ COMMENT Acts on the 3alpha-hydroxy group of androgens of the 5alpha-androstane series; and also, more slowly, on the 17alpha-hydroxy group of both androgenic and estrogenic substrates (cf. EC 1.1.1.51 3(or 17)beta-hydroxysteroid dehydrogenase). REFERENCE 1 [PMID:6955302] Lau, P.C.K., Layne, D.S. and Williamson, D.G. A 3(17)alpha-hydroxysteroid dehydrogenase of female rabbit kidney cytosol. Purification and characterization of multiple forms of the enzyme. J. Biol. Chem. 257 (1982) 9444-9449. 2 [PMID:6955303] Lau, P.C.K., Layne, D.S. and Williamson, D.G. Comparison of the multiple forms of the soluble 3(17)alpha-hydroxysteroid dehydrogenases of female rabbit kidney and liver. J. Biol. Chem. 257 (1982) 9450-9456. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.209 ExPASy - ENZYME nomenclature database: 1.1.1.209 ERGO genome analysis and discovery system: 1.1.1.209 BRENDA, the Enzyme Database: 1.1.1.209 CAS: 83294-77-3 /// ENTRY EC 1.1.1.210 NAME 3beta(or 20alpha)-hydroxysteroid dehydrogenase progesterone reductase dehydrogenase, 3beta,20alpha-hydroxy steroid 3beta,20alpha-hydroxysteroid oxidoreductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3beta(or 20alpha)-hydroxysteroid:NADP+ oxidoreductase REACTION 5alpha-androstan-3beta,17beta-diol + NADP+ = 17beta-hydroxy-5alpha-androstan-3-one + NADPH + H+ SUBSTRATE 5alpha-androstan-3beta,17beta-diol NADP+ PRODUCT 17beta-hydroxy-5alpha-androstan-3-one NADPH H+ COMMENT Also acts on 20alpha-hydroxysteroids. GENES BTK: BT9727_3001 REFERENCE 1 [PMID:6958329] Sharaf, M.A. and Sweet, F. Dual activity at an enzyme active site: 3beta,20alpha-hydroxysteroid oxidoreductase from fetal blood. Biochemistry 21 (1982) 4615-4620. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.210 ExPASy - ENZYME nomenclature database: 1.1.1.210 ERGO genome analysis and discovery system: 1.1.1.210 BRENDA, the Enzyme Database: 1.1.1.210 CAS: 82869-26-9 /// ENTRY EC 1.1.1.211 NAME long-chain-3-hydroxyacyl-CoA dehydrogenase beta-hydroxyacyl-CoA dehydrogenase long-chain 3-hydroxyacyl coenzyme A dehydrogenase 3-hydroxyacyl-CoA dehydrogenase LCHAD CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME long-chain-(S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase REACTION (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+ SUBSTRATE (S)-3-hydroxyacyl-CoA NAD+ PRODUCT 3-oxoacyl-CoA NADH H+ COMMENT Acts most rapidly on derivatives with chain-length 8 or 10 (cf. EC 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase). PATHWAY PATH: map00062 Fatty acid biosynthesis (path 2) PATH: map00071 Fatty acid metabolism REFERENCE 1 [PMID:7150615] El-Fakhri, M. and Middleton, B. The existence of an inner-membrane-bound, long acyl-chain-specific 3-hydroxyacyl-CoA dehydrogenase in mammalian mitochondria. Biochim. Biophys. Acta 713 (1982) 270-279. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.211 ExPASy - ENZYME nomenclature database: 1.1.1.211 ERGO genome analysis and discovery system: 1.1.1.211 BRENDA, the Enzyme Database: 1.1.1.211 CAS: 84177-52-6 /// ENTRY EC 1.1.1.212 NAME 3-oxoacyl-[acyl-carrier-protein] reductase (NADH) 3-oxoacyl-[acyl carrier protein] (reduced nicotinamide adenine $dinucleotide) reductase 3-oxoacyl-[acyl-carrier-protein] reductase (NADH2) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NAD+ oxidoreductase REACTION (3R)-3-hydroxyacyl-[acyl-carrier protein] + NAD+ = 3-oxoacyl-[acyl-carrier protein] + NADH + H+ SUBSTRATE (3R)-3-hydroxyacyl-[acyl-carrier protein] NAD+ PRODUCT 3-oxoacyl-[acyl-carrier protein] NADH H+ COMMENT Forms part of the fatty acid synthase system in plants. Can be separated from EC 1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase. REFERENCE 1 [PMID:7075600] Caughey, I. and Kekwick, R.G.O. The characteristics of some components of the fatty acid synthetase system in the plastids from the mesocarp of avocado (Persea americana) fruit. Eur. J. Biochem. 123 (1982) 553-561. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.212 ExPASy - ENZYME nomenclature database: 1.1.1.212 ERGO genome analysis and discovery system: 1.1.1.212 BRENDA, the Enzyme Database: 1.1.1.212 CAS: 82047-86-7 /// ENTRY EC 1.1.1.213 NAME 3alpha-hydroxysteroid dehydrogenase (A-specific) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3alpha-hydroxysteroid:NAD(P)+ oxidoreductase (A-specific) REACTION androsterone + NAD(P)+ = 5alpha-androstane-3,17-dione + NAD(P)H + H+ SUBSTRATE androsterone NAD+ NADP+ PRODUCT 5alpha-androstane-3,17-dione NADH NADPH H+ COMMENT Also acts on other 3alpha-hydroxysteroids. A-specific with respect to NAD+ or NADP+ (cf. EC 1.1.1.50). GENES HSA: 1109(AKR1C4) 1645(AKR1C1) 1646(AKR1C2) 8644(AKR1C3) STRUCTURES PDB: 1J96 1LWI 1S1P 1S1R 1S2A 1S2C REFERENCE 1 [PMID:4392180] Bjorkhem, I. and Danielsson, H. Stereochemistry of hydrogen transfer from pyridine nucleotides catalyzed by delta4-3-oxosteroid 5-beta-reductase and 3-alpha-hydroxysteroid dehydrogenase from rat liver. Eur. J. Biochem. 12 (1970) 80-84. 2 Tomkins, G.M. A mammalian 3alpha-hydroxysteroid dehydrogenase. J. Biol. Chem. 218 (1956) 437-447. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.213 ExPASy - ENZYME nomenclature database: 1.1.1.213 ERGO genome analysis and discovery system: 1.1.1.213 BRENDA, the Enzyme Database: 1.1.1.213 /// ENTRY EC 1.1.1.214 NAME 2-dehydropantolactone reductase (B-specific) 2-oxopantoyl lactone reductase 2-ketopantoyl lactone reductase ketopantoyl lactone reductase 2-dehydropantoyl-lactone reductase (B-specific) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-pantolactone:NADP+ oxidoreductase (B-specific) REACTION (R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+ SUBSTRATE (R)-pantolactone NADP+ PRODUCT 2-dehydropantolactone NADPH H+ COMMENT The Escherichia coli enzyme differs from that from yeast [EC 1.1.1.168 2-dehydropantolactone reductase (A-specific)], which is specific for the A-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase. REFERENCE 1 [PMID:234966] Wilken, D.R., King, H.L., Jr. and Dyar, R.E. Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate. J. Biol. Chem. 250 (1975) 2311-2314. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.214 ExPASy - ENZYME nomenclature database: 1.1.1.214 ERGO genome analysis and discovery system: 1.1.1.214 BRENDA, the Enzyme Database: 1.1.1.214 CAS: 37211-75-9 /// ENTRY EC 1.1.1.215 NAME gluconate 2-dehydrogenase 2-keto-D-gluconate reductase 2-ketogluconate reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-gluconate:NADP+ oxidoreductase REACTION D-gluconate + NADP+ = 2-dehydro-D-gluconate + NADPH + H+ SUBSTRATE D-gluconate NADP+ PRODUCT 2-dehydro-D-gluconate NADPH H+ COMMENT Also acts on L-idonate, D-galactonate and D-xylonate. GENES CAL: orf19.1796 orf19.2176 orf19.2989 orf19.3584 ECO: b3553(tkrA) ECJ: JW3522(yiaE) ECE: Z4978(yiaE) ECS: ECs4438 ECC: c4372(yiaE) STY: STY4156(yiaE) STT: t3873(yiaE) STM: STM3646(yiaE) YPE: YPO4078 YPK: y4096 YPM: YP3988(ldhA3) YPS: YPTB3910 SFL: SF3587(yiaE) SFX: S4182(yiaE) ECA: ECA0078(tkrA) XCC: XCC2550 XAC: XAC2724 PAE: PA2263 PPU: PP3376(kguD) ACI: ACIAD1327(tkrA) RSO: RS05388 BPS: BPSL1577(tkrA) BME: BMEI1952 BMEII0313 BJA: blr7063 BSU: BG12409(yvcT) BAN: BA5135 BAR: GBAA5135 BAA: BA_0009 BAT: BAS4773 BCE: BC4903 BCA: BCE5042 BCZ: BTZK4635 BTK: BT9727_4613 BLI: BL03603(yvcT) OIH: OB2848 ANA: all8087 PTO: PTO1438 MOTIF PS: PS00065 [LIVMA]-[AG]-[IVT]-[LIVMFY]-[AG]-x-G-[NHKRQGSAC]-[LIV]- G-x(13,14)-[LIVMFT]-x(2)-[FYWCTH]-[DNSTK] PS: PS00670 [LIVMFYWA]-[LIVFYWC]-x(2)-[SAC]-[DNQHR]-[IVFA]-[LIVF]- x-[LIVF]-[HNI]-x-P-x(4)-[STN]-x(2)-[LIVMF]-x-[GSDN] PS: PS00671 [LMFATC]-[KPQ]-x-[GSTDN]-x-[LIVMFYWR]-[LIVMFYW](2)-N-x- [STAGC]-R-[GP]-x-[LIVH]-[LIVMC]-[DNV] REFERENCE 1 Adachi, O., Chiyonobu, T., Shinagawa, E., Matsushita, K. and Ameyama, M. Crystalline 2-ketogluconate reductase from Acetobacter ascendens, the second instance of crystalline enzyme in genus Acetobacter. Agric. Biol. Chem. 42 (1978) 2057. 2 Chiyonobu, T., Shinagawa, E., Adachi, O. and Ameyama, M. Purification, crystallization and properties of 2-ketogluconate reductase from Acetobacter rancens. Agric. Biol. Chem. 40 (1976) 175-184. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.215 ExPASy - ENZYME nomenclature database: 1.1.1.215 ERGO genome analysis and discovery system: 1.1.1.215 BRENDA, the Enzyme Database: 1.1.1.215 CAS: 68417-42-5 /// ENTRY EC 1.1.1.216 NAME farnesol dehydrogenase NADP-farnesol dehydrogenase farnesol (nicotinamide adenine dinucleotide phosphate) dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 2-trans,6-trans-farnesol:NADP+ 1-oxidoreductase REACTION 2-trans,6-trans-farnesol + NADP+ = 2-trans,6-trans-farnesal + NADPH + H+ SUBSTRATE 2-trans,6-trans-farnesol NADP+ PRODUCT 2-trans,6-trans-farnesal NADPH H+ COMMENT Also acts, more slowly, on 2-cis,6-trans-farnesol, geraniol, citronerol and nerol. REFERENCE 1 Inoue, H., Tsuji, H. and Uritani, I. Characterization and activity change of farnesol dehydrogenase in black rot fungus-infected sweet-potato. Agric. Biol. Chem. 48 (1984) 733-738. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.216 ExPASy - ENZYME nomenclature database: 1.1.1.216 ERGO genome analysis and discovery system: 1.1.1.216 BRENDA, the Enzyme Database: 1.1.1.216 CAS: 90804-55-0 /// ENTRY EC 1.1.1.217 NAME benzyl-2-methyl-hydroxybutyrate dehydrogenase benzyl 2-methyl-3-hydroxybutyrate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME benzyl-(2R,3S)-2-methyl-3-hydroxybutanoate:NADP+ 3-oxidoreductase REACTION benzyl (2R,3S)-2-methyl-3-hydroxybutanoate + NADP+ = benzyl 2-methyl-3-oxobutanoate + NADPH + H+ SUBSTRATE benzyl (2R,3S)-2-methyl-3-hydroxybutanoate NADP+ PRODUCT benzyl 2-methyl-3-oxobutanoate NADPH H+ COMMENT Also acts on benzyl (2S,3S)-2-methyl-3-hydroxybutanoate; otherwise highly specific. REFERENCE 1 Furuichi, A., Akita, H., Matsukura, H., Oishi, T. and Horikoshi, K. Purification and properties of an asymmetric reduction enzyme of 2-methyl-3-oxobutyrate in baker's yeast. Agric. Biol. Chem. 49 (1985) 2563-2570. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.217 ExPASy - ENZYME nomenclature database: 1.1.1.217 ERGO genome analysis and discovery system: 1.1.1.217 BRENDA, the Enzyme Database: 1.1.1.217 CAS: 99332-62-4 /// ENTRY EC 1.1.1.218 NAME morphine 6-dehydrogenase naloxone reductase reductase, naloxone CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME morphine:NAD(P)+ 6-oxidoreductase REACTION morphine + NAD(P)+ = morphinone + NAD(P)H + H+ SUBSTRATE morphine NAD+ NADP+ PRODUCT morphinone NADH NADPH H+ COMMENT Also acts on some other alkaloids, including codeine, normorphine and ethylmorphine, but only very slowly on 7,8-saturated derivatives such as dihydromorphine and dihydrocodeine. In the reverse direction, also reduces naloxone to the 6alpha-hydroxy analogue. Activated by 2-mercaptoethanol. PATHWAY PATH: map00950 Alkaloid biosynthesis I ORTHOLOG KO: K03378 morphine 6-dehydrogenase GENES LMF: LMOf2365_2565(morA) CGL: NCgl1003(Cgl1048) NCgl1302(Cgl1356) MOTIF PS: PS00062 [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY] PS: PS00063 [LIVM]-[PAIV]-[KR]-[ST]-x(4)-R-x(2)-[GSTAEQK]-[NSL]- x(2)-[LIVMFA] PS: PS00798 G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGC]-[AS]-x(5)-E-x(2)- [LIVM]-G REFERENCE 1 [PMID:2580834] Yamano, S., Kaguera, E., Ishida, T. and Toki, S. Purification and characterization of guinea pig liver morphine 6-dehydrogenase. J. Biol. Chem. 260 (1985) 5259-5264. 2 [PMID:3539118] Yamano, S., Nishida, F. and Toki, S. Guinea-pig liver morphine 6-dehydrogenase as a naloxone reductase. Biochem. Pharmacol. 35 (1986) 4321-4326. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.218 ExPASy - ENZYME nomenclature database: 1.1.1.218 ERGO genome analysis and discovery system: 1.1.1.218 BRENDA, the Enzyme Database: 1.1.1.218 CAS: 97002-71-6 /// ENTRY EC 1.1.1.219 NAME dihydrokaempferol 4-reductase dihydroflavanol 4-reductase dihydromyricetin reductase NADPH-dihydromyricetin reductase dihydroquercetin reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase REACTION cis-3,4-leucopelargonidin + NADP+ = (+)-dihydrokaempferol + NADPH + H+ SUBSTRATE cis-3,4-leucopelargonidin NADP+ PRODUCT (+)-dihydrokaempferol NADPH H+ COMMENT Also acts, in the reverse direction, on (+)-dihydroquercitin and (+)-dihydromyricetin; each dihydroflavonol is reduced to the corresponding cis-flavan-3,4-diol. NAD+ can act instead of NADP+, but more slowly. Involved in the biosynthesis of anthocyanidins in plants. PATHWAY PATH: map00941 Flavonoid biosynthesis ORTHOLOG KO: K00091 dihydroflavonol-4-reductase GENES ATH: At1g61720(T13M11.8) At5g42800(MJB21.18) CAL: orf19.2581 orf19.3150(GRP4) orf19.3151(GRP6) orf19.6868(GRP5) CVI: CV0690(hpnA) NEU: NE1170(dfrA) GSU: GSU0687 BBA: Bd0142(dfrA) BJA: bll5833 blr6564 MTU: Rv0139 MTC: MT0147 MPA: MAP3556 SYN: slr1706(dfrA) TEL: tlr1370 GVI: glr1747 ANA: alr4268 PMM: PMM1377 REFERENCE 1 Heller, W., Forkmann, G., Britsch, L. and Grisebach, H. Enzymatic reduction of (+)-dihydroflavonols to flavan-3,4-cis- diols with flower extracts from Matthiola incana and its role in anthocyanin biosynthesis. Planta 165 (1985) 284-287. 2 Stafford, H.A. and Lester, H.H. Flavan-3-ol biosynthesis - the conversion of (+)- dihydromyricetin to its flavan-3,4-diol (leucodelphinidin) and to (+)-gallocatechin by reductases extracted from tissue-cultures of Ginkgo biloba and Pseudotsuga-menziesii. Plant Physiol. 78 (1985) 791-794. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.219 ExPASy - ENZYME nomenclature database: 1.1.1.219 ERGO genome analysis and discovery system: 1.1.1.219 BRENDA, the Enzyme Database: 1.1.1.219 CAS: 98668-58-7 /// ENTRY EC 1.1.1.220 NAME 6-pyruvoyltetrahydropterin 2'-reductase 6-pyruvoyltetrahydropterin reductase 6PPH4(2'-oxo) reductase 6-pyruvoyl tetrahydropterin (2'-oxo)reductase 6-pyruvoyl-tetrahydropterin 2'-reductase pyruvoyl-tetrahydropterin reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 6-lactoyl-5,6,7,8-tetrahydropterin:NADP+ 2'-oxidoreductase REACTION 6-lactoyl-5,6,7,8-tetrahydropterin + NADP+ = 6-pyruvoyltetrahydropterin + NADPH + H+ SUBSTRATE 6-lactoyl-5,6,7,8-tetrahydropterin NADP+ PRODUCT 6-pyruvoyltetrahydropterin NADPH H+ COMMENT Not identical with EC 1.1.1.153 sepiapterin reductase. PATHWAY PATH: map00790 Folate biosynthesis ORTHOLOG KO: K04071 6-pyruvoyltetrahydropterin 2'-reductase GENES PTO: PTO1063 REFERENCE 1 [PMID:4004850] Milstien, S. and Kaufman, S. Biosynthesis of tetrahydrobiopterin: conversion of dihydroneopterin triphosphate to tetrahydropterin intermediates. Biochem. Biophys. Res. Commun. 128 (1985) 1099-1107. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.220 ExPASy - ENZYME nomenclature database: 1.1.1.220 ERGO genome analysis and discovery system: 1.1.1.220 BRENDA, the Enzyme Database: 1.1.1.220 CAS: 97089-79-7 /// ENTRY EC 1.1.1.221 NAME vomifoliol 4'-dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME vomifoliol:NAD+ 4'-oxidoreductase REACTION (+/-)-6-hydroxy-3-oxo-alpha-ionol + NAD+ = (+/-)-6-hydroxy-3-oxo-alpha-ionone + NADH + H+ SUBSTRATE (+/-)-6-hydroxy-3-oxo-alpha-ionol NAD+ PRODUCT (+/-)-6-hydroxy-3-oxo-alpha-ionone NADH H+ COMMENT Oxidizes vomifoliol to dehydrovomifoliol; involved in the metabolism of abscisic acid in Corynebacterium sp. REFERENCE 1 Hasegawa, S., Poling, S.M., Maier, V.P. and Bennett, R.D. Metabolism of abscisic-acid - bacterial conversion to dehydrovomifoliol and vomifoliol dehydrogenase-activity Phytochemistry 23 (1984) 2769-2771. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.221 ExPASy - ENZYME nomenclature database: 1.1.1.221 ERGO genome analysis and discovery system: 1.1.1.221 BRENDA, the Enzyme Database: 1.1.1.221 CAS: 94949-18-5 /// ENTRY EC 1.1.1.222 NAME (R)-4-hydroxyphenyllactate dehydrogenase (R)-aromatic lactate dehydrogenase D-hydrogenase, D-aryllactate CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (R)-3-(4-hydroxyphenyl)lactate:NAD(P)+ 2-oxidoreductase REACTION (R)-3-(4-hydroxyphenyl)lactate + NAD(P)+ = 3-(4-hydroxyphenyl)pyruvate + NAD(P)H + H+ SUBSTRATE (R)-3-(4-hydroxyphenyl)lactate NAD+ NADP+ PRODUCT 3-(4-hydroxyphenyl)pyruvate NADH NADPH H+ COMMENT Also acts, more slowly, on (R)-3-phenyllactate, (R)-3-(indole-3-yl)lactate and (R)-lactate. PATHWAY PATH: map00350 Tyrosine metabolism PATH: map00360 Phenylalanine metabolism REFERENCE 1 Bode, R., Lippoldt, A. and Birnbaum, D. Purification and properties of D-aromatic lactate dehydrogenase an enzyme involved in the catabolism of the aromatic amino acids of Candida maltosa. Biochem. Physiol. Pflanzen 181 (1986) 189-198. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.222 ExPASy - ENZYME nomenclature database: 1.1.1.222 ERGO genome analysis and discovery system: 1.1.1.222 BRENDA, the Enzyme Database: 1.1.1.222 CAS: 101754-02-3 /// ENTRY EC 1.1.1.223 NAME isopiperitenol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (-)-trans-isopiperitenol:NAD+ oxidoreductase REACTION (-)-trans-isopiperitenol + NAD+ = (-)-isopiperitenone + NADH + H+ SUBSTRATE (-)-trans-isopiperitenol NAD+ PRODUCT (-)-isopiperitenone NADH H+ COMMENT Acts on (-)-trans-isopiperitenol, (+)-trans-piperitenol and (+)-trans-pulegol. Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves. PATHWAY PATH: map00902 Monoterpenoid biosynthesis REFERENCE 1 [PMID:3885858] Kjonaas, R.B., Venkatachalam, K.V. and Croteau, R. Metabolism of monoterpenes: oxidation of isopiperitenol to isopiperitenone, and subsequent isomerization to piperitenone by soluble enzyme preparations from peppermint (Mentha piperita) leaves. Arch. Biochem. Biophys. 238 (1985) 49-60. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.223 ExPASy - ENZYME nomenclature database: 1.1.1.223 ERGO genome analysis and discovery system: 1.1.1.223 UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.223 BRENDA, the Enzyme Database: 1.1.1.223 CAS: 96595-05-0 /// ENTRY EC 1.1.1.224 NAME mannose-6-phosphate 6-reductase NADPH-dependent mannose 6-phosphate reductase mannose-6-phosphate reductase 6-phosphomannose reductase NADP-dependent mannose-6-P:mannitol-1-P oxidoreductase NADPH-dependent M6P reductase NADPH-mannose-6-P reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME D-mannitol-1-phosphate:NADP+ 6-oxidoreductase REACTION D-mannitol 1-phosphate + NADP+ = D-mannose 6-phosphate + NADPH + H+ SUBSTRATE D-mannitol 1-phosphate NADP+ PRODUCT D-mannose 6-phosphate NADPH H+ COMMENT Involved in the biosynthesis of mannitol in celery (Apium graveolens) leaves. REFERENCE 1 Rumpho, M.E., Edwards, G.E. and Loescher, W.H. A pathway for photosynthetic carbon flow to mannitol in celery leaves - Activity and localization of key enzymes. Plant Physiol. 73 (1983) 869-873. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.224 ExPASy - ENZYME nomenclature database: 1.1.1.224 ERGO genome analysis and discovery system: 1.1.1.224 BRENDA, the Enzyme Database: 1.1.1.224 CAS: 88747-79-9 /// ENTRY EC 1.1.1.225 NAME chlordecone reductase CDR CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME chlordecone-alcohol:NADP+ 2-oxidoreductase REACTION chlordecone alcohol + NADP+ = chlordecone + NADPH + H+ SUBSTRATE chlordecone alcohol NADP+ PRODUCT chlordecone NADPH H+ COMMENT Chlordecone is an organochlorine pesticide. GENES HSA: 1109(AKR1C4) MOTIF PS: PS00062 [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY] PS: PS00063 [LIVM]-[PAIV]-[KR]-[ST]-x(4)-R-x(2)-[GSTAEQK]-[NSL]- x(2)-[LIVMFA] PS: PS00798 G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGC]-[AS]-x(5)-E-x(2)- [LIVM]-G REFERENCE 1 [PMID:2427522] Molowa, D.T., Shayne, A.G. and Guzelian, P.S. Purification and characterization of chlordecone reductase from human liver. J. Biol. Chem. 261 (1986) 12624-12627. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.225 ExPASy - ENZYME nomenclature database: 1.1.1.225 ERGO genome analysis and discovery system: 1.1.1.225 BRENDA, the Enzyme Database: 1.1.1.225 CAS: 102484-73-1 /// ENTRY EC 1.1.1.226 NAME 4-hydroxycyclohexanecarboxylate dehydrogenase trans-4-hydroxycyclohexanecarboxylate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME trans-4-hydroxycyclohexanecarboxylate:NAD+ 4-oxidoreductase REACTION trans-4-hydroxycyclohexanecarboxylate + NAD+ = 4-oxocyclohexanecarboxylate + NADH + H+ SUBSTRATE trans-4-hydroxycyclohexanecarboxylate NAD+ PRODUCT 4-oxocyclohexanecarboxylate NADH H+ COMMENT The enzyme from Corynebacterium cyclohexanicum is highly specific for the trans-4-hydroxy derivative. REFERENCE 1 [PMID:3292236] Obata, H., Uebayashi, M. and Kaneda, T. Purification and properties of 4-hydroxycyclohexanecarboxylate dehydrogenase from Corynebacterium cyclohexanicum. Eur. J. Biochem. 174 (1988) 451-458. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.226 ExPASy - ENZYME nomenclature database: 1.1.1.226 ERGO genome analysis and discovery system: 1.1.1.226 BRENDA, the Enzyme Database: 1.1.1.226 CAS: 67272-36-0 /// ENTRY EC 1.1.1.227 NAME (-)-borneol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (-)-borneol:NAD+ oxidoreductase REACTION (-)-borneol + NAD+ = (-)-camphor + NADH + H+ SUBSTRATE (-)-borneol NAD+ PRODUCT (-)-camphor NADH H+ COMMENT NADP+ can also act, but more slowly. REFERENCE 1 [PMID:3310901] Dehal, S.S. and Croteau, R. Metabolism of monoterpenes: specificity of the dehydrogenases responsible for the biosynthesis of camphor, 3-thujone, and 3-isothujone. Arch. Biochem. Biophys. 258 (1987) 287-291. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.227 ExPASy - ENZYME nomenclature database: 1.1.1.227 ERGO genome analysis and discovery system: 1.1.1.227 BRENDA, the Enzyme Database: 1.1.1.227 CAS: 111940-48-8 /// ENTRY EC 1.1.1.228 NAME (+)-sabinol dehydrogenase (+)-cis-sabinol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (+)-cis-sabinol:NAD+ oxidoreductase REACTION (+)-cis-sabinol + NAD+ = (+)-sabinone + NADH + H+ SUBSTRATE (+)-cis-sabinol NAD+ PRODUCT (+)-sabinone NADH H+ COMMENT NADP+ can also act, but more slowly. Involved in the biosynthesis of (+)-3-thujone and (-)-3-isothujone. REFERENCE 1 [PMID:3310901] Dehal, S.S. and Croteau, R. Metabolism of monoterpenes: specificity of the dehydrogenases responsible for the biosynthesis of camphor, 3-thujone, and 3-isothujone. Arch. Biochem. Biophys. 258 (1987) 287-291. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.228 ExPASy - ENZYME nomenclature database: 1.1.1.228 ERGO genome analysis and discovery system: 1.1.1.228 BRENDA, the Enzyme Database: 1.1.1.228 CAS: 111940-50-2 /// ENTRY EC 1.1.1.229 NAME diethyl 2-methyl-3-oxosuccinate reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME diethyl-(2R,3R)-2-methyl-3-hydroxysuccinate:NADP+ 3-oxidoreductase REACTION diethyl (2R,3R)-2-methyl-3-hydroxysuccinate + NADP+ = diethyl 2-methyl-3-oxosuccinate + NADPH + H+ SUBSTRATE diethyl (2R,3R)-2-methyl-3-hydroxysuccinate NADP+ PRODUCT diethyl 2-methyl-3-oxosuccinate NADPH H+ COMMENT Also acts on diethyl (2S,3R)-2-methyl-3-hydroxysuccinate; and on the corresponding dimethyl esters. REFERENCE 1 Furuichi, A., Akita, H., Matsukura, H., Oishi, T. and Horikoshi, K. Purification and properties of an asymmetric reduction of diethyl 2-methyl-3-oxosuccinate in Saccharomyces fermentati. Agric. Biol. Chem. 51 (1987) 293-299. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.229 ExPASy - ENZYME nomenclature database: 1.1.1.229 ERGO genome analysis and discovery system: 1.1.1.229 BRENDA, the Enzyme Database: 1.1.1.229 CAS: 110369-21-6 /// ENTRY EC 1.1.1.230 NAME 3alpha-hydroxyglycyrrhetinate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3alpha-hydroxyglycyrrhetinate:NADP+ 3-oxidoreductase REACTION 3alpha-hydroxyglycyrrhetinate + NADP+ = 3-oxoglycyrrhetinate + NADPH + H+ SUBSTRATE 3alpha-hydroxyglycyrrhetinate NADP+ PRODUCT 3-oxoglycyrrhetinate NADPH H+ COMMENT Highly specific to 3alpha-hydroxy derivatives of glycyrrhetinate and its analogues. Not identical to EC 1.1.1.50 3alpha-hydroxysteroid dehydrogenase (B-specific). REFERENCE 1 [PMID:3164718] Akao, T., Akao, T., Hattori, M., Namba, T. and Kobashi, K. Purification and properties of 3alpha-hydroxyglycyrrhetinate dehydrogenase of Clostridium innocuum from human intestine. J. Biochem. (Tokyo) 103 (1988) 504-507. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.230 ExPASy - ENZYME nomenclature database: 1.1.1.230 ERGO genome analysis and discovery system: 1.1.1.230 BRENDA, the Enzyme Database: 1.1.1.230 CAS: 114308-07-5 /// ENTRY EC 1.1.1.231 NAME 15-hydroxyprostaglandin-I dehydrogenase (NADP+) prostacyclin dehydrogenase PG I2 dehydrogenase NADP-linked 15-hydroxyprostaglandin (prostacyclin) dehydrogenase NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase 15-hydroxyprostaglandin-I dehydrogenase (NADP) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13- $dienoate:NADP+ 15-oxidoreductase REACTION (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13- $dienoate + NADP+ = (5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15- $oxoprosta-5,13-dienoate + NADPH + H+ SUBSTRATE (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13- $dienoate NADP+ PRODUCT (5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate NADPH H+ COMMENT Specific for prostaglandin I2. REFERENCE 1 [PMID:6182444] Korff, J.M. and Jarabak, J. Isolation and properties of an NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase from rabbit kidney. Methods Enzymol. 86 (1982) 152-155. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.231 ExPASy - ENZYME nomenclature database: 1.1.1.231 ERGO genome analysis and discovery system: 1.1.1.231 BRENDA, the Enzyme Database: 1.1.1.231 CAS: 79468-49-8 /// ENTRY EC 1.1.1.232 NAME 15-hydroxyicosatetraenoate dehydrogenase 15-hydroxyeicosatetraenoate dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate:NAD(P)+ $15-oxidoreductase REACTION (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)+ = 15-oxo-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)H + H+ SUBSTRATE (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate NAD+ NADP+ PRODUCT 15-oxo-5,8,11-cis-13-trans-icosatetraenoate NADH NADPH H+ REFERENCE 1 [PMID:3052453] Sok, D.-E., Kang, J.B. and Shin, H.D. 15-Hydroxyeicosatetraenoic acid dehydrogenase activity in microsomal fraction of mouse liver homogenate. Biochem. Biophys. Res. Commun. 156 (1988) 524-529. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.232 ExPASy - ENZYME nomenclature database: 1.1.1.232 ERGO genome analysis and discovery system: 1.1.1.232 BRENDA, the Enzyme Database: 1.1.1.232 CAS: 117910-46-0 /// ENTRY EC 1.1.1.233 NAME N-acylmannosamine 1-dehydrogenase N-acylmannosamine dehydrogenase N-acetyl-D-mannosamine dehydrogenase N-acyl-D-mannosamine dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME N-acyl-D-mannosamine:NAD+ 1-oxidoreductase REACTION N-acyl-D-mannosamine + NAD+ = N-acyl-D-mannosaminolactone + NADH + H+ SUBSTRATE N-acyl-D-mannosamine NAD+ PRODUCT N-acyl-D-mannosaminolactone NADH H+ COMMENT Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine. Highly specific. PATHWAY PATH: map00530 Aminosugars metabolism GENES BCZ: BTZK4967(wecC) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] REFERENCE 1 [PMID:3240988] Horiuchi, T. and Kurokawa, T. Purification and properties of N-acyl-D-mannosamine dehydrogenase from Flavobacterium sp. 141-8. J. Biochem. (Tokyo) 104 (1988) 466-471. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.233 ExPASy - ENZYME nomenclature database: 1.1.1.233 ERGO genome analysis and discovery system: 1.1.1.233 BRENDA, the Enzyme Database: 1.1.1.233 CAS: 117698-08-5 /// ENTRY EC 1.1.1.234 NAME flavanone 4-reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (2S)-flavan-4-ol:NADP+ 4-oxidoreductase REACTION (2S)-flavan-4-ol + NADP+ = (2S)-flavanone + NADPH + H+ SUBSTRATE (2S)-flavan-4-ol NADP+ PRODUCT (2S)-flavanone NADPH H+ COMMENT Involved in the biosynthesis of 3-deoxyanthocyanidins from flavanones such as naringenin or eriodictyol. PATHWAY PATH: map00941 Flavonoid biosynthesis REFERENCE 1 Stich, K. and Forkmann, G. Biosynthesis of 3-deoxyanthocyanins with flower extracts from Sinningia cardinalis. Phytochemistry 27 (1988) 785-789. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.234 ExPASy - ENZYME nomenclature database: 1.1.1.234 ERGO genome analysis and discovery system: 1.1.1.234 BRENDA, the Enzyme Database: 1.1.1.234 CAS: 115232-53-6 /// ENTRY EC 1.1.1.235 NAME 8-oxocoformycin reductase 8-ketodeoxycoformycin reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME coformycin:NADP+ 8-oxidoreductase REACTION coformycin + NADP+ = 8-oxocoformycin + NADPH + H+ SUBSTRATE coformycin NADP+ PRODUCT 8-oxocoformycin NADPH H+ COMMENT B-specific with respect to NADPH. Also reduces 8-oxodeoxy-coformycin to the nucleoside antibiotic deoxycoformycin. REFERENCE 1 [PMID:3052586] Hanvey, J.C., Hawkins, E.S., Baker, D.C. and Suhadolnick, R.J. 8-Ketodeoxycoformycin and 8-ketocoformycin as intermediates in the biosynthesis of 2'-deoxycoformycin and coformycin. Biochemistry 27 (1988) 5790-5795. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.235 ExPASy - ENZYME nomenclature database: 1.1.1.235 ERGO genome analysis and discovery system: 1.1.1.235 BRENDA, the Enzyme Database: 1.1.1.235 CAS: 114995-16-3 /// ENTRY EC 1.1.1.236 NAME tropinone reductase tropinone (psi-tropine-forming) reductase tropinone reductase II pseudotropine forming tropinone reductase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME pseudotropine:NADP+ 3-oxidoreductase REACTION pseudotropine + NADP+ = tropinone + NADPH + H+ SUBSTRATE pseudotropine NADP+ PRODUCT tropinone NADPH H+ PATHWAY PATH: map00960 Alkaloid biosynthesis II ORTHOLOG KO: K05354 tropinone reductase GENES CAL: orf19.5879(AYR2) MOTIF PS: PS00061 [LIVSPADNK]-x(12)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K- {PC}-[SAGFYR]-[LIVMSTAGD]-x(2)-[LIVMFYW]-x(3)- [LIVMFYWGAPTHQ]-[GSACQRHM] STRUCTURES PDB: 1AE1 1IPE 1IPF 1XHL 2AE1 2AE2 REFERENCE 1 Drager, B., Hashimoto, T. and Yamada, Y. Purification and characterization of pseudotropine forming tropinone reductase from Hyoscyamus niger root cultures. Agric. Biol. Chem. 52 (1988) 2663-2667. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.236 ExPASy - ENZYME nomenclature database: 1.1.1.236 ERGO genome analysis and discovery system: 1.1.1.236 BRENDA, the Enzyme Database: 1.1.1.236 CAS: 136111-61-0 /// ENTRY EC 1.1.1.237 NAME hydroxyphenylpyruvate reductase HPRP CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 4-hydroxyphenyllactate:NAD+ oxidoreductase REACTION 3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+ SUBSTRATE 3-(4-hydroxyphenyl)lactate NAD+ PRODUCT 3-(4-hydroxyphenyl)pyruvate NADH H+ COMMENT Also acts on 3-(3,4-dihydroxyphenyl)lactate. Involved with EC 2.3.1.140 rosmarinate synthase in the biosynthesis of rosmarinic acid. PATHWAY PATH: map00350 Tyrosine metabolism PATH: map00360 Phenylalanine metabolism REFERENCE 1 Petersen, M. and Alfermann, A.W. Two new enzymes of rosmarinic acid biosynthesis from cell cultures of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic acid synthase. Z. Naturforsch. C: Biosci. 43 (1988) 501-504. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.237 ExPASy - ENZYME nomenclature database: 1.1.1.237 ERGO genome analysis and discovery system: 1.1.1.237 BRENDA, the Enzyme Database: 1.1.1.237 CAS: 117590-77-9 /// ENTRY EC 1.1.1.238 NAME 12beta-hydroxysteroid dehydrogenase 12beta-hydroxy steroid (nicotinamide adenine dinucleotide $phosphate) dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 12beta-hydroxysteroid:NADP+ 12-oxidoreductase REACTION 3alpha,7alpha,12beta-trihydroxy-5beta-cholanate + NADP+ = 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADPH + H+ SUBSTRATE 3alpha,7alpha,12beta-trihydroxy-5beta-cholanate NADP+ PRODUCT 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate NADPH H+ COMMENT Acts on a number of bile acids, both in their free and conjugated forms. REFERENCE 1 [PMID:3167086] Edenharder, R. and Pfutzner, A. Characterization of NADP-dependent 12beta-hydroxysteroid dehydrogenase from Clostridium paraputrificum. Biochim. Biophys. Acta 962 (1988) 362-370. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.238 ExPASy - ENZYME nomenclature database: 1.1.1.238 ERGO genome analysis and discovery system: 1.1.1.238 BRENDA, the Enzyme Database: 1.1.1.238 CAS: 118390-62-8 /// ENTRY EC 1.1.1.239 NAME 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+) 3alpha,17beta-hydroxy steroid dehydrogenase 3alpha(17beta)-HSD 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 3alpha(or 17beta)-hydroxysteroid:NAD+ oxidoreductase REACTION testosterone + NAD+ = androst-4-ene-3,17-dione + NADH + H+ SUBSTRATE testosterone NAD+ PRODUCT androst-4-ene-3,17-dione NADH H+ COMMENT Also acts on other 17beta-hydroxysteroids, on the 3alpha-hydroxy group of pregnanes and bile acids, and on benzene dihydrodiol. Different from EC 1.1.1.50 3alpha-hydroxysteroid dehydrogenase (B-specific) or EC 1.1.1.213 3alpha-hydroxysteroid dehydrogenase (A-specific). PATHWAY PATH: map00150 Androgen and estrogen metabolism REFERENCE 1 [PMID:2317205] Ohmura, M., Hara, A., Nakagawa, M. and Sawada, H. Demonstration of 3alpha(17beta)-hydroxysteroid dehydrogenase distinct from 3alpha-hydroxysteroid dehydrogenase in hamster liver. Biochem. J. 266 (1990) 583-589. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.239 ExPASy - ENZYME nomenclature database: 1.1.1.239 ERGO genome analysis and discovery system: 1.1.1.239 BRENDA, the Enzyme Database: 1.1.1.239 CAS: 126469-82-7 /// ENTRY EC 1.1.1.240 NAME N-acetylhexosamine 1-dehydrogenase N-acetylhexosamine dehydrogenase N-acetyl-D-hexosamine dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME N-acetyl-D-hexosamine:NAD+ 1-oxidoreductase REACTION N-acetyl-D-glucosamine + NAD+ = N-acetyl-D-glucosaminate + NADH + H+ SUBSTRATE N-acetyl-D-glucosamine NAD+ PRODUCT N-acetyl-D-glucosaminate NADH H+ COMMENT Also acts on N-acetylgalactosamine and, more slowly, on N-acetylmannosamine. REFERENCE 1 Horiuchi, T. and Kurokawa, T. Purification and characterization of N-acetyl-D-hexosamine dehydrogenase from Pseudomonas sp no 53. Agric. Biol. Chem. 53 (1989) 1919-1925. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.240 ExPASy - ENZYME nomenclature database: 1.1.1.240 ERGO genome analysis and discovery system: 1.1.1.240 BRENDA, the Enzyme Database: 1.1.1.240 CAS: 122785-18-6 /// ENTRY EC 1.1.1.241 NAME 6-endo-hydroxycineole dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME 6-endo-hydroxycineole:NAD+ 6-oxidoreductase REACTION 6-endo-hydroxycineole + NAD+ = 6-oxocineole + NADH + H+ SUBSTRATE 6-endo-hydroxycineole NAD+ PRODUCT 6-oxocineole NADH H+ PATHWAY PATH: map00900 Terpenoid biosynthesis REFERENCE 1 Williams, D.R., Trudgill, P.W. and Taylor, D.G. Metabolism of 1,8-cineole by Rhodococcus species: ring cleavage reactions. J. Gen. Microbiol. 135 (1989) 1957-1967. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.241 ExPASy - ENZYME nomenclature database: 1.1.1.241 ERGO genome analysis and discovery system: 1.1.1.241 BRENDA, the Enzyme Database: 1.1.1.241 CAS: 122933-68-0 /// ENTRY EC 1.1.1.242 Obsolete NAME Transferred to 1.3.1.69 CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT Transferred entry: now EC 1.3.1.69 zeatin reductase (EC 1.1.1.242 created 1992, deleted 2001) DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.242 ExPASy - ENZYME nomenclature database: 1.1.1.242 ERGO genome analysis and discovery system: 1.1.1.242 BRENDA, the Enzyme Database: 1.1.1.242 /// ENTRY EC 1.1.1.243 NAME carveol dehydrogenase (-)-trans-carveol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME (-)-trans-carveol:NADP+ oxidoreductase REACTION (-)-trans-carveol + NADP+ = (-)-carvone + NADPH + H+ SUBSTRATE (-)-trans-carveol NADP+ PRODUCT (-)-carvone NADPH H+ PATHWAY PATH: map00902 Monoterpenoid biosynthesis PATH: map00903 Limonene and pinene degradation REFERENCE 1 Gershenzon, J., Maffei, M. and Croteau, R. Biochemical and histochemical-localization of monoterpene biosynthesis in the glandular trichomes of spearmint (Mentha spicata). Plant Physiol. 89 (1989) 1351-1357. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.243 ExPASy - ENZYME nomenclature database: 1.1.1.243 ERGO genome analysis and discovery system: 1.1.1.243 UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.243 BRENDA, the Enzyme Database: 1.1.1.243 CAS: 122653-66-1 /// ENTRY EC 1.1.1.244 NAME methanol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME methanol:NAD+ oxidoreductase REACTION methanol + NAD+ = formaldehyde + NADH + H+ SUBSTRATE methanol NAD+ PRODUCT formaldehyde NADH H+ PATHWAY PATH: map00680 Methane metabolism ORTHOLOG KO: K00093 methanol dehydrogenase GENES YPE: YPO0327 YPS: YPTB0382 MOTIF PS: PS00060 [GSW]-x-[LIVTSACD]-[GH]-x(2)-[GSAE]-[GSHYQ]-x-[LIVTP]- [GAST]-[GAS]-x(3)-[LIVMT]-x-[HNS]-[GA]-x-[GTAC] PS: PS00913 [STALIV]-[LIVF]-x-[DE]-x(6,7)-P-x(4)-[ALIV]-x-[GST]- x(2)-D-[TAIVM]-[LIVMF]-x(4)-E REFERENCE 1 [PMID:2673121] Arfman, N., Watling, E.M., Clement, W., van Oosterwijk, R.J., de Vries, G.E., Harder, W., Attwood, M.M. and Dijkhuizen, L. Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme. Arch. Microbiol. 152 (1989) 280-288. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.244 ExPASy - ENZYME nomenclature database: 1.1.1.244 ERGO genome analysis and discovery system: 1.1.1.244 BRENDA, the Enzyme Database: 1.1.1.244 CAS: 74506-37-9 /// ENTRY EC 1.1.1.245 NAME cyclohexanol dehydrogenase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME cyclohexanol:NAD+ oxidoreductase REACTION cyclohexanol + NAD+ = cyclohexanone + NADH + H+ SUBSTRATE cyclohexanol NAD+ PRODUCT cyclohexanone NADH H+ COMMENT Also oxidizes some other alicyclic alcohols and diols. PATHWAY PATH: map00930 Caprolactam degradation REFERENCE 1 Dangel, W., Tschech, A. and Fuchs, G. Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species. Arch. Microbiol. 152 (1989) 273-279. 2 [PMID:1261] Donoghue, N.A. and Trudgill, P.W. The metabolism of cyclohexanol by Acinetobacter NCIB 9871. Eur. J. Biochem. 60 (1975) 1-7. 3 Trower, M.K., Buckland, R.M., Higgins, R. and Griffin, M. Isolation and characterization of a cyclohexane-metabolizing Xanthobacter sp. Appl. Environ. Microbiol. 49 (1985) 1282-1289. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.245 ExPASy - ENZYME nomenclature database: 1.1.1.245 ERGO genome analysis and discovery system: 1.1.1.245 UM-BBD (Biocatalysis/Biodegradation Database): 1.1.1.245 BRENDA, the Enzyme Database: 1.1.1.245 CAS: 63951-98-4 /// ENTRY EC 1.1.1.246 NAME pterocarpin synthase pterocarpan synthase CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME medicarpin:NADP+ 2'-oxidoreductase REACTION medicarpin + NADP+ = vestitone + NADPH + H+ SUBSTRATE medicarpin NADP+ PRODUCT vestitone NADPH H+ COMMENT Catalyses the final step in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain. REFERENCE 1 Bless, W. and Barz, W. Isolation of pterocarpan synthase, the terminal enzyme of pterocarpan phytoalexin biosynthesis in cell-suspension cultures of Cicer arietinum. FEBS Lett. 235 (1988) 47-50. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.246 ExPASy - ENZYME nomenclature database: 1.1.1.246 ERGO genome analysis and discovery system: 1.1.1.246 BRENDA, the Enzyme Database: 1.1.1.246 CAS: 118477-70-6 /// ENTRY EC 1.1.1.247 NAME codeinone reductase (NADPH) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME codeine:NADP+ oxidoreductase REACTION codeine + NADP+ = codeinone + NADPH + H+ SUBSTRATE codeine NADP+ PRODUCT codeinone NADPH H+ COMMENT Catalyses the reversible reduction of codeinone to codeine, which is a direct precursor of morphine in the opium poppy plant, Papaver somniferum. PATHWAY PATH: map00950 Alkaloid biosynthesis I REFERENCE 1 Lenz, R. and Zenk, M.H. Stereoselective reduction of codeinone, the penultimate step during morphine biosynthesis in Papaver somniferum. Tetrahedron Lett. 36 (1995) 2449-2452. 2 [PMID:7588736] Lenz, R. and Zenk, M.H. Purification and properties of codeinone reductase (NADPH) from Papaver somniferum cell cultures. Eur. J. Biochem. 233 (1995) 132-139. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.247 ExPASy - ENZYME nomenclature database: 1.1.1.247 ERGO genome analysis and discovery system: 1.1.1.247 BRENDA, the Enzyme Database: 1.1.1.247 CAS: 153302-41-1 /// ENTRY EC 1.1.1.248 NAME salutaridine reductase (NADPH) CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor SYSNAME salutaridinol:NADP+ 7-oxidoreductase REACTION salutaridinol + NADP+ = salutaridine + NADPH + H+ SUBSTRATE salutaridinol NADP+ PRODUCT salutaridine NADPH H+ COMMENT Catalyses the reversible reduction of salutaridine to salutaridinol, which is a direct precursor of morphinan alkaloids in the poppy plant. PATHWAY PATH: map00950 Alkaloid biosynthesis I REFERENCE 1 Gerady, R. and Zenk, M.H. Purification and characterization of salutaridine:NADPH 7-oxidoreductase from Papaver somniferum. Phytochemistry 34 (1993) 125-132. DBLINKS IUBMB Enzyme Nomenclature: 1.1.1.248 ExPASy - ENZYME nomenclature database: 1.1.1.248 ERGO genome analysis and discovery system: 1.1.1.248 BRENDA, the Enzyme Database: 1.1.1.248 CAS: 152743-95-8 /// ENTRY EC 1.1.1.249 Obsolete NAME Deleted entry CLASS Oxidoreductases Acting on the CH-OH group of donors With NAD+ or NADP+ as acceptor COMMENT provisional entr