EC 1.1.1.1 to EC 1.1.1.50See separate file for EC 1.1.1.201 to EC 1.1.1.250
EC 1.1.1.51 to EC 1.1.1.100
EC 1.1.1.101 to EC 1.1.1.150
See the following files for:
EC 1.1.1.201 to EC 1.1.1.250
EC 1.1.1.251 to EC 1.1.1.300
EC 1.1.1.301 to EC 1.1.1.350
EC 1.1.1.351 to EC 1.1.1.441
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.
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]
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 reaction 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. [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]
Accepted name: ureidoglycolate dehydrogenase
Reaction: (S)-ureidoglycolate + NAD(P)+ = oxalureate + NAD(P)H + H+
For diagram 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.M. and Vogels, G.D. S-Ureidoglycolate dehydrogenase: purification and properties. Arch. Biochem. Biophys. 145 (1971) 465-469. [PMID: 4399430]
[EC 1.1.1.155 Deleted entry: the enzyme is identical to EC 1.1.1.87, homoisocitrate dehydrogenase (EC 1.1.1.155 created 1976, deleted 2004)]
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. [PMID: 4146296]
Accepted name: 3-hydroxybutyryl-CoA dehydrogenase
Reaction: (S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+
For diagram of reaction 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. [PMID: 4405720]
[EC 1.1.1.158 Transferred entry: UDP-N-acetylmuramate dehydrogenase. Now EC 1.3.1.98, UDP-N-acetylmuramate dehydrogenase (EC 1.1.1.158 created 1976, modified 1983, modified 2002, deleted 2013)]
Accepted name: 7α-hydroxysteroid dehydrogenase
Reaction: cholate + NAD+ = 3α,12α-dihydroxy-7-oxo-5β-cholanate + NADH + H+
Glossary: cholate = 3α,7α,12α-trihydroxy-5β-cholanate
Other name(s): 7α-hydroxy steroid dehydrogenase; 7α-HSDH
Systematic name: 7α-hydroxysteroid:NAD+ 7-oxidoreductase
Comments: Catalyses the oxidation of the 7α-hydroxyl 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. [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. [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. [PMID: 236764]
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]
[EC 1.1.1.161 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)]
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, 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]
Accepted name: cyclopentanol dehydrogenase
Reaction: cyclopentanol + NAD+ = cyclopentanone + NADH + H+
Other Name(s): cyclopentanol:NADP+ oxidoreductase (incorrect)
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; 69 (2003) 2414 (only). [PMID: 12406764]
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]
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.
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]
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. In: Biochemistry of Insects, issue 17, V.I. Lenin State Pedagogical Institute, Moscow, 1971, p. 56.
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]
Accepted name: 2-dehydropantoate 2-reductase
Reaction: (R)-pantoate + NADP+ = 2-dehydropantoate + NADPH + H+
For diagram of reaction 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. 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.
Accepted name: 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating)
Reaction: a 3β-hydroxysteroid-4α-carboxylate + NAD(P)+ = a 3-oxosteroid + CO2 + NAD(P)H
For diagram of reaction 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. [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. [PMID: 14506130]
[EC 1.1.1.171 Transferred entry: now EC 1.5.1.20 methylenetetrahydrofolate reductase (NADPH) (EC 1.1.1.171 created 1978, deleted 1984)]
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. [PMID: 185965]
Accepted name: L-rhamnose 1-dehydrogenase
Reaction: L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+
For diagram of reaction 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. [PMID: 8142]
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. [PMID: 856571]
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.
Accepted name: 12α-hydroxysteroid dehydrogenase
Reaction: cholate + NADP+ = 3α,7α-dihydroxy-12-oxo-5β-cholanate + NADPH + H+
Glossary: cholate = 3α,7α,12α-trihydroxy-5β-cholanate
Other name(s): 12α-hydroxy steroid dehydrogenase; 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. [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]
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; glycerol-3-phosphate 1-dehydrogenase (NADP); 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. [in Russian] Biokhimiya 41 (1976) 1788-1790.
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]
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]
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.
[EC 1.1.1.180 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)
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 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-hydroxy-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]
[EC 1.1.1.182 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)]
Accepted name: geraniol dehydrogenase
Reaction: geraniol + NADP+ = geranial + NADPH + H+
For diagram of reaction click here.
Systematic name: geraniol:NADP+ oxidoreductase
Comments: Also acts, more slowly, on nerol, farnesol and citronellol.
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.
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; NADPH2-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. [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. [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]
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. [PMID: 7018582]
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, CAS registry number:
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. [PMID: 4381717]
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+
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
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. [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]
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; prostaglandin-D2 11-reductase; 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. [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. [PMID: 7248317]
5. Wong, P.Y.-K. Purification of PGD2 11-ketoreductase from rabbit liver. Methods Enzymol. 86 (1982) 117-125. [PMID: 7132748]
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. [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. [PMID: 3901124]
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 (NADH2); 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]
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 (NADPH2); 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]
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]
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]
Accepted name: coniferyl-alcohol dehydrogenase
Reaction: coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+
Other name(s): CAD
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. [PMID: 1250]
Accepted name: cinnamyl-alcohol dehydrogenase
Reaction: cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH + H+
Other name(s): cinnamyl alcohol dehydrogenase; CAD
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. [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. [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. [PMID: 572771]
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]
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]
Accepted name: (+)-borneol dehydrogenase
Reaction: (+)-borneol + NAD+ = (+)-camphor + NADH + H+
For diagram of reaction 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. [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. [PMID: 3310901]
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)-usnic acid + NADH + H+
For diagram click here.
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.
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.