EC 1.1.1.1 to EC 1.1.1.50See separate file for EC 1.1.1.301 to EC 1.1.1.350
EC 1.1.1.51 to EC 1.1.1.100
EC 1.1.1.101 to EC 1.1.1.150
EC 1.1.1.151 to EC 1.1.1.200
EC 1.1.1.201 to EC 1.1.1.250
EC 1.1.1.301 to EC 1.1.1.350
EC 1.1.1.351 to EC 1.1.1.441
Accepted name: galactitol-1-phosphate 5-dehydrogenase
Reaction: galactitol-1-phosphate + NAD+ = D-tagatose 6-phosphate + NADH + H+
Other name(s): gatD (gene name)
Systematic name: galactitol-1-phosphate:NAD+ oxidoreductase
Comments: The enzyme from the bacterium Escherichia coli is involved in a galactitol degradation pathway. It contains two zinc atoms per subunit.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 60120-43-6
References:
1. Wolff, J.B., Kaplan, N.O. Hexitol metabolism in Escherichia coli. J. Bacteriol. 71 (1956) 557Ð564. [PMID: 13331868]
2. Nobelmann, B. and Lengeler, J.W. Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262 (1995) 69-72. [PMID: 7772602]
3. Benavente, R., Esteban-Torres, M., Kohring, G.W., Cortes-Cabrera, A., Sanchez-Murcia, P.A., Gago, F., Acebron, I., de las Rivas, B., Munoz, R. and Mancheno, J.M. Enantioselective oxidation of galactitol 1-phosphate by galactitol-1-phosphate 5-dehydrogenase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 71 (2015) 1540Ð1554. [PMID: 26143925]
Accepted name: tetrahydroxynaphthalene reductase
Reaction: scytalone + NADP+ = 1,3,6,8-tetrahydroxynaphthalene + NADPH + H+
Systematic name: scytalone:NADP+ δ5-oxidoreductase
Comments: Reduces 1,3,6,8-tetrahydroxynaphthalene to scytalone and also reduces 1,3,8-trihydroxynaphthalene to vermelone. Involved with EC 4.2.1.94 scytalone dehydratase in the biosynthesis of melanin in pathogenic fungi.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 141350-13-2
References:
1. Wheeler, M.H. and Greenblatt, G.A. The inhibition of melanin biosynthetic reactions in Pyricularia oryzae by compounds that prevent rice blast disease. Exp. Mycol. 12 (1988) 151-160.
2. Vidal-Cros, A., Viviani, F., Labesse, G., Boccara, M. and Gaudry M. Polyhydroxynaphthalene reductase involved in melanin biosynthesis in Magnaporthe grisea. Purification, cDNA cloning and sequencing. Eur. J. Biochem. 219 (1994) 985-992. [PMID: 8112349]
3. Thompson, J.E., Basarab, G.S., Andersson, A., Lindqvist, Y. and Jordan, D.B. Trihydroxynaphthalene reductase from Magnaporthe grisea: realization of an active center inhibitor and elucidation of the kinetic mechanism. Biochemistry 36 (1997) 1852-1860. [PMID: 9048570]
[EC 1.1.1.253 Transferred entry: now EC 1.5.1.33 pteridine reductase. (EC 1.1.1.253 created 1999, deleted 2003)]
Accepted name: (S)-carnitine 3-dehydrogenase
Reaction: (S)-carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+
Systematic name: (S)-carnitine:NAD+ oxidoreductase
Comments: specific for the (S)-enantiomer of carnitine, i.e., the enantiomer of the substrate of EC 1.1.1.108 carnitine 3-dehydrogenase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 54215-16-4, 169277-49-0
References:
1. Setyahadi, S., Ueyama, T., Arimoto, T., Mori, N. and Kitamoto, Y. Purification and properties of a new enzyme, D-carnitine dehydrogenase, from Agrobacterium sp. 525a. Biosci. Biotechnol. Biochem. 61 (1997) 1055-1058. [PMID: 9214773]
Accepted name: mannitol dehydrogenase
Reaction: D-mannitol + NAD+ = D-mannose + NADH + H+
Other name(s): MTD; NAD-dependent mannitol dehydrogenase
Systematic name: mannitol:NAD+ 1-oxidoreductase
Comments: The enzyme from Apium graveolens (celery) oxidizes alditols with a minimum requirement of 2R chirality at the carbon adjacent to the primary carbon undergoing the oxidation. The enzyme is specific for NAD+ and does not use NADP+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 144941-29-7
References:
1. Stoop, J.M.H. and Pharr, D.M. Partial purification and characterization of mannitol: mannose 1-oxidoreductase from celeriac (Apium graveolens var. rapaceum) roots. Arch. Biochem. Biophys. 298 (1992) 612-619. [PMID: 1416989]
2. Stoop, J.M.H., Williamson, J.D., Conkling, M.A. and Pharr, D.M. Purification of NAD-dependent mannitol dehydrogenase from celery suspension cultures. Plant Physiol. (1995) 108 (1995) 1219-1225. [PMID: 7630943]
3. Williamson, J.D., Stoop, J.M.H., Massel, M.O., Conkling, M.A. and Pharr, D.M. Sequence analysis of a mannitol dehydrogenase cDNA from plants reveals a function for the pathogenesis-related protein ELI3. Proc. Natl. Acad. Sci. USA 92 (1995) 7148-7152. [PMID: 7638158]
4. Stoop, J.M.H., Chilton, W.S. and Pharr, D.M. Substrate specificity of the NAD-dependent mannitol dehydrogenase from celery. Phytochemistry 43 (1996) 1145-1150.
Accepted name: fluoren-9-ol dehydrogenase
Reaction: fluoren-9-ol + NAD(P)+ = fluoren-9-one + NAD(P)H + H+
For diagram click here.
Systematic name: fluoren-9-ol:NAD(P)+ oxidoreductase
Comments: Involved in the pathway for fluorene metabolism in Arthrobacter sp.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 154215-16-4
References:
1. Casellas, M., Grifoll, M., Bayona, J.M. and Solanas, A.M. New metabolites in the degradation of fluorene by Arthrobacter sp. strain F101. Appl. Environ. Microbiol. 63 (1997) 819-826. [PMID: 9055403]
2. Grifoll, M., CASellas, M., Bayona, J.M. and Solanas, A.M. Isolation and characterization of a fluorene-degrading bacterium: identification of ring oxidation and ring fission products. Appl. Environ. Microbiol. 58 (1992) 2910-2917. [PMID: 1444405]
Accepted name: 4-(hydroxymethyl)benzenesulfonate dehydrogenase
Reaction: 4-(hydroxymethyl)benzenesulfonate + NAD+ = 4-formylbenzenesulfonate + NADH + H+
Systematic name: 4-(hydroxymethyl)benzenesulfonate:NAD+ oxidoreductase
Comments: Involved in the toluene-4-sulfonate degradation pathway in Comamonas testosteroni.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 167973-64-0
References:
1. Junker, F., Saller, E., Schläfli Oppenberg, H.R., Kroneck, P.M., Leisinger, T. and Cook, A.M. Degradative pathways for p-toluenecarboxylate and p-toluenesulfonate and their multicomponent oxygenases in Comamonas testosteroni strains PSB-4 and T-2. Microbiology 142 (1996) 2419-2427. [PMID: 8828208]
Accepted name: 6-hydroxyhexanoate dehydrogenase
Reaction: 6-hydroxyhexanoate + NAD+ = 6-oxohexanoate + NADH + H+
Systematic name: 6-hydroxyhexanoate:NAD+ oxidoreductase
Comments: Involved in the cyclohexanol degradation pathway in Acinetobacter NCIB 9871.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 77000-03-4
References:
1. Donoghue, N.A. and Trudgill, P.W. The metabolism of cyclohexanol by Acinetobacter NCIB 9871. Eur. J. Biochem. 60 (1975) 1-7. [PMID: 1261]
2. Hecker, L.I., Tondeur, Y. and Farrelly, J.G. Formation of ε-hydroxycaproate and ε-aminocaproate from N-nitrosohexamethyleneimine: evidence that microsomal α-hydroxylation of cyclic nitrosamines may not always involve the insertion of molecular oxygen into the substrate. Chem. Biol. Interact. 49 (1984) 235-248. [PMID: 6722936]
Accepted name: 3-hydroxypimeloyl-CoA dehydrogenase
Reaction: 3-hydroxypimeloyl-CoA + NAD+ = 3-oxopimeloyl-CoA + NADH + H+
Glossary entries:
pimelic acid = heptanedioic acid
Systematic name: 3-hydroxypimeloyl-CoA:NAD+ oxidoreductase
Comments: Involved in the anaerobic pathway of benzoate degradation in bacteria.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 1187536-27-1
References:
1. Harwood, C.S. and Gibson, J. Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes? J. Bacteriol. 179 (1997) 301-309. [PMID: 8990279]
Accepted name: sulcatone reductase
Reaction: sulcatol + NAD+ = sulcatone + NADH + H+
Glossary entries:
sulcatone: 6-methylhept-5-en-2-one
sulcatol: 6-methylhept-5-en-2-ol
Systematic name: sulcatol:NAD+ oxidoreductase
Comments: Studies on the effects of growth-stage and nutrient supply on the stereochemistry of sulcatone reduction in Clostridia pasteurianum, C. tyrobutyricum and Lactobacillus brevis suggest that there may be at least two sulcatone reductases with different stereospecificities.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 196522-54-0
References:
1. Belan, A., Botle, J., Fauve, A., Gourcy, J.G. and Veschambre, H. Use of biological systems for the preparation of chiral molecules. 3. An application in pheromone synthesis: Preparation of sulcatol enantiomers. J. Org. Chem. 52 (1987) 256-260.
2. Tidswell, E.C., Salter, G.J., Kell, D.B. and Morris, J.G. Enantioselectivity of sulcatone reduction by some anaerobic bacteria. Enzyme Microb. Technol. 21 (1997) 143-147.
3. Tidswell, E.C., Thompson, A.N. and Morris, J.G. Selection in chemostat culture of a mutant strain of Clostridium tryobutyricum improved in its reduction of ketones. J. Appl. Microbiol. Biotechnol. 35 (1991) 317-322.
Accepted name: sn-glycerol-1-phosphate dehydrogenase
Reaction: sn-glycerol 1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
For diagram of reaction click here.
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): glycerol-1-phosphate dehydrogenase [NAD(P)+]; sn-glycerol-1-phosphate:NAD+ oxidoreductase; G-1-P dehydrogenase; Gro1PDH
Systematic name: sn-glycerol-1-phosphate:NAD(P)+ 2-oxidoreductase
Comments: This Zn2+-dependent metalloenzyme is responsible for the formation of archaea-specific sn-glycerol-1-phosphate, the first step in the biosynthesis of polar lipids in archaea. It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes. The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 (phosphoglycerol geranylgeranyltransferase) and EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase), which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 (CDP-archaeol synthase) to form CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [4]. Activity of the enzyme is stimulated by K+ [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 204594-18-3
References:
1. Nishihara, M. and Koga, Y. sn-Glycerol-1-phosphate dehydrogenase in Methanobacterium thermoautotrophicum: key enzyme in biosynthesis of the enantiomeric glycerophosphate backbone of ether phospholipids of archaebacteria. J. Biochem. 117 (1995) 933-935. [PMID: 8586635]
2. Nishihara, M. and Koga, Y. Purification and properties of sn-glycerol-1-phosphate dehydrogenase from Methanobacterium thermoautotrophicum: characterization of the biosynthetic enzyme for the enantiomeric glycerophosphate backbone of ether polar lipids of Archaea. J. Biochem. 122 (1997) 572-576. [PMID: 9348086]
3. Koga, Y., Kyuragi, T., Nishihara, M. and Sone, N. Did archaeal and bacterial cells arise independently from noncellular precursors? A hypothesis stating that the advent of membrane phospholipid with enantiomeric glycerophosphate backbones caused the separation of the two lines of descent. J. Mol. Evol. 46 (1998) 54-63. [PMID: 9419225]
4. Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568-36574. [PMID: 10960477]
5. Han, J.S. and Ishikawa, K. Active site of Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase from Aeropyrum pernix K1. Archaea 1 (2005) 311-317. [PMID: 15876564]
Accepted name: 4-hydroxythreonine-4-phosphate dehydrogenase
Reaction: 4-phosphooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH + H+
For diagram of reaction click here.
Other name(s): NAD+-dependent threonine 4-phosphate dehydrogenase; L-threonine 4-phosphate dehydrogenase; 4-(phosphohydroxy)-L-threonine dehydrogenase; PdxA; 4-(phosphonooxy)-L-threonine:NAD+ oxidoreductase; 4-phosphooxy-L-threonine:NAD+ oxidoreductase
Systematic name: 4-phosphooxy-L-threonine:NAD+ 3-oxidoreductase (decarboxylating)
Comments: The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5'-phosphate found in anaerobic bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 230310-36-8
References:
1. Cane, D.E., Hsiung, Y., Cornish, J.A., Robinson, J.K and Spenser, I.D. Biosynthesis of vitamine B6: The oxidation of L-threonine 4-phosphate by PdxA. J. Am. Chem. Soc. 120 (1998) 1936-1937.
2. Laber, B., Maurer, W., Scharf, S., Stepusin, K. and Schmidt, F.S. Vitamin B6 biosynthesis: formation of pyridoxine 5'-phosphate from 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by PdxA and PdxJ protein. FEBS Lett. 449 (1999) 45-48. [PMID: 10225425]
3. Sivaraman, J., Li, Y., Banks, J., Cane, D.E., Matte, A. and Cygler, M. Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway. J. Biol. Chem. 278 (2003) 43682-43690. [PMID: 12896974]
4. Banks, J. and Cane, D.E. Biosynthesis of vitamin B6: direct identification of the product of the PdxA-catalyzed oxidation of 4-hydroxy-l-threonine-4-phosphate using electrospray ionization mass spectrometry. Bioorg. Med. Chem. Lett. 14 (2004) 1633-1636. [PMID: 15026039]
Accepted name: 1,5-anhydro-D-fructose reductase
Reaction: 1,5-anhydro-D-glucitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
Systematic name: 1,5-anhydro-D-glucitol:NADP+ oxidoreductase
Comments: Also reduces pyridine-3-aldehyde and 2,3-butanedione. Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are poor substrates, but there is no detectable action on glucose, mannose and fructose.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 206138-19-4
References:
1. Sakuma, M., Kametani, S. and Akanuma, H. Purification and some properties of a hepatic NADPH-dependent reductase that specifically acts on 1,5-anhydro-D-fructose. J. Biochem. (Tokyo) 123 (1998) 189-193.
Accepted name: L-idonate 5-dehydrogenase
Reaction: L-idonate + NAD(P)+ = 5-dehydro-D-gluconate + NAD(P)H + H+
Other name(s): L-idonate 5-dehydrogenase
Systematic name: L-idonate:NAD(P)+ oxidoreductase
Comments: The enzyme from the bacterium Escherichia coli is specific for 5-dehydro-D-gluconate. cf. EC 1.1.1.366, L-idonate 5-dehydrogenase (NAD+).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 211737-68-7
References:
1. Bausch, C., Peekhaus, N., Utz, C., Blais, T., Murray, E., Lowary, T. and Conway, T. Sequence analysis of the GntII (subsidiary) system for gluconate metabolism reveals a novel pathway for L-idonic acid catabolism in Escherichia coli. J. Bacteriol. 180 (1998) 3704-3710. [PMID: 9658018]
Accepted name: 3-methylbutanal reductase
Reaction: 3-methylbutanol + NAD(P)+ = 3-methylbutanal + NAD(P)H + H+
Systematic name: 3-methylbutanol:NAD(P)+ oxidoreductase
Comments: The enzyme purified from Saccharomyces cerevisiae catalyses the reduction of a number of straight-chain and branched aldehydes, as well as some aromatic aldehydes.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 214265-44-8
References:
1. van Iersel, M.F.M., Eppink, M.H.M., van Berkel, W.J.H., Rombouts, F.M. and Abee, T. Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from Saccharomyces cerevisiae. Appl. Environ. Microbiol. 63 (1997) 4079-4082. [PMID: 9327572]
2. Ven Nedervelde, L., Verlinden, V., Philipp, D. and Debourg, A. Purification and characterization of yeast 3-methyl butanal reductases involved in the removal of wort carbonyls during fermentation. Proc. 26th Congr.-Eur. Brew. Conv. (1997) 447-454.
Accepted name: dTDP-4-dehydro-6-deoxyglucose reductase
Reaction: dTDP-α-D-fucopyranose + NAD(P)+ = dTDP-4-dehydro-6-deoxy-α-D-glucose + NAD(P)H + H+
For diagram of reaction click here.
Glossary: dTDP-4-dehydro-6-deoxy-α-D-glucose = dTDP-6-deoxy-α-D-xylo-hexopyranos-4-ulose = thymidine 5'-[3-(6-deoxy-D-xylo-hexopyranosyl-4-ulose) diphosphate]
Other name(s): dTDP-4-keto-6-deoxyglucose reductase; dTDP-D-fucose:NADP+ oxidoreductase; Fcf1; dTDP-6-deoxy-D-xylo-hex-4-ulopyranose reductase
Systematic name: dTDP-α-D-fucopyranose:NAD(P)+ oxidoreductase
Comments: The enzymes from the Gram-negative bacteria Aggregatibacter actinomycetemcomitans and Escherichia coli O52 are involved in activation of fucose for incorporation into capsular polysaccharide O-antigens [1,3]. The enzyme from the Gram-positive bacterium Geobacillus tepidamans is involved in activation of fucose for incorporation into the organism's S-layer [2].The enzyme from Escherichia coli O52 has a higher catalytic efficiency with NADH than with NADPH [3].
Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:
References:
1. Yoshida, Y., Nakano, Y., Nezu, T., Yamashita, Y. and Koga, T. A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose. J. Biol. Chem. 274 (1999) 16933-16939. [PMID: 10358040]
2. Zayni, S., Steiner, K., Pfostl, A., Hofinger, A., Kosma, P., Schaffer, C. and Messner, P. The dTDP-4-dehydro-6-deoxyglucose reductase encoding fcd gene is part of the surface layer glycoprotein glycosylation gene cluster of Geobacillus tepidamans GS5-97T. Glycobiology 17 (2007) 433-443. [PMID: 17202151]
3. Wang, Q., Ding, P., Perepelov, A.V., Xu, Y., Wang, Y., Knirel, Y.A., Wang, L. and Feng, L. Characterization of the dTDP-D-fucofuranose biosynthetic pathway in Escherichia coli O52. Mol. Microbiol. 70 (2008) 1358-1367. [PMID: 19019146]
Accepted name: 1-deoxy-D-xylulose-5-phosphate reductoisomerase
Reaction: 2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
For diagram click here.
Other name(s): DXP-reductoisomerase; 1-deoxy-D-xylulose-5-phosphate isomeroreductase; 2-C-methyl-D-erythritol 4-phosphate (MEP) synthase
Systematic name: 2-C-methyl-D-erythritol-4-phosphate:NADP+ oxidoreductase (isomerizing)
Comments: The enzyme requires Mn2+, Co2+ or Mg2+ for activity, with the first being most effective. The enzyme from several eubacteria, including Escherichia coli, forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here). The mechanism has been shown to be a retroaldol/aldol reaction [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 210756-42-6
References:
1. Takahashi, S., Kuzuyama, T., Watanabe, H. and Seto, H. A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis. Proc. Natl. Acad. Sci. USA 95 (1998) 9879-9884. [PMID: 9707569]
2 Munos, J.W., Pu, X., Mansoorabadi, S.O., Kim, H.J. and Liu, H.W. A secondary kinetic isotope effect study of the 1-deoxy-D-xylulose-5-phosphate reductoisomerase-catalyzed reaction: evidence for a retroaldol-aldol rearrangement. J. Am. Chem. Soc. 131 (2009) 2048-2049. [PMID: 19159292]
Accepted name: 2-(R)-hydroxypropyl-CoM dehydrogenase
Reaction: 2-(R)-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
For diagram click here.
Glossary:
coenzyme M (CoM) = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
Other name(s): 2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase
Systematic name: 2-{[(2R)-2-hydroxypropyl]sulfanyl}ethane-1-sulfonate:NAD+ oxidoreductase
Comments: The enzyme is highly specific for (R)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.269, 2-(S)-hydroxypropyl-CoM dehydrogenase, which is highly specific for the (S)-enantiomer. This enzyme forms component III of a four-component enzyme system {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]} that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 244301-33-5
References:
1. Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96 (1999) 8432-8437. [PMID: 10411892]
Accepted name: 2-(S)-hydroxypropyl-CoM dehydrogenase
Reaction: (2S)-2-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
For diagram click here.
Glossary:
coenzyme M (CoM) = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
Other name(s): 2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase; 2-[2-(S)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase
Systematic name: 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonate:NAD+ oxidoreductase
Comments: The enzyme is highly specific for (2S)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.268, 2-(R)-hydroxypropyl-CoM dehydrogenase, which is highly specific for the (R)-enantiomer. This enzyme forms component IV of a four-component enzyme system {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]} that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 369364-40-9
References:
1. Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96 (1999) 8432-8437. [PMID: 10411892]
Accepted name: 3β-hydroxysteroid 3-dehydrogenase
Reaction: a 3β-hydroxysteroid + NADP+ = a 3-oxosteroid + NADPH + H+
For diagram of reaction, click here
Other name(s): 3-keto-steroid reductase; 3-KSR; HSD17B7 (gene name); ERG27 (gene name)
Systematic name: 3β-hydroxysteroid:NADP+ 3-oxidoreductase
Comments: The enzyme acts on multiple 3β-hydroxysteroids. Participates in the biosynthesis of zemosterol and cholesterol, where it catalyses the reaction in the opposite direction to that shown. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.62, 17β-estradiol 17-dehydrogenase [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 42616-29-5
References:
1. Swindell, A.C. and Gaylor, J.L. Investigation of the component reactions of oxidative sterol demethylation. Formation and metabolism of 3-ketosteroid intermediates. J. Biol. Chem. 243 (1968) 5546-5555. [PMID: 4387005]
2. Billheimer, J.T., Alcorn, M. and Gaylor, J.L. Solubilization and partial purification of a microsomal 3-ketosteroid reductase of cholesterol biosynthesis. Purification and properties of 3β-hydroxysteroid dehydrogenase and Δ5-3-ketosteroid isomerase from bovine corpora lutea. Arch. Biochem. Biophys. 211 (1981) 430-438. [PMID: 6946726]
3. Gachotte, D., Sen, S.E., Eckstein, J., Barbuch, R., Krieger, M., Ray, B.D. and Bard, M. Characterization of the Saccharomyces cerevisiae ERG27 gene encoding the 3-keto reductase involved in C-4 sterol demethylation. Proc. Natl. Acad. Sci. USA 96 (1999) 12655-12660. [PMID: 10535978]
4. Marijanovic, Z., Laubner, D., Moller, G., Gege, C., Husen, B., Adamski, J. and Breitling, R. Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis. Mol. Endocrinol. 17 (2003) 1715-1725. [PMID: 12829805]
Accepted name: GDP-L-fucose synthase
Reaction: GDP-β-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-α-D-mannose + NADPH + H+
For diagram click here.
Other name(s): GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase; GDP-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)
Systematic name: GDP-β-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)
Comments: Both human and Escherichia coli enzymes can use NADH in place of NADPH to a slight extent.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 113756-18-6
References:
1. Chang, S., Duerr, B. and Serif, G. An epimerase-reductase in L-fucose synthesis. J. Biol. Chem. 263 (1988) 1693-1697. [PMID: 3338988]
2. Mattila, P., Räbinä, J, Hortling, S., Jelin, J. and Renkonen, R. Functional expression of Escherichia coli enzymes synthesizing GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces cerevisiae. Glycobiology, 10, (2000) 1041-1047. [PMID: 11030750]
3. Menon, S., Stahl, M., Kumar, R., Xu, G.-Y. and Sullivan, F. Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli. J. Biol. Chem., 274, (1999) 26743-26750. [PMID: 10480878]
4. Somers, W.S., Stahl, M.L. and Sullivan, F.X. GDP-fucose synthetase from Escherichia coli: Structure of a unique member of the short-chain dehydrogenase/reductase family that catalyzes two distinct reactions at the same active site. Structure, 6, (1998) 1601-1612. [PMID: 9862812]
Accepted name: D-2-hydroxyacid dehydrogenase (NADP+)
Reaction: an (R)-2-hydroxycarboxylate + NADP+ = a 2-oxocarboxylate + NADPH + H+
For diagram of reaction click here.
Other name(s): ddh (gene name)
Systematic name: (R)-2-hydroxycarboxylate:NADP+ oxidoreductase
Comments: This enzyme, characterized from the halophilic archaeon Haloferax mediterranei, catalyses a reversible stereospecific reduction of 2-ketocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. The enzyme prefers substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain, and can use NADH with much lower efficiency. cf. EC 1.1.1.345, (D)-2-hydroxyacid dehydrogenase (NAD+).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 81210-65-3
References:
1. Domenech, J. and Ferrer, J. A new D-2-hydroxyacid dehydrogenase with dual coenzyme-specificity from Haloferax mediterranei, sequence analysis and heterologous overexpression. Biochim. Biophys. Acta 1760 (2006) 1667-1674. [PMID: 17049749]
Accepted name: vellosimine dehydrogenase
Reaction: 10-deoxysarpagine + NADP+ = vellosimine + NADPH + H+
For diagram click here.
Systematic name: 10-deoxysarpagine:NADP+ oxidoreductase
Comments: Also acts on related alkaloids with an endo-aldehyde group as vellosimine (same stereochemistry at C-16) but only slight activity with exo-aldehydes. Detected in many cell suspension cultures of plants from the family Apocynaceae.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 86777-26-6
References:
1. Pfitzner, A., Krausch, B. and Stöckigt, J. Characteristics of vellosimine reductase, a specific enzyme involved in the biosynthesis of the Rauwolfia alkaloid sarpagine. Tetrahedron 40 (1984) 1691-1699.
Accepted name: 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)
Reaction: 2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
Other name(s): 2,5-diketo-D-gluconate reductase (ambiguous)
Systematic name: 2-dehydro-D-gluconate:NADP+ 2-oxidoreductase (2-dehydro-D-gluconate-forming)
Comments: The enzyme is involved in the catabolism of 2,5-didehydrogluconate. cf. EC 1.1.1.346, 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 95725-95-4
References:
1. Sonoyama, T., Kageyama, B., Yagi, S. and Mitsushima, K. Biochemical aspects of 2-keto-L-gulonate accumulation from 2,5-diketo-D-gluconate by Corynebacterium sp. and its mutants. Agric Biol Chem. 51 (1987) 3039-3047.
Accepted name: (+)-trans-carveol dehydrogenase
Reaction: (+)-trans-carveol + NAD+ = (+)-(S)-carvone + NADH + H+
For diagram click here.
Other name(s): carveol dehydrogenase
Systematic name: (+)-trans-carveol:NAD+ oxidoreductase
Comments: NADP+ cannot replace NAD+. Forms part of the monoterpenoid biosynthesis pathway in Carum carvi (caraway) seeds.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Bouwmeester, H.J., Gershenzon, J., Konings, M.C.J.M. and Croteau, R. Biosynthesis of the monoterpenes limonene and carvone in the fruit of caraway. I. Demonstration of enzyme activities and their changes with development. Plant Physiol. 117 (1998) 901-912. [PMID: 9662532]
Accepted name: serine 3-dehydrogenase (NADP+)
Reaction: L-serine + NADP+ = 2-aminoacetaldehyde + CO2 + NADPH + H+ (overall reaction)
(1a) L-serine + NADP+ = 2-aminomalonate semialdehyde + NADPH + H+
(1b) 2-aminomalonate semialdehyde = 2-aminoacetaldehyde + CO2 (spontaneous)
Other name(s): serine 3-dehydrogenase
Systematic name: L-serine:NADP+ 3-oxidoreductase
Comments: NAD+ cannot replace NADP+ [cf. EC 1.1.1.387, serine 3-dehydrogenase (NAD+)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9038-55-5
References:
1. Fujisawa, H., Nagata, S., Chowdhury, E.K., Matsumoto, M. and Misono, H. Cloning and sequencing of the serine dehydrogenase gene from Agrobacterium tumefaciens. Biosci. Biotechnol. Biochem. 66 (2002) 1137-1139. [PMID: 12092831]
2. Chowdhury, E.K., Higuchi, K., Nagata, S. and Misono, H. A novel NADP+ dependent serine dehydrogenase from Agrobacterium tumefaciens. Biosci. Biotechnol. Biochem. 61 (1997) 152-157. [PMID: 9028042]
Accepted name: 3β-hydroxy-5β-steroid dehydrogenase
Reaction: 3β-hydroxy-5β-pregnane-20-one + NADP+ = 5β-pregnan-3,20-dione + NADPH + H+
For diagram click here.
Other name(s): 3β-hydroxysteroid 5β-oxidoreductase; 3β-hydroxysteroid 5β-progesterone oxidoreductase
Systematic name: 3β-hydroxy-5β-steroid:NADP+ 3-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 162731-81-9
References:
1. Stuhlemmer, U. and Kreis, W. Cardenolide formation and activity of pregnane-modifying enzymes in cell suspension cultures, shoot cultures and leaves of Digitalis lanata. Plant Physiol. Biochem. 34 (1996) 85-91.
2. Seitz, H.U. and Gaertner, D.E. Enzymes in cardenolide-accumulating shoot cultures of Digitalis purpurea. Plant Cell Tissue Organ. Cult. 38 (1994) 337-344.
3. Lindemann, P. and Luckner, M. Biosynthesis of pregnane derivatives in somatic embryos of Digitalis lanata. Phytochemistry 46 (1997) 507-513.
Accepted name: 3β-hydroxy-5α-steroid dehydrogenase
Reaction: 3β-hydroxy-5α-pregnane-20-one + NADP+ = 5α-pregnan-3,20-dione + NADPH + H+
For diagram click here.
Systematic name: 3β-hydroxy-5α-steroid:NADP+ 3-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 58875-02-8
References:
1. Lindemann, P. and Luckner, M. Biosynthesis of pregnane derivatives in somatic embryos of Digitalis lanata. Phytochemistry 46 (1997) 507-513.
2. Warneck, H.M. and Seitz, H.U. 3β-Hydroxysteroid oxidoreductase in suspension cultures of Digitalis lanata EHRH. Z. Naturforsch. C: Biosci. 45 (1990) 963-972. [PMID: 2291772]
Accepted name: (R)-3-hydroxyacid-ester dehydrogenase
Reaction: ethyl (R)-3-hydroxyhexanoate + NADP+ = ethyl 3-oxohexanoate + NADPH + H+
Other name(s): 3-oxo ester (R)-reductase
Systematic name: ethyl-(R)-3-hydroxyhexanoate:NADP+ 3-oxidoreductase
Comments: Also acts on ethyl (R)-3-oxobutanoate and some other (R)-3-hydroxy acid esters. The (R)- symbol is allotted on the assumption that no substituents change the order of priority from O-3 > C-2 > C-4. A subunit of yeast fatty acid synthase EC 2.3.1.86, fatty-acyl-CoA synthase system. cf. EC 1.1.1.280, (S)-3-hydroxyacid ester dehydrogenase.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number: 114705-02-1
References:
1. Heidlas, J., Engel, K.-H. and Tressl, R. Purification and characterization of two oxidoreductases involved in the enantioselective reduction of 3-oxo, 4-oxo and 5-oxo esters in baker's yeast. Eur. J. Biochem. 172 (1988) 633-639. [PMID: 3280313]
Accepted name: (S)-3-hydroxyacid-ester dehydrogenase
Reaction: ethyl (S)-3-hydroxyhexanoate + NADP+ = ethyl 3-oxohexanoate + NADPH + H+
Other name(s): 3-oxo ester (S)-reductase
Systematic name: ethyl-(S)-3-hydroxyhexanoate:NADP+ 3-oxidoreductase
Comments: Also acts on 4-oxo- and 5-oxo-fatty acids and their esters. cf. EC 1.1.1.279 (R)-3-hydroxyacid-ester dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 114705-03-2
References:
1. Heidlas, J., Engel, K.-H. and Tressl, R. Purification and characterization of two oxidoreductases involved in the enantioselective reduction of 3-oxo, 4-oxo and 5-oxo esters in baker's yeast. Eur. J. Biochem. 172 (1988) 633-639. [PMID: 3280313]
Accepted name: GDP-4-dehydro-6-deoxy-D-mannose reductase
Reaction: GDP-α-D-rhamnose + NAD(P)+ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H+
For diagram click here.
Glossary: GDP-α-D-rhamnose = GDP-6-deoxy-α-D-mannose
GDP-4-dehydro-α-D-rhamnose = GDP-4-dehydro-6-deoxy-α-D-mannose
Other name(s): GDP-4-keto-6-deoxy-D-mannose reductase [ambiguous]; GDP-6-deoxy-D-lyxo-4-hexulose reductase; Rmd; GDP-6-deoxy-D-mannose:NAD(P)+ 4-oxidoreductase (D-rhamnose-forming); GDP-6-deoxy-β-D-mannose:NAD(P)+ 4-oxidoreductase (D-rhamnose-forming)
Systematic name: GDP-α-D-rhamnose:NAD(P)+ 4-oxidoreductase
Comments: This enzyme differs from EC 1.1.1.187, GDP-4-dehydro-D-rhamnose reductase, in that the only product formed is GDP-α-D-rhamnose (GDP-6-deoxy-α-D-mannose). D-Rhamnose is a constituent of lipopolysaccharides of Gram-negative plant and human pathogenic bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kneidinger, B., Graninger, M., Adam, G., Puchberger, M., Kosma, P., Zayni, S. and Messner, P. Identification of two GDP-6-deoxy-D-lyxo-4-hexulose reductases synthesizing GDP-D-rhamnose in Aneurinibacillus thermoaerophilus L420-91T. J. Biol. Chem. 276 (2001) 5577-5583. [PMID: 11096116]
2. Mäki, M., Järvinen, N., Räbinä, J., Roos, C., Maaheimo, H., Mattila, P. and Renkonen, R. Functional expression of Pseudomonas aeruginosa GDP-4-keto-6-deoxy-D-mannose reductase which synthesizes GDP-rhamnose. Eur. J. Biochem. 269 (2002) 593-601. [PMID: 11856318]
Accepted name: quinate/shikimate dehydrogenase [NAD(P)+]
Reaction: (1) L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
(2) shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
For diagram of reaction, click here
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering.
Other name(s): YdiB; quinate/shikimate dehydrogenase (ambiguous)
Systematic name: L-quinate:NAD(P)+ 3-oxidoreductase
Comments: This is the second shikimate dehydrogenase enzyme found in Escherichia coli. It can use both quinate and shikimate as substrates and either NAD+ or NADP+ as acceptor. The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Michel, G., Roszak, A.W., Sauvé, V., Maclean, J., Matte, A., Coggins, J.R., Cygler, M. and Lapthorn, A.J. Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common structural framework for different activities. J. Biol. Chem. 278 (2003) 19463-19472. [PMID: 12637497]
2. Benach, J., Lee, I., Edstrom, W., Kuzin, A.P., Chiang, Y., Acton, T.B., Montelione, G.T. and Hunt, J.F. The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase. J. Biol. Chem. 278 (2003) 19176-19182. [PMID: 12624088]
Accepted name: methylglyoxal reductase (NADPH)
Reaction: (S)-lactaldehyde + NADP+ = methylglyoxal + NADPH + H+
Glossary: methylglyoxal = 2-oxopropanal
Other name(s): lactaldehyde dehydrogenase (NADP+); GRE2 (gene name); methylglyoxal reductase (NADPH-dependent); lactaldehyde:NADP+ oxidoreductase
Systematic name: (S)-lactaldehyde:NADP+ oxidoreductase
Comments: The enzyme from the yeast Saccharomyces cerevisiae catalyses the reduction of a keto group in a number of compounds, forming enantoiopure products. Among the substrates are methylglyoxal (which is reduced to (S)-lactaldehyde) [1,2], 3-methylbutanal [3], hexane-2,5-dione [4] and 3-chloro-1-phenylpropan-1-one [5]. It differs in cosubstrate requirement from EC 1.1.1.78, methylglyoxal reductase (NADH), which is found in mammals.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 78310-66-4
References:
1. Murata, K., Fukuda, Y., Simosaka, M., Watanabe, K., Saikusa, T. and Kimura, A. Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae. Eur. J. Biochem. 151 (1985) 631-636. [PMID: 3896793]
2. Chen, C.N., Porubleva, L., Shearer, G., Svrakic, M., Holden, L.G., Dover, J.L., Johnston, M., Chitnis, P.R. and Kohl, D.H. Associating protein activities with their genes: rapid identification of a gene encoding a methylglyoxal reductase in the yeast Saccharomyces cerevisiae. Yeast 20 (2003) 545-554. [PMID: 12722185]
3. Hauser, M., Horn, P., Tournu, H., Hauser, N.C., Hoheisel, J.D., Brown, A.J. and Dickinson, J.R. A transcriptome analysis of isoamyl alcohol-induced filamentation in yeast reveals a novel role for Gre2p as isovaleraldehyde reductase. FEMS Yeast Res. 7 (2007) 84-92. [PMID: 16999827]
4. Muller, M., Katzberg, M., Bertau, M. and Hummel, W. Highly efficient and stereoselective biosynthesis of (2S,5S)-hexanediol with a dehydrogenase from Saccharomyces cerevisiae. Org. Biomol. Chem. 8 (2010) 1540-1550. [PMID: 20237665]
5. Choi, Y.H., Choi, H.J., Kim, D., Uhm, K.N. and Kim, H.K. Asymmetric synthesis of (S)-3-chloro-1-phenyl-1-propanol using Saccharomyces cerevisiae reductase with high enantioselectivity. Appl. Microbiol. Biotechnol. 87 (2010) 185-193. [PMID: 20111861]
6. Breicha, K., Muller, M., Hummel, W. and Niefind, K. Crystallization and preliminary crystallographic analysis of Gre2p, an NADP(+)-dependent alcohol dehydrogenase from Saccharomyces cerevisiae. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 (2010) 838-841. [PMID: 20606287]
Accepted name: S-(hydroxymethyl)glutathione dehydrogenase
Reaction: S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H + H+
Other name(s): NAD-linked formaldehyde dehydrogenase (incorrect); formaldehyde dehydrogenase (incorrect); formic dehydrogenase (incorrect); class III alcohol dehydrogenase; ADH3; χ-ADH; FDH (incorrect); formaldehyde dehydrogenase (glutathione) (incorrect); GS-FDH (incorrect); glutathione-dependent formaldehyde dehydrogenase (incorrect); GD-FALDH; NAD- and glutathione-dependent formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase (incorrect)
Systematic name: S-(hydroxymethyl)glutathione:NAD+ oxidoreductase
Comments: The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase. This enzyme forms part of the pathway that detoxifies formaldehyde, since the product is hydrolysed by EC 3.1.2.12, S-formylglutathione hydrolase. The human enzyme belongs to the family of zinc-dependent alcohol dehydrogenases. Also specifically reduces S-nitrosylglutathione.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd ed, vol. 7, Academic Press, New York, pp. 203-221.
2. Rose, Z.B. and Racker, E. Formaldehyde dehydrogenase. Methods Enzymol. 9 (1966) 357-360.
3. Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J. and Stamler, J.S. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410 (2001) 490-494. [PMID: 11260719]
4. Sanghani, P.C., Stone, C.L., Ray, B.D., Pindel, E.V., Hurley, T.D. and Bosron, W.F. Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase. Biochemistry 39 (2000) 10720-10729. [PMID: 10978156]
5. van Ophem, P.W. and Duine, J.A. NAD- and co-substrate (GSH or factor)-dependent formaldehyde dehydrogenases from methylotrophic microorganisms act as a class III alcohol dehydrogenase. FEMS Microbiol. Lett. 116 (1994) 87-94.
6. Ras, J., van Ophem, P.W., Reijnders, W.N., Van Spanning, R.J., Duine, J.A., Stouthamer, A.H. and Harms, N. Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth. J. Bacteriol. 177 (1995) 247-251. [PMID: 7798140]
7. Barber, R.D., Rott, M.A. and Donohue, T.J. Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides. J. Bacteriol. 178 (1996) 1386-1393. [PMID: 8631716]
Accepted name: 3"-deamino-3"-oxonicotianamine reductase
Reaction: 2'-deoxymugineic acid + NAD(P)+ = 3"-deamino-3"-oxonicotianamine + NAD(P)H + H+
For diagram click here.
Systematic name: 2'-deoxymugineic acid:NAD(P)+ 3"-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Shojima, S., Nishizawa, N.-K., Fushiya, S., Nozoe, S., Irifune, T. and Mori, S. In vitro biosynthesis of 2'-deoxymugineic acid from L-methionine and nicotianamine. Plant Physiol. 93 (1990) 1497-1503.
Accepted name: isocitrate—homoisocitrate dehydrogenase
Reaction: (1) isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH
(2) (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+
Other name(s): homoisocitrate—isocitrate dehydrogenase; PH1722
Systematic name: isocitrate(homoisocitrate):NAD+ oxidoreductase (decarboxylating)
Comments: Requires Mn2+ and K+ or NH4+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+) and EC 1.1.1.87, homoisocitrate dehydrogenase, this enzyme, from Pyrococcus horikoshii, can use both isocitrate and homoisocitrate as substrates. The enzyme may play a role in both the lysine and glutamate biosynthesis pathways.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Miyazaki, K. Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of β-decarboxylating dehydrogenase. Biochem. Biophys. Res. Commun. 331 (2005) 341-346. [PMID: 15845397]
Accepted name: D-arabinitol dehydrogenase (NADP+)
Reaction: (1) D-arabinitol + NADP+ = D-xylulose + NADPH + H+
(2) D-arabinitol + NADP+ = D-ribulose + NADPH + H+
Other name(s): NADP+-dependent D-arabitol dehydrogenase; ARD1p; D-arabitol dehydrogenase 1
Systematic name: D-arabinitol:NADP+ oxidoreductase
Comments: The enzyme from the rust fungus Uromyces fabae can use D-arabinitol and D-mannitol as substrates in the forward direction and D-xylulose, D-ribulose and, to a lesser extent, D-fructose as substrates in the reverse direction. This enzyme carries out the reactions of both EC 1.1.1.11, D-arabinitol 4-dehydrogenase and EC 1.1.1.250, D-arabinitol 2-dehydrogenase, but unlike them, uses NADP+ rather than NAD+ as cofactor. D-Arabinitol is capable of quenching reactive oxygen species involved in defense reactions of the host plant.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Link, T., Lohaus, G., Heiser, I., Mendgen, K., Hahn, M. and Voegele, R.T. Characterization of a novel NADP+-dependent D-arabitol dehydrogenase from the plant pathogen Uromyces fabae. Biochem. J. 389 (2005) 289-295. [PMID: 15796718]
Accepted name: xanthoxin dehydrogenase
Reaction: xanthoxin + NAD+ = abscisic aldehyde + NADH + H+
For diagram click here (mechanism).
Other name(s): xanthoxin oxidase; ABA2
Systematic name: xanthoxin:NAD+ oxidoreductase
Comments: Requires a molybdenum cofactor for activity. NADP+ cannot replace NAD+ and short-chain alcohols such as ethanol, isopropanol, butanol and cyclohexanol cannot replace xanthoxin as substrate [3]. Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.2.3.14 (abscisic aldehyde oxidase), EC 1.13.11.51 (9-cis-epoxycarotenoid dioxygenase) and EC 1.14.13.93 [(+)-abscisic acid 8'-hydroxylase]. Abscisic acid is a sesquiterpenoid plant hormone that is involved in the control of a wide range of essential physiological processes, including seed development, germination and responses to stress [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 129204-37-1
References:
1. Sindhu, R.K. and Walton, D.C. Xanthoxin metabolism in cell-free preparations from wild type and wilty mutants of tomato. Plant Physiol. 88 (1988) 178-182.
2. Schwartz, S.H., Leon-Kloosterziel, K.M., Koornneef, M. and Zeevaart, J.A. Biochemical characterization of the aba2 and aba3 mutants in Arabidopsis thaliana. Plant Physiol. 114 (1997) 161-166. [PMID: 9159947]
3. González-Guzmán, M., Apostolova, N., Bellés, J.M., Barrero, J.M., Piqueras, P., Ponce, M.R., Micol, J.L., Serrano, R. and Rodríguez, P.L. The short-chain alcohol dehydrogenase ABA2 catalyzes the conversion of xanthoxin to abscisic aldehyde. Plant Cell. 14 (2002) 1833-1846. [PMID: 12172025]
Accepted name: sorbose reductase
Reaction: D-glucitol + NADP+ = L-sorbose + NADPH + H+
For diagram, click here
Glossary: L-sorbose = L-xylo-hex-2-ulose
Other name(s): Sou1p
Systematic name: D-glucitol:NADP+ oxidoreductase
Comments: The reaction occurs predominantly in the reverse direction. This enzyme can also convert D-fructose into D-mannitol, but more slowly. Belongs in the short-chain dehydrogenase family.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 138440-90-1
References:
1. Greenberg, J.R., Price, N.P., Oliver, R.P., Sherman, F. and Rustchenko, E. Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose utilization. Yeast 22 (2005) 957-969. [PMID: 16134116]
2. Sugisawa, T., Hoshino, T. and Fujiwara, A. Purification and properties of NADPH-linked L-sorbose reductase from Gluconobacter melanogenus N44-1. Agric. Biol. Chem. 55 (1991) 2043-2049.
3. Shinjoh, M., Tazoe, M. and Hoshino, T. NADPH-dependent L-sorbose reductase is responsible for L-sorbose assimilation in Luconobacter suboxydans IFO 3291. J. Bacteriol. 184 (2002) 861-863. [PMID: 11790761]
Accepted name: 4-phosphoerythronate dehydrogenase
Reaction: 4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH + H+
For diagram of reaction click here.
Other name(s): PdxB; PdxB 4PE dehydrogenase; 4-O-phosphoerythronate dehydrogenase
Systematic name: 4-phospho-D-erythronate:NAD+ 2-oxidoreductase
Comments: This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid [6]. cf. EC 1.1.1.399, 2-oxoglutarate reductase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 125858-75-5
References:
1. Lam, H.M. and Winkler, M.E. Metabolic relationships between pyridoxine (vitamin B6) and serine biosynthesis in Escherichia coli K-12. J. Bacteriol. 172 (1990) 6518-6528. [PMID: 2121717]
2. Pease, A.J., Roa, B.R., Luo, W. and Winkler, M.E. Positive growth rate-dependent regulation of the pdxA, ksgA, and pdxB genes of Escherichia coli K-12. J. Bacteriol. 184 (2002) 1359-1369. [PMID: 11844765]
3. Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178 (1996) 232-239. [PMID: 8550422]
4. Grant, G.A. A new family of 2-hydroxyacid dehydrogenases. Biochem. Biophys. Res. Commun. 165 (1989) 1371-1374. [PMID: 2692566]
5. Schoenlein, P.V., Roa, B.B. and Winkler, M.E. Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12. J. Bacteriol. 171 (1989) 6084-6092. [PMID: 2681152]
6. Rudolph, J., Kim, J. and Copley, S.D. Multiple turnovers of the nicotino-enzyme PdxB require α-keto acids as cosubstrates. Biochemistry 49 (2010) 9249-9255. [PMID: 20831184]
Accepted name: 2-hydroxymethylglutarate dehydrogenase
Reaction: (S)-2-hydroxymethylglutarate + NAD+ = 2-formylglutarate + NADH + H+
For diagram click here.
Other name(s): HgD
Systematic name: (S)-2-hydroxymethylglutarate:NAD+ oxidoreductase
Comments: NADP+ cannot replace NAD+. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 3.5.2.18 (enamidase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 1073478-76-8
References:
1. Alhapel, A., Darley, D.J., Wagener, N., Eckel, E., Elsner, N. and Pierik, A.J. Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri. Proc. Natl. Acad. Sci. USA 103 (2006) 12341-12346. [PMID: 16894175]
Accepted name: 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
Reaction: 1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
For diagram click here.
Other name(s): 1,5-anhydro-D-fructose reductase (ambiguous); AFR (ambiguous)
Systematic name: 1,5-anhydro-D-mannitol:NADP+ oxidoreductase
Comments: This enzyme is present in some but not all Rhizobium species and belongs in the GFO/IDH/MocA protein family [2]. This enzyme differs from hepatic 1,5-anhydro-D-fructose reductase, which yields 1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263). In Sinorhizobium morelense, the product of the reaction, 1,5-anhydro-D-mannitol, can be further metabolized to D-mannose [1]. The enzyme also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and 2-ketoaldoses (called osones), such as D-glucosone (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone. It does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones [1].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kühn, A., Yu, S. and Giffhorn, F. Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis. Appl. Environ. Microbiol. 72 (2006) 1248-1257. [PMID: 16461673]
2. Dambe, T.R., Kühn, A.M., Brossette, T., Giffhorn, F. and Scheidig, A.J. Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 Å resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis. Biochemistry 45 (2006) 10030-10042. [PMID: 16906761]
[EC 1.1.1.293 Deleted entry: tropinone reductase I. This enzyme was already in the Enzyme List as EC 1.1.1.206, tropine dehydrogenase so EC 1.1.1.293 has been withdrawn at the public-review stage. (EC 1.1.1.293 created 2007, withdrawn while undergoing public review)]
Accepted name: chlorophyll(ide) b reductase
Reaction: 71-hydroxychlorophyllide a + NAD(P)+ = chlorophyllide b + NAD(P)H + H+
For diagram of reaction click here.
Other name(s): chlorophyll b reductase; Chl b reductase
Systematic name: 71-hydroxychlorophyllide-a:NAD(P)+ oxidoreductase
Comments: This enzyme carries out the first step in the conversion of chlorophyll b to chlorophyll a. It is involved in chlorophyll degradation, which occurs during leaf senescence [3] and it also forms part of the chlorophyll cycle, which interconverts chlorophyll a and b in response to changing light conditions [4,5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Scheumann, V., Ito, H., Tanaka, A., Schoch, S. and Rüdiger, W. Substrate specificity of chlorophyll(ide) b reductase in etioplasts of barley (Hordeum vulgare L.). Eur. J. Biochem. 242 (1996) 163-170. [PMID: 8954166]
2. Scheumann, V., Schoch, S. and Rüdiger, W. Chlorophyll a formation in the chlorophyll b reductase reaction requires reduced ferredoxin. J. Biol. Chem. 273 (1998) 35102-35108. [PMID: 9857045]
3. Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55-77. [PMID: 16669755]
4. Ito, H., Ohtsuka, T. and Tanaka, A. Conversion of chlorophyll b to chlorophyll a via 7-hydroxymethyl chlorophyll. J. Biol. Chem. 271 (1996) 1475-1479. [PMID: 8576141]
5. Rüdiger, W. Biosynthesis of chlorophyll b and the chlorophyll cycle. Photosynth. Res. 74 (2002) 187-193. [PMID: 16228557]
Accepted name: momilactone-A synthase
Reaction: 3β-hydroxy-9β-pimara-7,15-diene-19,6β-olide + NAD(P)+ = momilactone A + NAD(P)H + H+
For diagram of reaction, click here
Other name(s): momilactone A synthase; OsMAS
Systematic name: 3β-hydroxy-9β-pimara-7,15-diene-19,6β-olide:NAD(P)+ oxidoreductase
Comments: The rice phytoalexin momilactone A is a diterpenoid secondary metabolite that is involved in the defense mechanism of the plant. Momilactone A is produced in response to attack by a pathogen through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation. The enzyme, which catalyzes the last step in the biosynthesis of momilactone A, can use both NAD+ and NADP+ but activity is higher with NAD+ [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Atawong, A., Hasegawa, M. and Kodama, O. Biosynthesis of rice phytoalexin: enzymatic conversion of 3β-hydroxy-9β-pimara-7,15-dien-19,6β-olide to momilactone A. Biosci. Biotechnol. Biochem. 66 (2002) 566-570. [PMID: 12005050]
2. Shimura, K., Okada, A., Okada, K., Jikumaru, Y., Ko, K.W., Toyomasu, T., Sassa, T., Hasegawa, M., Kodama, O., Shibuya, N., Koga, J., Nojiri, H. and Yamane, H. Identification of a biosynthetic gene cluster in rice for momilactones. J. Biol. Chem. 282 (2007) 34013-34018. [PMID: 17872948]
Accepted name: dihydrocarveol dehydrogenase
Reaction: ment-8-en-2-ol + NAD+ = meth-8-en-2-one + NADH + H+
For diagram of reaction click here.
Glossary: (+)-dihydrocarveol = (1S,2S,4S)-menth-8-en-2-ol
(+)-isodihydrocarveol = (1S,2S,4R)-menth-8-en-2-ol
(+)-neoisodihydrocarveol = (1S,2R,4R)-menth-8-en-2-ol
(–)-dihydrocarvone = (1S,4S)-menth-8-en-2-one
(+)-isodihydrocarvone = (1S,4R)-menth-8-en-2-one
Other name(s): carveol dehydrogenase
Systematic name: menth-8-en-2-ol:NAD+ oxidoreductase
Comments: This enzyme from the the Gram-positive bacterium Rhodococcus erythropolis DCL14 forms part of the carveol and dihydrocarveol degradation pathway. The enzyme accepts all eight stereoisomers of menth-8-en-2-ol as substrate, although some isomers are converted faster than others. The preferred substrates are (+)-neoisodihydrocarveol, (+)-isodihydrocarveol, (+)-dihydrocarveol and (–)-isodihydrocarveol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129-1141. [PMID: 10832640]
Accepted name: limonene-1,2-diol dehydrogenase
Reaction: menth-8-ene-1,2-diol + NAD+ = 1-hydroxymenth-8-en-2-one + NADH + H+ (general reaction)
(1) (1S,2S,4R)-menth-8-ene-1,2-diol + NAD+ = (1S,4R)-1-hydroxymenth-8-en-2-one + NADH + H+
(2) (1R,2R,4S)-menth-8-ene-1,2-diol + NAD+ = (1R,4S)-1-hydroxymenth-8-en-2-one + NADH + H+
For diagram of reaction click here.
Glossary: limonene-1,2-diol = menth-8-ene-1,2-diol = 1-methyl-4-(prop-1-en-2-yl)cyclohexane-1,2-diol
Other name(s): NAD+-dependent limonene-1,2-diol dehydrogenase
Systematic name: menth-8-ene-1,2-diol:NADP+ oxidoreductase
Comments: While the enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 can use both (1S,2S,4R)- and (1R,2R,4S)-menth-8-ene-1,2-diol as substrate, activity is higher with (1S,2S,4R)-menth-8-ene-1,2-diol as substrate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. van der Werf, M.J., Swarts, H.J. and de Bont, J.A. Rhodococcus erythropolis DCL14 contains a novel degradation pathway for limonene. Appl. Environ. Microbiol. 65 (1999) 2092-2102. [PMID: 10224006]
Accepted name: 3-hydroxypropionate dehydrogenase (NADP+)
Reaction: 3-hydroxypropanoate + NADP+ = malonate semialdehyde + NADPH + H+
For diagram of reaction click here (another example), another example).
Systematic name: 3-hydroxypropanoate:NADP+ oxidoreductase
Comments: Catalyses the reduction of malonate semialdehyde to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively [1,2]. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the upstream reaction in the pathway, EC 1.2.1.75 [3]. Different from EC 1.1.1.59 [3-hydroxypropionate dehydrogenase (NAD+)] by cofactor preference.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Strauss, G. and Fuchs, G. Enzymes of a novel autotrophic CO2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle. Eur. J. Biochem. 215 (1993) 633-643. [PMID: 8354269]
2. Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782-1786. [PMID: 18079405]
3. Hugler, M., Menendez, C., Schagger, H. and Fuchs, G. Malonyl-coenzyme A reductase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO2 fixation. J. Bacteriol. 184 (2002) 2404-2410. [PMID: 11948153]
Accepted name: malate dehydrogenase [NAD(P)+]
Reaction: (S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
Other name(s): MdH II, NAD(P)+-dependent malate dehyrogenase
Systematic name: (S)-malate:NAD(P)+ oxidoreductase
Comments: This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity [1]. Different from EC 1.1.1.37 [malate dehydrogenase (NAD+)], EC 1.1.1.82 [malate dehydrogenase (NADP+)] and EC 1.1.5.4 [malate dehydrogenase (quinone)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Thompson, H., Tersteegen, A., Thauer, R.K. and Hedderich, R. Two malate dehydrogenases in Methanobacterium thermoautotrophicum. Arch. Microbiol. 170 (1998) 38-42. [PMID: 9639601]
Accepted name: NADP-retinol dehydrogenase
Reaction: retinol + NADP+ = retinal + NADPH + H+
Other name(s): all-trans retinal reductase (ambiguous); all-trans-retinol dehydrogenase; NADP(H)-dependent retinol dehydrogenase/reductase; RDH11; RDH12; RDH13; RDH14; retinol dehydrogenase 12; retinol dehydrogenase 14; retinol dehydrogenase [NADP+]; RalR1; PSDR1
Systematic name: retinol:NADP+ oxidoreductase
Comments: Greater catalytic efficiency in the reductive direction. This observation, and the enzyme's localization at the entrance to the mitochondrial matrix, suggest that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinal produced from dietary β-carotene by EC 1.13.11.63 (β-carotene 15,15'-monooxygenase) [2]. Km-values for NADP+ and NADPH are at least 800-fold lower than those for NAD+ and NADH [1,4]. This enzyme differs from EC 1.1.1.105, retinol dehydrogenase, which prefers NAD+ and NADH. This enzyme is distinct from EC 1.1.1.71, alcohol dehydrogenase (NAD(P)+), which shows a broad specificity for aldehydes.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Belyaeva, O.V., Korkina, O.V., Stetsenko, A.V., Kim, T., Nelson, P.S. and Kedishvili, N.Y. Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids. Biochemistry 44 (2005) 7035-7047. [PMID: 15865448]
2. Belyaeva, O.V., Korkina, O.V., Stetsenko, A.V. and Kedishvili, N.Y. Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity. FEBS J. 275 (2008) 138-147. [PMID: 18039331]
3. Haeseleer, F., Huang, J., Lebioda, L., Saari, J.C. and Palczewski, K. Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal. J. Biol. Chem. 273 (1998) 21790-21799. [PMID: 9705317]
4. Kedishvili, N.Y., Chumakova, O.V., Chetyrkin, S.V., Belyaeva, O.V., Lapshina, E.A., Lin, D.W., Matsumura, M. and Nelson, P.S. Evidence that the human gene for prostate short-chain dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase (RalR1). J. Biol. Chem. 277 (2002) 28909-28915. [PMID: 12036956]