EC |
1.1.1.151 |
Accepted name: |
21-hydroxysteroid dehydrogenase (NADP+) |
Reaction: |
pregnan-21-ol + NADP+ = pregnan-21-al + NADPH + H+ |
Other name(s): |
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) |
Systematic name: |
21-hydroxysteroid:NADP+ 21-oxidoreductase |
Comments: |
Acts on a number of 21-hydroxycorticosteroids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-76-3 |
References: |
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. [PMID: 14253469] |
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[EC 1.1.1.151 created 1972] |
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EC |
1.1.1.152 |
Accepted name: |
3α-hydroxy-5β-androstane-17-one 3α-dehydrogenase |
Reaction: |
3α-hydroxy-5β-androstane-17-one + NAD+ = 5β-androstane-3,17-dione + NADH + H+ |
Other name(s): |
etiocholanolone 3α-dehydrogenase; etiocholanolone 3α-dehydrogenase; 3α-hydroxy-5β-steroid dehydrogenase |
Systematic name: |
3α-hydroxy-5β-steroid:NAD+ 3-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-77-4 |
References: |
1. |
Roe, C.R. and Kaplan, N.O. Purification and substrate specificities of bacterial hydroxysteroid dehydrogenases. Biochemistry 8 (1969) 5093–5103. [PMID: 5365796] |
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[EC 1.1.1.152 created 1972] |
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EC |
1.1.1.153 |
Accepted name: |
sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) |
Reaction: |
(1) L-erythro-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+ (2) L-erythro-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+ |
|
For diagram of biopterin biosynthesis, click here |
Glossary: |
sepiapterin = 2-amino-6-lactoyl-7,8-dihydropteridin-4(3H)-one
tetrahydrobiopterin = 5,6,7,8-tetrahydrobiopterin = 2-amino-6-(1,2-dihydroxypropyl)-5,6,7,8-tetrahydropteridin-4(3H)-one |
Other name(s): |
SR |
Systematic name: |
L-erythro-7,8-dihydrobiopterin:NADP+ oxidoreductase |
Comments: |
This enzyme catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP. The enzyme, which is found in higher animals and some fungi and bacteria, produces the erythro form of tetrahydrobiopterin. cf. EC 1.1.1.325, sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9059-48-7 |
References: |
1. |
Katoh, S. Sepiapterin reductase from horse liver: purification and properties of the enzyme. Arch. Biochem. Biophys. 146 (1971) 202–214. [DOI] [PMID: 4401291] |
2. |
Matsubara, M., Katoh, S., Akino, M. and Kaufman, S. Sepiapterin reductase. Biochim. Biophys. Acta 122 (1966) 202–212. [PMID: 5969298] |
3. |
Werner, E.R., Schmid, M., Werner-Felmayer, G., Mayer, B. and Wachter, H. Synthesis and characterization of 3H-labelled tetrahydrobiopterin. Biochem. J. 304 (1994) 189–193. [PMID: 7528005] |
4. |
Kim, Y.A., Chung, H.J., Kim, Y.J., Choi, Y.K., Hwang, Y.K., Lee, S.W. and Park, Y.S. Characterization of recombinant Dictyostelium discoideum sepiapterin reductase expressed in E. coli. Mol. Cells 10 (2000) 405–410. [PMID: 10987137] |
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[EC 1.1.1.153 created 1972, modified 2012] |
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EC |
1.1.1.154 |
Accepted name: |
ureidoglycolate dehydrogenase |
Reaction: |
(S)-ureidoglycolate + NAD(P)+ = oxalureate + NAD(P)H + H+ |
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For diagram of AMP catabolism, click here |
Systematic name: |
(S)-ureidoglycolate:NAD(P)+ oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-62-1 |
References: |
1. |
van der Drift, C., van Helvoort, P.E. and Vogels, G.D. S-Ureidoglycolate dehydrogenase: purification and properties. Arch. Biochem. Biophys. 145 (1971) 465–469. [DOI] [PMID: 4399430] |
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[EC 1.1.1.154 created 1976] |
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EC
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1.1.1.155
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Deleted entry: | homoisocitrate dehydrogenase. The enzyme is identical to EC 1.1.1.87, homoisocitrate dehydrogenase |
[EC 1.1.1.155 created 1976, deleted 2004] |
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EC |
1.1.1.156 |
Accepted name: |
glycerol 2-dehydrogenase (NADP+) |
Reaction: |
glycerol + NADP+ = glycerone + NADPH + H+ |
Other name(s): |
dihydroxyacetone reductase; dihydroxyacetone (reduced nicotinamide adenine dinucleotide phosphate) reductase; dihydroxyacetone reductase (NADPH); DHA oxidoreductase; glycerol 2-dehydrogenase (NADP) |
Systematic name: |
glycerol:NADP+ 2-oxidoreductase (glycerone-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39342-20-6 |
References: |
1. |
Ben-Amotz, A. and Avron, M. NADP specific dihydroxyacetone reductase from Dunaliella parva. FEBS Lett. 29 (1973) 153–155. [DOI] [PMID: 4146296] |
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[EC 1.1.1.156 created 1976] |
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EC |
1.1.1.157 |
Accepted name: |
3-hydroxybutyryl-CoA dehydrogenase |
Reaction: |
(S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+ |
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For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here |
Other name(s): |
β-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; β-hydroxybutyryl-CoA dehydrogenase |
Systematic name: |
(S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39319-78-3 |
References: |
1. |
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. [DOI] [PMID: 4405720] |
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[EC 1.1.1.157 created 1976] |
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EC
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1.1.1.158
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Transferred entry: | UDP-N-acetylmuramate dehydrogenase. Now EC 1.3.1.98, UDP-N-acetylmuramate dehydrogenase
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[EC 1.1.1.158 created 1976, modified 1983, modified 2002, deleted 2013] |
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EC |
1.1.1.159 |
Accepted name: |
7α-hydroxysteroid dehydrogenase |
Reaction: |
cholate + NAD+ = 3α,12α-dihydroxy-7-oxo-5β-cholan-24-oate + NADH + H+ |
Glossary: |
cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate |
Other name(s): |
7α-hydroxy steroid dehydrogenase; 7α-HSDH |
Systematic name: |
7α-hydroxysteroid:NAD+ 7-oxidoreductase |
Comments: |
Catalyses the oxidation of the 7α-hydroxy group of bile acids and alcohols both in their free and conjugated forms. The Bacteroides fragilis and Clostridium enzymes can also utilize NADP+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39361-64-3 |
References: |
1. |
Haslewood, E.S. and Haslewood, G.A.D. The specificity of a 7α-hydroxy steroid dehydrogenase from Escherichia coli. Biochem. J. 157 (1976) 207–210. [PMID: 786279] |
2. |
Macdonald, I.A. and Roach, P.D. Bile induction of 7α- and 7β-hydroxysteroid dehydrogenases in Clostridium absonum. Biochim. Biophys. Acta 665 (1981) 262–269. [DOI] [PMID: 6945134] |
3. |
Macdonald, I.A., Williams, C.N. and Mahony, D.E. 7α-Hydroxysteroid dehydrogenase from Escherichia coli B: preliminary studies. Biochim. Biophys. Acta 309 (1973) 243–253. [DOI] [PMID: 4581498] |
4. |
Macdonald, I.A., Williams, C.N., Mahony, D.E. and Christie, W.M. NAD- and NADP-dependent 7α-hydroxysteroid dehydrogenases from Bacteroides fragilis. Biochim. Biophys. Acta 384 (1975) 12–24. [DOI] [PMID: 236764] |
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[EC 1.1.1.159 created 1976, modified 1980] |
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EC |
1.1.1.160 |
Accepted name: |
dihydrobunolol dehydrogenase |
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+ |
Other name(s): |
bunolol reductase |
Systematic name: |
(±)-5-[(tert-butylamino)-2′-hydroxypropoxy]-1,2,3,4-tetrahydro-1-naphthol:NADP+ oxidoreductase |
Comments: |
Also acts, more slowly, with NAD+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-61-0 |
References: |
1. |
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. [PMID: 4560367] |
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[EC 1.1.1.160 created 1976] |
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EC
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1.1.1.161
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Deleted entry: | cholestanetetraol 26-dehydrogenase. The activity is part of EC 1.14.13.15, cholestanetriol 26-monooxygenase |
[EC 1.1.1.161 created 1976, deleted 2012] |
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EC |
1.1.1.162 |
Accepted name: |
erythrulose reductase |
Reaction: |
D-threitol + NADP+ = D-erythrulose + NADPH + H+ |
Other name(s): |
D-erythrulose reductase; erythritol:NADP+ oxidoreductase |
Systematic name: |
D-threitol:NADP+ oxidoreductase |
Comments: |
NAD+ is also utilized, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52064-49-0 |
References: |
1. |
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. [PMID: 4152124] |
2. |
Uehara, K. and Hosomi, S. D-Erythrulose reductase from beef liver. Methods Enzymol. 89 (1982) 232–237. [PMID: 6292658] |
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[EC 1.1.1.162 created 1976] |
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EC |
1.1.1.163 |
Accepted name: |
cyclopentanol dehydrogenase |
Reaction: |
cyclopentanol + NAD+ = cyclopentanone + NADH + H+ |
Systematic name: |
cyclopentanol:NAD+ oxidoreductase |
Comments: |
4-Methylcyclohexanol and cyclohexanol can also act as substrates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37364-12-8 |
References: |
1. |
Griffin, M. and Trudgill, P.W. The metabolism of cyclopentanol by Pseudomonas N.C.I.B. 9872. Biochem. J. 129 (1972) 595–603. [PMID: 4349113] |
2. |
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. [DOI] [PMID: 12406764] |
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[EC 1.1.1.163 created 1976] |
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EC |
1.1.1.164 |
Accepted name: |
hexadecanol dehydrogenase |
Reaction: |
hexadecanol + NAD+ = hexadecanal + NADH + H+ |
Systematic name: |
hexadecanol:NAD+ oxidoreductase |
Comments: |
The liver enzyme acts on long-chain alcohols from C8 to C16. The Euglena enzyme also oxidizes the corresponding aldehydes to fatty acids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-59-6 |
References: |
1. |
Kolattukuday, P.E. Reduction of fatty acids to alcohols by cell-free preparations of Euglena gracilis. Biochemistry 9 (1970) 1095–1102. [PMID: 4313936] |
2. |
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. [PMID: 5432753] |
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[EC 1.1.1.164 created 1976] |
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EC |
1.1.1.165 |
Accepted name: |
2-alkyn-1-ol dehydrogenase |
Reaction: |
2-butyne-1,4-diol + NAD+ = 4-hydroxy-2-butynal + NADH + H+ |
Systematic name: |
2-butyne-1,4-diol:NAD+ 1-oxidoreductase |
Comments: |
Acts on a variety of 2-alkyn-1-ols, and also on 1,4-butanediol. NADP+ also acts as acceptor, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 54576-94-2 |
References: |
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. |
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[EC 1.1.1.165 created 1976] |
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EC |
1.1.1.166 |
Accepted name: |
hydroxycyclohexanecarboxylate dehydrogenase |
Reaction: |
(1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate + NAD+ = (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate + NADH + H+ |
Other name(s): |
dihydroxycyclohexanecarboxylate dehydrogenase; (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate-NAD+ oxidoreductase |
Systematic name: |
(1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate:NAD+ 3-oxidoreductase |
Comments: |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 55467-53-3 |
References: |
1. |
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. [PMID: 4375976] |
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[EC 1.1.1.166 created 1976] |
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EC |
1.1.1.167 |
Accepted name: |
hydroxymalonate dehydrogenase |
Reaction: |
hydroxymalonate + NAD+ = oxomalonate + NADH + H+ |
Systematic name: |
hydroxymalonate:NAD+ oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 58693-60-0 |
References: |
1. |
Jukova, N.I., Klunova, S.M. and Philippovich, Y.B. Biochemistry of Insects, issue 17. , V.I. Lenin State Pedagogical Institute, Moscow, 1971, p. 56. |
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[EC 1.1.1.167 created 1976] |
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EC |
1.1.1.168 |
Accepted name: |
2-dehydropantolactone reductase (Re-specific) |
Reaction: |
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+ |
Other name(s): |
2-oxopantoyl lactone reductase; ketopantoyl lactone reductase; 2-ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (A-specific); (R)-pantolactone:NADP+ oxidoreductase (A-specific); 2-dehydropantolactone reductase (A-specific) |
Systematic name: |
(R)-pantolactone:NADP+ oxidoreductase (Re-specific) |
Comments: |
The yeast enzyme differs from that from Escherichia coli [EC 1.1.1.214 2-dehydropantolactone reductase (Si-specific)], which is specific for the Si-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37211-75-9 |
References: |
1. |
King, H.L., Jr., Dyar, R.E. 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. [PMID: 4603075] |
2. |
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. [PMID: 234966] |
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[EC 1.1.1.168 created 1976, modified 1986, modified 1999] |
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EC |
1.1.1.169 |
Accepted name: |
2-dehydropantoate 2-reductase |
Reaction: |
(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH + H+ |
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For diagram of the early stages of CoA biosynthesis, click here |
Glossary: |
pantoate = 2,4-dihydroxy-3,3-dimethylbutanoate |
Other name(s): |
2-oxopantoate reductase; 2-ketopantoate reductase; 2-ketopantoic acid reductase; ketopantoate reductase; ketopantoic acid reductase |
Systematic name: |
(R)-pantoate:NADP+ 2-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37211-74-8 |
References: |
1. |
King, H.L., Jr., Dyar, R.E. 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. [PMID: 4603075] |
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[EC 1.1.1.169 created 1976] |
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EC |
1.1.1.170 |
Accepted name: |
3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating) |
Reaction: |
a 3β-hydroxysteroid-4α-carboxylate + NAD(P)+ = a 3-oxosteroid + CO2 + NAD(P)H |
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For diagram of sterol ring A modification, click here |
Other name(s): |
3β-hydroxy-4β-methylcholestenecarboxylate 3-dehydrogenase (decarboxylating); 3β-hydroxy-4β-methylcholestenoate dehydrogenase; sterol 4α-carboxylic decarboxylase; sterol-4α-carboxylate 3-dehydrogenase (decarboxylating) (ambiguous); ERG26 (gene name); NSDHL (gene name) |
Systematic name: |
3β-hydroxysteroid-4α-carboxylate:NAD(P)+ 3-oxidoreductase (decarboxylating) |
Comments: |
The enzyme participates in the biosynthesis of several important sterols such as ergosterol and cholesterol. It is part of a three enzyme system that removes methyl groups from the C-4 position of steroid molecules. The first enzyme, EC 1.14.18.9, 4α-methylsterol monooxygenase, catalyses three successive oxidations of the methyl group, resulting in a carboxyl group; the second enzyme, EC 1.1.1.170, catalyses an oxidative decarboxylation that results in a reduction of the 3β-hydroxy group at the C-3 carbon to an oxo group; and the last enzyme, EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase, reduces the 3-oxo group back to a 3β-hydroxyl. If a second methyl group remains at the C-4 position, this enzyme also catalyses its epimerization from 4β to 4α orientation, so it could serve as a substrate for a second round of demethylation. cf. EC 1.1.1.418, plant 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 71822-23-6 |
References: |
1. |
Sharpless, K.B., Snyder, T.E., Spencer, T.A., Maheshwari, K.K. and Nelson, J.A. Biological demethylation of 4,4-dimethyl sterols, Evidence for enzymic epimerization of the 4β-methyl group prior to its oxidative removal. J. Am. Chem. Soc. 91 (1969) 3394–3396. [PMID: 5791927] |
2. |
Rahimtula, A.D. and Gaylor, J.L. Partial purification of a microsomal sterol 4α-carboxylic acid decarboxylase. J. Biol. Chem. 247 (1972) 9–15. [PMID: 4401584] |
3. |
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. [PMID: 7430141] |
4. |
Gachotte, D., Barbuch, R., Gaylor, J., Nickel, E. and Bard, M. Characterization of the Saccharomyces cerevisiae ERG26 gene encoding the C-3 sterol dehydrogenase (C-4 decarboxylase) involved in sterol biosynthesis. Proc. Natl. Acad. Sci. USA 95 (1998) 13794–13799. [DOI] [PMID: 9811880] |
5. |
Caldas, H. and Herman, G.E. NSDHL, an enzyme involved in cholesterol biosynthesis, traffics through the Golgi and accumulates on ER membranes and on the surface of lipid droplets. Hum. Mol. Genet. 12 (2003) 2981–2991. [DOI] [PMID: 14506130] |
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[EC 1.1.1.170 created 1978, modified 2002, modified 2012, modified 2019] |
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EC
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1.1.1.171
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Transferred entry: | methylenetetrahydrofolate reductase (NADPH). Now EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H]
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[EC 1.1.1.171 created 1978, deleted 1984] |
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EC |
1.1.1.172 |
Accepted name: |
2-oxoadipate reductase |
Reaction: |
2-hydroxyadipate + NAD+ = 2-oxoadipate + NADH + H+ |
Other name(s): |
2-ketoadipate reductase; α-ketoadipate reductase; 2-ketoadipate reductase |
Systematic name: |
2-hydroxyadipate:NAD+ 2-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 61116-21-0 |
References: |
1. |
Suda, T., Robinson, J.C. and Fjellstedt, T.A. Purification and properties of α-ketoadipate reductase, a newly discovered enzyme from human placenta. Arch. Biochem. Biophys. 176 (1976) 610–620. [DOI] [PMID: 185965] |
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[EC 1.1.1.172 created 1978] |
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EC |
1.1.1.173 |
Accepted name: |
L-rhamnose 1-dehydrogenase |
Reaction: |
L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+ |
|
For diagram of L-Rhamnose metabolism, click here |
Systematic name: |
L-rhamnofuranose:NAD+ 1-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52227-67-5 |
References: |
1. |
Rigo, L.U., Maréchal, 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. |
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. [DOI] [PMID: 8142] |
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[EC 1.1.1.173 created 1978] |
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EC |
1.1.1.174 |
Accepted name: |
cyclohexane-1,2-diol dehydrogenase |
Reaction: |
trans-cyclohexane-1,2-diol + NAD+ = 2-hydroxycyclohexan-1-one + NADH + H+ |
Systematic name: |
trans-cyclohexane-1,2-diol:NAD+ 1-oxidoreductase |
Comments: |
Also oxidizes, more slowly, the cis isomer and 2-hydroxycyclohexanone. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62628-27-7 |
References: |
1. |
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. [DOI] [PMID: 856571] |
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[EC 1.1.1.174 created 1978] |
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|
EC |
1.1.1.175 |
Accepted name: |
D-xylose 1-dehydrogenase |
Reaction: |
D-xylose + NAD+ = D-xylonolactone + NADH + H+ |
Other name(s): |
NAD-D-xylose dehydrogenase; D-xylose dehydrogenase; (NAD)-linked D-xylose dehydrogenase |
Systematic name: |
D-xylose:NAD+ 1-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62931-20-8 |
References: |
1. |
Yamanaka, K., Gino, M. and Kaneda, R. A specific NAD-D-xylose dehydrogenase from Arthrobacter sp. Agric. Biol. Chem. 41 (1977) 1493–1499. |
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[EC 1.1.1.175 created 1978] |
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EC |
1.1.1.176 |
Accepted name: |
12α-hydroxysteroid dehydrogenase |
Reaction: |
cholate + NADP+ = 3α,7α-dihydroxy-12-oxo-5β-cholan-24-oate + NADPH + H+ |
Glossary: |
cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate
|
Other name(s): |
12α-hydroxy steroid dehydrogenase; NAD+-dependent 12α-hydroxysteroid dehydrogenase; NADP+-12α-hydroxysteroid dehydrogenase |
Systematic name: |
12α-hydroxysteroid:NADP+ 12-oxidoreductase |
Comments: |
Catalyses the oxidation of the 12α-hydroxy group of bile acids, both in their free and conjugated form. Also acts on bile alcohols. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 61642-40-8 |
References: |
1. |
Macdonald, I.A., Mahony, D.E., Jellett, J.F. and Meier, C.E. NAD-dependent 3α- and 12α-hydroxysteroid dehydrogenase activities from Eubacterium lentum ATCC no. 25559. Biochim. Biophys. Acta 489 (1977) 466–476. [DOI] [PMID: 201289] |
2. |
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. [PMID: 921266] |
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[EC 1.1.1.176 created 1978] |
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EC |
1.1.1.177 |
Accepted name: |
glycerol-3-phosphate 1-dehydrogenase (NADP+) |
Reaction: |
sn-glycerol 3-phosphate + NADP+ = D-glyceraldehyde 3-phosphate + NADPH + H+ |
Other name(s): |
glycerol phosphate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; L-glycerol 3-phosphate:NADP+ oxidoreductase; glycerin-3-phosphate dehydrogenase; NADPH-dependent glycerin-3-phosphate dehydrogenase; NADP-specific glycerol 3-phosphate 1-dehydrogenase |
Systematic name: |
sn-glycerol-3-phosphate:NADP+ 1-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37213-46-0 |
References: |
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. Biokhimiya 41 (1976) 1788–1790. [PMID: 1024580] (in Russian) |
2. |
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. [PMID: 4152128] |
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[EC 1.1.1.177 created 1980, modified 1980] |
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EC |
1.1.1.178 |
Accepted name: |
3-hydroxy-2-methylbutyryl-CoA dehydrogenase |
Reaction: |
(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH + H+ |
Other name(s): |
2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase; 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase; 2-methyl-3-hydroxy-butyryl CoA dehydrogenase |
Systematic name: |
(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA:NAD+ oxidoreductase |
Comments: |
Also acts, more slowly, on (2S,3S)-2-hydroxy-3-methylpentanoyl-CoA. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52227-66-4 |
References: |
1. |
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. [PMID: 4150713] |
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[EC 1.1.1.178 created 1981] |
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EC |
1.1.1.179 |
Accepted name: |
D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming) |
Reaction: |
D-xylose + NADP+ = D-xylono-1,5-lactone + NADPH + H+ |
Other name(s): |
D-xylose (nicotinamide adenine dinucleotide phosphate) dehydrogenase (ambiguous); D-xylose-NADP dehydrogenase (ambiguous); D-xylose:NADP+ oxidoreductase (ambiguous); D-xylose 1-dehydrogenase (NADP) (ambiguous) |
Systematic name: |
D-xylose:NADP+ 1-oxidoreductase (D-xylono-1,5-lactone-forming) |
Comments: |
The enzyme, characterized from pig arterial vessels and eye lens, also acts, more slowly, on L-arabinose and D-ribose. cf. EC 1.1.1.424, D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83534-37-6 |
References: |
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. |
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[EC 1.1.1.179 created 1982, modified 2020] |
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EC
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1.1.1.180
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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] |
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EC |
1.1.1.181 |
Accepted name: |
cholest-5-ene-3β,7α-diol 3β-dehydrogenase |
Reaction: |
cholest-5-ene-3β,7α-diol + NAD+ = 7α-hydroxycholest-4-en-3-one + NADH + H+ |
|
For diagram of cholesterol catabolism (rings A, B and C), click here |
Other name(s): |
3β-hydroxy-Δ5-C27-steroid oxidoreductase (ambiguous) |
Systematic name: |
cholest-5-ene-3β,7α-diol:NAD+ 3-oxidoreductase |
Comments: |
Highly specific for 3β,7α-dihydroxy-C27-steroids with Δ5-double bond. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 56626-16-5 |
References: |
1. |
Wikvall, K. Purification and properties of a 3β-hydroxy-Δ5-C27-steroid oxidoreductase from rabbit liver microsomes. J. Biol. Chem. 256 (1981) 3376–3380. [PMID: 6937465] |
2. |
Schwarz, M., Wright, A.C., Davis, D.L., Nazer, H., Bjorkhem, I. and Russell, D.W. The bile acid synthetic gene 3β-hydroxy-Δ5-C27-steroid oxidoreductase is mutated in progressive intrahepatic cholestasis. J. Clin. Invest. 106 (2000) 1175–1184. [PMID: 11067870] |
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[EC 1.1.1.181 created 1983] |
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EC
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1.1.1.182
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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] |
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EC |
1.1.1.183 |
Accepted name: |
geraniol dehydrogenase (NADP+) |
Reaction: |
geraniol + NADP+ = geranial + NADPH + H+ |
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For diagram of acyclic monoterpenoid biosynthesis, click here |
Systematic name: |
geraniol:NADP+ oxidoreductase |
Comments: |
Also acts, more slowly on farnesol but not on nerol. The enzyme produces a mixture known as citral, which includes geranial and neral. It is still not known whether neral is produced directly by the enzyme, or by isomerization of geranial. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 56802-96-1 |
References: |
1. |
Potty, V.H. and Bruemmer, J.H. Oxidation of geraniol by an enzyme system from orange. Phytochemistry 9 (1970) 1001–1007. |
2. |
Sekiwa-Iijima, Y., Aizawa, Y. and Kubota, K. Geraniol dehydrogenase activity related to aroma formation in ginger (Zingiber officinale Roscoe). J. Agric. Food Chem. 49 (2001) 5902–5906. [DOI] [PMID: 11743782] |
3. |
Saito, Y., Ito, S., Koltunow, A.M. and Sakai, H. Crystallization and preliminary X-ray analysis of geraniol dehydrogenase from Backhousia citriodora (lemon myrtle). Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 665–667. [DOI] [PMID: 21636906] |
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[EC 1.1.1.183 created 1983] |
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EC |
1.1.1.184 |
Accepted name: |
carbonyl reductase (NADPH) |
Reaction: |
R-CHOH-R′ + NADP+ = R-CO-R′ + NADPH + H+ |
Other name(s): |
aldehyde reductase 1; prostaglandin 9-ketoreductase; xenobiotic ketone reductase; NADPH-dependent carbonyl reductase; ALR3; carbonyl reductase; nonspecific NADPH-dependent carbonyl reductase; carbonyl reductase (NADPH2) |
Systematic name: |
secondary-alcohol:NADP+ oxidoreductase |
Comments: |
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. Si-specific with respect to NADPH [cf. EC 1.1.1.2 alcohol dehydrogenase (NADP+)]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 89700-36-7 |
References: |
1. |
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. [DOI] [PMID: 31888] |
2. |
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. [DOI] [PMID: 666816] |
3. |
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. [PMID: 7005231] |
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[EC 1.1.1.184 created 1983] |
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EC |
1.1.1.185 |
Accepted name: |
L-glycol dehydrogenase |
Reaction: |
an L-glycol + NAD(P)+ = a 2-hydroxycarbonyl compound + NAD(P)H + H+ |
Other name(s): |
glycol (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; L-(+)-glycol:NAD(P) oxidoreductase; L-glycol:NAD(P) dehydrogenase |
Systematic name: |
L-glycol:NAD(P)+ oxidoreductase |
Comments: |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77967-75-0 |
References: |
1. |
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. [DOI] [PMID: 7018582] |
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[EC 1.1.1.185 created 1984] |
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EC |
1.1.1.186 |
Accepted name: |
dTDP-galactose 6-dehydrogenase |
Reaction: |
dTDP-D-galactose + 2 NADP+ + H2O = dTDP-D-galacturonate + 2 NADPH + 2 H+ |
Other name(s): |
thymidine-diphosphate-galactose dehydrogenase |
Systematic name: |
dTDP-D-galactose:NADP+ 6-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
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. [DOI] [PMID: 4381717] |
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[EC 1.1.1.186 created 1984, modified 2002] |
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EC |
1.1.1.187 |
Accepted name: |
GDP-4-dehydro-D-rhamnose reductase |
Reaction: |
(1) GDP-α-D-rhamnose + NAD(P)+ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H+ (2) GDP-6-deoxy-α-D-talose + NAD(P)+ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H+ |
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For diagram of gdp-l-fucose and GDP-mannose biosynthesis, 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
GDP-6-deoxy-α-D-talose = GDP-α-D-pneumose
|
Other name(s): |
GDP-4-keto-6-deoxy-D-mannose reductase; GDP-4-keto-D-rhamnose reductase; guanosine diphosphate-4-keto-D-rhamnose reductase; GDP-6-deoxy-D-mannose:NAD(P)+ 4-oxidoreductase; GDP-6-deoxy-α-D-mannose:NAD(P)+ 4-oxidoreductase |
Systematic name: |
GDP-4-dehydro-α-D-rhamnose:NAD(P)+ 4-oxidoreductase |
Comments: |
The enzyme, which operates in the opposite direction to that shown, forms a mixture of GDP-α-D-rhamnose and its C-4 epimer, GDP-6-deoxy-α-D-talose. cf. EC 1.1.1.281, GDP-4-dehydro-6-deoxy-D-mannose reductase and EC 1.1.1.135, GDP-6-deoxy-D-talose 4-dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-56-3 |
References: |
1. |
Barber, G.A. The synthesis of guanosine 5′-diphosphate D-rhamnose by enzymes of a higher plant. Biochim. Biophys. Acta 165 (1968) 68–75. [DOI] [PMID: 4386238] |
2. |
Winkler, N.W. and Markovitz, A. Guanosine diphosphate-4-keto-D-rhamnose reductase. A non-stereoselective enzyme. J. Biol. Chem. 246 (1971) 5868–5876. [PMID: 4398966] |
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[EC 1.1.1.187 created 1984] |
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EC |
1.1.1.188 |
Accepted name: |
prostaglandin-F synthase |
Reaction: |
(5Z,13E)-(15S)-9α,11α,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9α,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+ |
Other name(s): |
prostaglandin-D2 11-reductase; reductase, 15-hydroxy-11-oxoprostaglandin; PGD2 11-ketoreductase; PGF2α synthetase; prostaglandin 11-ketoreductase; prostaglandin D2-ketoreductase; prostaglandin F synthase; prostaglandin F synthetase; synthetase, prostaglandin F2α; PGF synthetase; NADPH-dependent prostaglandin D2 11-keto reductase; prostaglandin 11-keto reductase |
Systematic name: |
(5Z,13E)-(15S)-9α,11α,15-trihydroxyprosta-5,13-dienoate:NADP+ 11-oxidoreductase |
Comments: |
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-nitroacetophenone. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 55976-95-9 |
References: |
1. |
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. [DOI] [PMID: 7248318] |
2. |
Watanabe, K., Shimizu, T. and Hayaishi, O. Enzymatic conversion of prostaglandin-D2 to prostaglandin-F2α in the rat lung. Biochem. Int. 2 (1981) 603–610. |
3. |
Watanabe, K., Yoshida, R., Shimizu, T. and Hayaishi, O. Enzymatic formation of prostaglandin F2α from prostaglandin H2 and D2. Purification and properties of prostaglandin F synthetase from bovine lung. J. Biol. Chem. 260 (1985) 7035–7041. [PMID: 3858278] |
4. |
Wong, P.Y.-K. Purification and partial characterization of prostaglandin D2 11-keto reductase in rabbit liver. Biochim. Biophys. Acta 659 (1981) 169–178. [DOI] [PMID: 7248317] |
5. |
Wong, P.Y.-K. Purification of PGD2 11-ketoreductase from rabbit liver. Methods Enzymol. 86 (1982) 117–125. [PMID: 7132748] |
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[EC 1.1.1.188 created 1984, modified 1989, modified 1990] |
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EC |
1.1.1.189 |
Accepted name: |
prostaglandin-E2 9-reductase |
Reaction: |
(5Z,13E)-(15S)-9α,11α,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-11α,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH + H+ |
Other name(s): |
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 |
Systematic name: |
(5Z,13E)-(15S)-9α,11α,15-trihydroxyprosta-5,13-dienoate:NADP+ 9-oxidoreductase |
Comments: |
Reduces prostaglandin E2 to prostaglandin F2α. 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+). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 42613-35-4 |
References: |
1. |
Lee, S.-C. and Levine, L. Purification and regulatory properties of chicken heart prostaglandin E 9-ketoreductase. J. Biol. Chem. 250 (1975) 4549–4555. [PMID: 166995] |
2. |
Schlegel, W., Krüger, S. and Korte, K. Purification of prostaglandin E2 9-oxoreductase from human decidua vera. FEBS Lett. 171 (1984) 141–144. [DOI] [PMID: 6586494] |
3. |
Tai, H.-H. and Yuan, B. Purification and assay of 9-hydroxyprostaglandin dehydrogenase from rat kidney. Methods Enzymol. 86 (1982) 113–117. [PMID: 7132747] |
4. |
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. [DOI] [PMID: 3901124] |
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[EC 1.1.1.189 created 1984, modified 1989] |
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EC |
1.1.1.190 |
Accepted name: |
indole-3-acetaldehyde reductase (NADH) |
Reaction: |
(indol-3-yl)ethanol + NAD+ = (indol-3-yl)acetaldehyde + NADH + H+ |
Other name(s): |
indoleacetaldehyde reductase; indole-3-acetaldehyde reductase (NADH); indole-3-ethanol:NAD+ oxidoreductase |
Systematic name: |
(indol-3-yl)ethanol:NAD+ oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 58875-06-2 |
References: |
1. |
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. [PMID: 2607] |
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[EC 1.1.1.190 created 1984] |
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EC |
1.1.1.191 |
Accepted name: |
indole-3-acetaldehyde reductase (NADPH) |
Reaction: |
(indol-3-yl)ethanol + NADP+ = (indol-3-yl)acetaldehyde + NADPH + H+ |
Other name(s): |
indoleacetaldehyde (reduced nicotinamide adenine dinucleotide phosphate) reductase; indole-3-acetaldehyde reductase (NADPH); indole-3-ethanol:NADP+ oxidoreductase |
Systematic name: |
(indol-3-yl)ethanol:NADP+ oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 58875-05-1 |
References: |
1. |
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. [PMID: 2607] |
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[EC 1.1.1.191 created 1984] |
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EC |
1.1.1.192 |
Accepted name: |
long-chain-alcohol dehydrogenase |
Reaction: |
a long-chain alcohol + 2 NAD+ + H2O = a long-chain carboxylate + 2 NADH + 2 H+ |
Other name(s): |
long-chain alcohol dehydrogenase; fatty alcohol oxidoreductase |
Systematic name: |
long-chain-alcohol:NAD+ oxidoreductase |
Comments: |
Hexadecanol is a good substrate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 76774-36-2 |
References: |
1. |
Lee, T.-C. Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver. J. Biol. Chem. 254 (1979) 2892–2896. [PMID: 34610] |
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[EC 1.1.1.192 created 1984] |
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EC |
1.1.1.193 |
Accepted name: |
5-amino-6-(5-phosphoribosylamino)uracil reductase |
Reaction: |
5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP+ = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH + H+ |
Other name(s): |
aminodioxyphosphoribosylaminopyrimidine reductase |
Systematic name: |
5-amino-6-(5-phospho-D-ribitylamino)uracil:NADP+ 1′-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 69020-28-6 |
References: |
1. |
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. [PMID: 30756] |
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[EC 1.1.1.193 created 1984, modified 2011] |
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EC |
1.1.1.194 |
Accepted name: |
coniferyl-alcohol dehydrogenase |
Reaction: |
coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+ |
Other name(s): |
CAD (ambiguous) |
Systematic name: |
coniferyl-alcohol:NADP+ oxidoreductase |
Comments: |
Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37250-27-4 |
References: |
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. |
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. [DOI] [PMID: 1250] |
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[EC 1.1.1.194 created 1984] |
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EC |
1.1.1.195 |
Accepted name: |
cinnamyl-alcohol dehydrogenase |
Reaction: |
cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+ |
Other name(s): |
cinnamyl alcohol dehydrogenase; CAD (ambiguous) |
Systematic name: |
cinnamyl-alcohol:NADP+ oxidoreductase |
Comments: |
Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194 coniferyl-alcohol dehydrogenase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 55467-36-2 |
References: |
1. |
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. [DOI] [PMID: 6365550] |
2. |
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. [DOI] [PMID: 1250] |
3. |
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. [DOI] [PMID: 572771] |
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[EC 1.1.1.195 created 1984] |
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EC |
1.1.1.196 |
Accepted name: |
15-hydroxyprostaglandin-D dehydrogenase (NADP+) |
Reaction: |
(5Z,13E)-(15S)-9α,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADP+ = (5Z,13E)-9α-hydroxy-11,15-dioxoprosta-5,13-dienoate + NADPH + H+ |
Other name(s): |
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) |
Systematic name: |
(5Z,13E)-(15S)-9α,15-dihydroxy-11-oxoprosta-5,13-dienoate:NADP+ 15-oxidoreductase |
Comments: |
Specific for prostaglandins D [cf. EC 1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+)]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 84399-95-1 |
References: |
1. |
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. [PMID: 7354056] |
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[EC 1.1.1.196 created 1984, modified 1990] |
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EC |
1.1.1.197 |
Accepted name: |
15-hydroxyprostaglandin dehydrogenase (NADP+) |
Reaction: |
(13E)-(15S)-11α,15-dihydroxy-9-oxoprost-13-enoate + NADP+ = (13E)-11α-hydroxy-9,15-dioxoprost-13-enoate + NADPH + H+ |
Other name(s): |
NADP-dependent 15-hydroxyprostaglandin dehydrogenase; NADP-linked 15-hydroxyprostaglandin dehydrogenase; NADP-specific 15-hydroxyprostaglandin dehydrogenase; type II 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NADP) |
Systematic name: |
(13E)-(15S)-11α,15-dihydroxy-9-oxoprost-13-enoate:NADP+ 15-oxidoreductase |
Comments: |
Acts on prostaglandins E2, F2α 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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 54989-39-8 |
References: |
1. |
Lee, S.-C. and Levine, L. Prostaglandin metabolism. II. Identification of two 15-hydroxyprostaglandin dehydrogenase types. J. Biol. Chem. 250 (1975) 548–552. [PMID: 234431] |
2. |
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. [PMID: 803247] |
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[EC 1.1.1.197 created 1984] |
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EC |
1.1.1.198 |
Accepted name: |
(+)-borneol dehydrogenase |
Reaction: |
(+)-borneol + NAD+ = (+)-camphor + NADH + H+ |
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For diagram of bornane and related monoterpenoids, click here |
Other name(s): |
bicyclic monoterpenol dehydrogenase |
Systematic name: |
(+)-borneol:NAD+ oxidoreductase |
Comments: |
NADP+ can also act, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 111940-47-7 |
References: |
1. |
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. [DOI] [PMID: 677891] |
2. |
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. [DOI] [PMID: 3310901] |
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[EC 1.1.1.198 created 1984, modified 1990 (EC 1.1.1.182 created 1983, part incorporated 1990)] |
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EC |
1.1.1.199 |
Accepted name: |
(S)-usnate reductase |
Reaction: |
(6R)-2-acetyl-6-(3-acetyl-2,4,6-trihydroxy-5-methylphenyl)-3-hydroxy-6-methyl-2,4-cyclohexadien-1-one + NAD+ = (S)-usnate + NADH + H+ |
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For diagram of reaction, click here |
Glossary: |
reduced (S)-usnate = reduced (-)-usnate = (6R)-2-acetyl-6-(3-acetyl-2,4,6-trihydroxy-5-methylphenyl)-3-hydroxy-6-methyl-2,4-cyclohexadien-1-one |
Other name(s): |
L-usnic acid dehydrogenase |
Systematic name: |
reduced-(S)-usnate:NAD+ oxidoreductase (ether-bond-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77237-99-1 |
References: |
1. |
Estevéz, M.P., Legaz, E., Olmeda, L., Pérez, 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. |
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[EC 1.1.1.199 created 1984] |
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EC |
1.1.1.200 |
Accepted name: |
aldose-6-phosphate reductase (NADPH) |
Reaction: |
D-sorbitol 6-phosphate + NADP+ = D-glucose 6-phosphate + NADPH + H+ |
Other name(s): |
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) |
Systematic name: |
D-aldose-6-phosphate:NADP+ 1-oxidoreductase |
Comments: |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 76901-04-7 |
References: |
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. [PMID: 16661614] |
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[EC 1.1.1.200 created 1984] |
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