ExplorEnz: EC 1.*.*.*

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1.1.1.201

Accepted name:

7β-hydroxysteroid dehydrogenase (NADP⁺)

Reaction:

a 7β-hydroxysteroid + NADP⁺ = a 7-oxosteroid + NADPH + H⁺

Other name(s):

NADP-dependent 7β-hydroxysteroid dehydrogenase; 7β-hydroxysteroid dehydrogenase (NADP)

Systematic name:

7β-hydroxysteroid:NADP⁺ 7-oxidoreductase

Comments:

Catalyses the oxidation of the 7β-hydroxy group of bile acids such as ursodeoxycholate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 79393-83-2

References:

1.	Hirano, S. and Masuda, N. Characterization of NADP-dependent 7β-hydroxysteroid dehydrogenases from Peptostreptococcus productus and Eubacterium aerofaciens. Appl. Environ. Microbiol. 43 (1982) 1057–1063. [PMID: 6954878]
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., Rochon, Y.P., Hutchison, D.M. and Holdeman, L.V. Formation of ursodeoxycholic acid from chenodeoxycholic acid by a 7β-hydroxysteroid dehydrogenase-elaborating Eubacterium aerofaciens strain cocultured with 7α-hydroxysteroid dehydrogenase-elaborating organisms. Appl. Environ. Microbiol. 44 (1982) 1187–1195. [PMID: 6758698]

[EC 1.1.1.201 created 1984]

1.1.1.202

Accepted name:

1,3-propanediol dehydrogenase

Reaction:

propane-1,3-diol + NAD⁺ = 3-hydroxypropanal + NADH + H⁺

Other name(s):

3-hydroxypropionaldehyde reductase; 1,3-PD:NAD⁺ oxidoreductase; 1,3-propanediol:NAD⁺ oxidoreductase; 1,3-propanediol dehydrogenase

Systematic name:

propane-1,3-diol:NAD⁺ 1-oxidoreductase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81611-70-3

References:

1.	Abeles, R.H., Brownstein, A.M. and Randles, C.H. α-Hydroxypropionaldehyde, an intermediate in the formation of 1,3-propanediol by Aerobacter melanogaster. Biochim. Biophys. Acta 41 (1960) 530. [DOI] [PMID: 13791444]
2.	Forage, R.G. and Foster, M.A. Glycerol fermentation in Klebsiella pneumoniae: functions of the coenzyme B₁₂-dependent glycerol and diol dehydratases. J. Bacteriol. 149 (1982) 413–419. [PMID: 7035429]

[EC 1.1.1.202 created 1984]

1.1.1.203

Accepted name:

uronate dehydrogenase

Reaction:

(1) β-D-galacturonate + NAD⁺ = D-galactaro-1,5-lactone + NADH + H⁺
(2) β-D-glucuronate + NAD⁺ = D-glucaro-1,5-lactone + NADH + H⁺

Other name(s):

uronate:NAD-oxidoreductase; uronic acid dehydrogenase

Systematic name:

uronate:NAD⁺ 1-oxidoreductase

Comments:

Requires Mg²⁺. The enzyme, characterized from the bacterium Agrobacterium fabrum, participates in oxidative degradation pathways for galacturonate and glucuronate. The enzyme can only accept the β anomeric form of the substrate [4]. The 1,5-lactone product is rather stable at cytosolic pH and does not hydrolyse spontaneously at a substantial rate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-98-9

References:

1.	Kilgore, W.W. and Starr, M.P. Uronate oxidation by phytopathogenic pseudomonads. Nature (Lond.) 183 (1959) 1412–1413. [PMID: 13657147]
2.	Boer, H., Maaheimo, H., Koivula, A., Penttila, M. and Richard, P. Identification in Agrobacterium tumefaciens of the D-galacturonic acid dehydrogenase gene. Appl. Microbiol. Biotechnol. 86 (2010) 901–909. [DOI] [PMID: 19921179]
3.	Andberg, M., Maaheimo, H., Boer, H., Penttila, M., Koivula, A. and Richard, P. Characterization of a novel Agrobacterium tumefaciens galactarolactone cycloisomerase enzyme for direct conversion of D-galactarolactone to 3-deoxy-2-keto-L-threo-hexarate. J. Biol. Chem. 287 (2012) 17662–17671. [DOI] [PMID: 22493433]
4.	Parkkinen, T., Boer, H., Janis, J., Andberg, M., Penttila, M., Koivula, A. and Rouvinen, J. Crystal structure of uronate dehydrogenase from Agrobacterium tumefaciens. J. Biol. Chem. 286 (2011) 27294–27300. [DOI] [PMID: 21676870]

[EC 1.1.1.203 created 1972 as EC 1.2.1.35, transferred 1984 to EC 1.1.1.203, modified 2014]

1.1.1.204

Transferred entry:

xanthine dehydrogenase. Now EC 1.17.1.4, xanthine dehydrogenase. The enzyme was incorrectly classified as acting on a CH-OH group

[EC 1.1.1.204 created 1972 as EC 1.2.1.37, transferred 1984 to EC 1.1.1.204, modified 1989, deleted 2004]

1.1.1.205

Accepted name:

IMP dehydrogenase

Reaction:

IMP + NAD⁺ + H₂O = XMP + NADH + H⁺

For diagram of AMP and GMP biosynthesis, click here

Glossary:

IMP = inosine 5′-phosphate
XMP = xanthosine 5′-phosphate

Other name(s):

inosine-5′-phosphate dehydrogenase; inosinic acid dehydrogenase; inosinate dehydrogenase; inosine 5′-monophosphate dehydrogenase; inosine monophosphate dehydrogenase; IMP oxidoreductase; inosine monophosphate oxidoreductase

Systematic name:

IMP:NAD⁺ oxidoreductase

Comments:

The enzyme acts on the hydroxy group of the hydrated derivative of the substrate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-93-7

References:

1.	Magasanik, B., Moyed, H.S. and Gehring, L.B. Enzymes essential for the biosynthesis of nucleic acid guanine; inosine 5′-phosphate dehydrogenase of Aerobacter aerogenes. J. Biol. Chem. 226 (1957) 339–350. [PMID: 13428767]
2.	Turner, J.F. and King, J.E. Inosine 5-phosphate dehydrogenase of pea seeds. Biochem. J. 79 (1961) 147. [PMID: 13778733]

[EC 1.1.1.205 created 1961 as EC 1.2.1.14, transferred 1984 to EC 1.1.1.205]

1.1.1.206

Accepted name:

tropinone reductase I

Reaction:

tropine + NADP⁺ = tropinone + NADPH + H⁺

For diagram of reaction, click here

Glossary:

tropine = 3α-hydroxytropane = tropan-3-endo-ol

Other name(s):

tropine dehydrogenase; tropinone reductase (ambiguous); TR-I

Systematic name:

tropine:NADP⁺ 3α-oxidoreductase

Comments:

Also oxidizes other tropan-3α-ols, but not the corresponding β-derivatives [1]. This enzyme along with EC 1.1.1.236, tropinone reductase II, represents a branch point in tropane alkaloid metabolism [4]. Tropine (the product of EC 1.1.1.206) is incorporated into hyoscyamine and scopolamine whereas pseudotropine (the product of EC 1.1.1.236) is the first specific metabolite on the pathway to the calystegines [4]. Both enzymes are always found together in any given tropane-alkaloid-producing species, have a common substrate, tropinone, and are strictly stereospecific [3].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 118390-87-7

References:

1.	Koelen, K.J. and Gross, G.G. Partial purification and properties of tropine dehydrogenase from root cultures of Datura stramonium. Planta Med. 44 (1982) 227–230. [PMID: 17402126]
2.	Couladis, M.M, Friesen, J.B., Landgrebe, M.E. and Leete, E. Enzymes catalysing the reduction of tropinone to tropine and ψ-tropine isolated from the roots of Datura innoxia. Pytochemistry 30 (1991) 801–805.
3.	Nakajima, K., Hashimoto, T. and Yamada, Y. Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 9591–9595. [DOI] [PMID: 8415746]
4.	Dräger, B. Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism. Phytochemistry 67 (2006) 327–337. [DOI] [PMID: 16426652]

[EC 1.1.1.206 created 1984, modified 2007]

1.1.1.207

Accepted name:

(-)-menthol dehydrogenase

Reaction:

(-)-menthol + NADP⁺ = (-)-menthone + NADPH + H⁺

For diagram of menthol biosynthesis, click here

Other name(s):

monoterpenoid dehydrogenase

Systematic name:

(-)-menthol:NADP⁺ oxidoreductase

Comments:

Not identical with EC 1.1.1.208 (+)-neomenthol dehydrogenase. Acts also on a number of other cyclohexanols and cyclohexenols.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81811-58-7

References:

1.	Kjonaas, R., Martinkus-Taylor, C. and Croteau, R. Metabolism of monoterpenes: conversion of l-menthone to l-menthol and d-neomenthol by stereospecific dehydrogenases from peppermint (Mentha piperita) leaves. Plant Physiol. 69 (1982) 1013–1017. [PMID: 16662335]

[EC 1.1.1.207 created 1984]

1.1.1.208

Accepted name:

(+)-neomenthol dehydrogenase

Reaction:

(+)-neomenthol + NADP⁺ = (-)-menthone + NADPH + H⁺

For diagram of menthol biosynthesis, click here

Other name(s):

monoterpenoid dehydrogenase

Systematic name:

(+)-neomenthol:NADP⁺ oxidoreductase

Comments:

Not identical with EC 1.1.1.207 (-)-menthol dehydrogenase. Acts also on a number of other cyclohexanols and cyclohexenols.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81811-47-4

References:

1.	Kjonaas, R., Martinkus-Taylor, C. and Croteau, R. Metabolism of monoterpenes: conversion of l-menthone to l-menthol and d-neomenthol by stereospecific dehydrogenases from peppermint (Mentha piperita) leaves. Plant Physiol. 69 (1982) 1013–1017. [PMID: 16662335]

[EC 1.1.1.208 created 1984]

1.1.1.209

Accepted name:

3(or 17)α-hydroxysteroid dehydrogenase

Reaction:

androsterone + NAD(P)⁺ = 5α-androstane-3,17-dione + NAD(P)H + H⁺

Other name(s):

3(17)α-hydroxysteroid dehydrogenase

Systematic name:

3(or 17)α-hydroxysteroid:NAD(P)⁺ oxidoreductase

Comments:

Acts on the 3α-hydroxy group of androgens of the 5α-androstane series; and also, more slowly, on the 17α-hydroxy group of both androgenic and estrogenic substrates (cf. EC 1.1.1.51 3(or 17)β-hydroxysteroid dehydrogenase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83294-77-3

References:

1.	Lau, P.C.K., Layne, D.S. and Williamson, D.G. A 3(17)α-hydroxysteroid dehydrogenase of female rabbit kidney cytosol. Purification and characterization of multiple forms of the enzyme. J. Biol. Chem. 257 (1982) 9444–9449. [PMID: 6955302]
2.	Lau, P.C.K., Layne, D.S. and Williamson, D.G. Comparison of the multiple forms of the soluble 3(17)α-hydroxysteroid dehydrogenases of female rabbit kidney and liver. J. Biol. Chem. 257 (1982) 9450–9456. [PMID: 6955303]

[EC 1.1.1.209 created 1986]

1.1.1.210

Accepted name:

3β(or 20α)-hydroxysteroid dehydrogenase

Reaction:

5α-androstan-3β,17β-diol + NADP⁺ = 17β-hydroxy-5α-androstan-3-one + NADPH + H⁺

Other name(s):

progesterone reductase; dehydrogenase, 3β,20α-hydroxy steroid; 3β,20α-hydroxysteroid oxidoreductase

Systematic name:

3β(or 20α)-hydroxysteroid:NADP⁺ oxidoreductase

Comments:

Also acts on 20α-hydroxysteroids.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 82869-26-9

References:

1.	Sharaf, M.A. and Sweet, F. Dual activity at an enzyme active site: 3β,20α-hydroxysteroid oxidoreductase from fetal blood. Biochemistry 21 (1982) 4615–4620. [PMID: 6958329]

[EC 1.1.1.210 created 1986]

1.1.1.211

Accepted name:

long-chain-3-hydroxyacyl-CoA dehydrogenase

Reaction:

a long-chain (S)-3-hydroxyacyl-CoA + NAD⁺ = a long-chain 3-oxoacyl-CoA + NADH + H⁺

Glossary:

a long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 13 to 22 carbon atoms.

Other name(s):

β-hydroxyacyl-CoA dehydrogenase; long-chain 3-hydroxyacyl coenzyme A dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase; LCHAD

Systematic name:

long-chain-(S)-3-hydroxyacyl-CoA:NAD⁺ oxidoreductase

Comments:

This enzyme was purified from the mitochondrial inner membrane. The enzyme has a preference for long-chain substrates, and activity with a C₁₆ substrate was 6- to 15-fold higher than with a C₄ substrate (cf. EC 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 84177-52-6

References:

1.	El-Fakhri, M. and Middleton, B. The existence of an inner-membrane-bound, long acyl-chain-specific 3-hydroxyacyl-CoA dehydrogenase in mammalian mitochondria. Biochim. Biophys. Acta 713 (1982) 270–279. [DOI] [PMID: 7150615]

[EC 1.1.1.211 created 1986]

1.1.1.212

Accepted name:

3-oxoacyl-[acyl-carrier-protein] reductase (NADH)

Reaction:

a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NAD⁺ = a 3-oxoacyl-[acyl-carrier protein] + NADH + H⁺

Other name(s):

3-oxoacyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide) reductase; 3-oxoacyl-[acyl-carrier-protein] reductase (NADH); (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NAD⁺ oxidoreductase

Systematic name:

(3R)-3-hydroxyacyl-[acyl-carrier protein]:NAD⁺ oxidoreductase

Comments:

Forms part of the fatty acid synthase system in plants. Can be separated from EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82047-86-7

References:

1.	Caughey, I. and Kekwick, R.G.O. The characteristics of some components of the fatty acid synthetase system in the plastids from the mesocarp of avocado (Persea americana) fruit. Eur. J. Biochem. 123 (1982) 553–561. [DOI] [PMID: 7075600]

[EC 1.1.1.212 created 1986]

1.1.1.213

Accepted name:

3α-hydroxysteroid 3-dehydrogenase (Re-specific)

Reaction:

a 3α-hydroxysteroid + NAD(P)⁺ = a 3-oxosteroid + NAD(P)H + H⁺

Other name(s):

3α-hydroxysteroid dehydrogenase; 3α-hydroxysteroid:NAD(P)⁺ 3-oxidoreductase (A-specific); 3α-hydroxysteroid 3-dehydrogenase (A-specific)

Systematic name:

3α-hydroxysteroid:NAD(P)⁺ 3-oxidoreductase (Re-specific)

Comments:

The enzyme acts on multiple 3α-hydroxysteroids. Re-specific with respect to NAD⁺ or NADP⁺ [cf. EC 1.1.1.50, 3α-hydroxysteroid 3-dehydrogenase (Si-specific)]. Enzymes whose stereo-specificity with respect to NAD⁺ or NADP⁺ is not known are described by EC 1.1.1.357, 3α-hydroxysteroid 3-dehydrogenase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-56-2

References:

1.	Björkhem, I. and Danielsson, H. Stereochemistry of hydrogen transfer from pyridine nucleotides catalyzed by Δ⁴-3-oxosteroid 5-β-reductase and 3-α-hydroxysteroid dehydrogenase from rat liver. Eur. J. Biochem. 12 (1970) 80–84. [DOI] [PMID: 4392180]
2.	Tomkins, G.M. A mammalian 3α-hydroxysteroid dehydrogenase. J. Biol. Chem. 218 (1956) 437–447. [PMID: 13278351]

[EC 1.1.1.213 created 1986, modified 2012]

1.1.1.214

Accepted name:

2-dehydropantolactone reductase (Si-specific)

Reaction:

(R)-pantolactone + NADP⁺ = 2-dehydropantolactone + NADPH + H⁺

Other name(s):

2-oxopantoyl lactone reductase; 2-ketopantoyl lactone reductase; ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (B-specific); (R)-pantolactone:NADP⁺ oxidoreductase (B-specific); 2-dehydropantolactone reductase (B-specific)

Systematic name:

(R)-pantolactone:NADP⁺ oxidoreductase (Si-specific)

Comments:

The Escherichia coli enzyme differs from that from yeast [EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific)], which is specific for the Re-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.	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]

[EC 1.1.1.214 created 1986, modified 1999, modified 2013]

1.1.1.215

Accepted name:

gluconate 2-dehydrogenase

Reaction:

D-gluconate + NADP⁺ = 2-dehydro-D-gluconate + NADPH + H⁺

Other name(s):

2-keto-D-gluconate reductase; 2-ketogluconate reductase

Systematic name:

D-gluconate:NADP⁺ oxidoreductase

Comments:

Also acts on L-idonate, D-galactonate and D-xylonate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 68417-42-5

References:

1.	Adachi, O., Chiyonobu, T., Shinagawa, E., Matsushita, K. and Ameyama, M. Crystalline 2-ketogluconate reductase from Acetobacter ascendens, the second instance of crystalline enzyme in genus Acetobacter. Agric. Biol. Chem. 42 (1978) 2057.
2.	Chiyonobu, T., Shinagawa, E., Adachi, O. and Ameyama, M. Purification, crystallization and properties of 2-ketogluconate reductase from Acetobacter rancens. Agric. Biol. Chem. 40 (1976) 175–184.

[EC 1.1.1.215 created 1989]

1.1.1.216

Accepted name:

farnesol dehydrogenase (NADP⁺)

Reaction:

(2E,6E)-farnesol + NADP⁺ = (2E,6E)-farnesal + NADPH + H⁺

For diagram of juvenile hormone biosynthesis, click here

Other name(s):

NADP⁺-farnesol dehydrogenase; farnesol (nicotinamide adenine dinucleotide phosphate) dehydrogenase

Systematic name:

(2E,6E)-farnesol:NADP⁺ 1-oxidoreductase

Comments:

Also acts, more slowly, on (2Z,6E)-farnesol, geraniol, citronerol and nerol.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 89089-75-8, 90804-55-0

References:

1.	Inoue, H., Tsuji, H. and Uritani, I. Characterization and activity change of farnesol dehydrogenase in black rot fungus-infected sweet-potato. Agric. Biol. Chem. 48 (1984) 733–738.

[EC 1.1.1.216 created 1989]

1.1.1.217

Accepted name:

benzyl-2-methyl-hydroxybutyrate dehydrogenase

Reaction:

benzyl (2R,3S)-2-methyl-3-hydroxybutanoate + NADP⁺ = benzyl 2-methyl-3-oxobutanoate + NADPH + H⁺

Other name(s):

benzyl 2-methyl-3-hydroxybutyrate dehydrogenase

Systematic name:

benzyl-(2R,3S)-2-methyl-3-hydroxybutanoate:NADP⁺ 3-oxidoreductase

Comments:

Also acts on benzyl (2S,3S)-2-methyl-3-hydroxybutanoate; otherwise highly specific.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99332-62-4

References:

1.	Furuichi, A., Akita, H., Matsukura, H., Oishi, T. and Horikoshi, K. Purification and properties of an asymmetric reduction enzyme of 2-methyl-3-oxobutyrate in baker's yeast. Agric. Biol. Chem. 49 (1985) 2563–2570.

[EC 1.1.1.217 created 1989]

1.1.1.218

Accepted name:

morphine 6-dehydrogenase

Reaction:

morphine + NAD(P)⁺ = morphinone + NAD(P)H + H⁺

For diagram of morphine biosynthesis, click here

Other name(s):

naloxone reductase

Systematic name:

morphine:NAD(P)⁺ 6-oxidoreductase

Comments:

Also acts on some other alkaloids, including codeine, normorphine and ethylmorphine, but only very slowly on 7,8-saturated derivatives such as dihydromorphine and dihydrocodeine. In the reverse direction, also reduces naloxone to the 6α-hydroxy analogue. Activated by 2-sulfanylethan-1-ol (2-mercaptoethanol).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 97002-71-6

References:

1.	Yamano, S., Kaguera, E., Ishida, T. and Toki, S. Purification and characterization of guinea pig liver morphine 6-dehydrogenase. J. Biol. Chem. 260 (1985) 5259–5264. [PMID: 2580834]
2.	Yamano, S., Nishida, F. and Toki, S. Guinea-pig liver morphine 6-dehydrogenase as a naloxone reductase. Biochem. Pharmacol. 35 (1986) 4321–4326. [DOI] [PMID: 3539118]

[EC 1.1.1.218 created 1989, modified 1990]

1.1.1.219

Accepted name:

dihydroflavonol 4-reductase

Reaction:

a (2R,3S,4S)-leucoanthocyanidin + NADP⁺ = a (2R,3R)-dihydroflavonol + NADPH + H⁺

For diagram of flavonoid biosynthesis, click here

Other name(s):

dihydrokaempferol 4-reductase; dihydromyricetin reductase; NADPH-dihydromyricetin reductase; dihydroquercetin reductase; DFR (gene name); cis-3,4-leucopelargonidin:NADP⁺ 4-oxidoreductase; dihydroflavanol 4-reductase (incorrect)

Systematic name:

(2R,3S,4S)-leucoanthocyanidin:NADP⁺ 4-oxidoreductase

Comments:

This plant enzyme, involved in the biosynthesis of anthocyanidins, is known to act on (+)-dihydrokaempferol, (+)-taxifolin, and (+)-dihydromyricetin, although some enzymes may act only on a subset of these compounds. Each dihydroflavonol is reduced to the corresponding cis-flavan-3,4-diol. NAD⁺ can act instead of NADP⁺, but more slowly.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83682-99-9

References:

1.	Heller, W., Forkmann, G., Britsch, L. and Grisebach, H. Enzymatic reduction of (+)-dihydroflavonols to flavan-3,4-cis- diols with flower extracts from Matthiola incana and its role in anthocyanin biosynthesis. Planta 165 (1985) 284–287. [PMID: 24241054]
2.	Stafford, H.A. and Lester, H.H. Flavan-3-ol biosynthesis the conversion of (+)-dihydromyricetin to its flavan-3,4-diol (leucodelphinidin) and to (+)-gallocatechin by reductases extracted from tissue-cultures of Ginkgo biloba and Pseudotsuga-menziesii. Plant Physiol. 78 (1985) 791–794. [PMID: 16664326]
3.	Fischer, D., Stich, K., Britsch, L. and Grisebach, H. Purification and characterization of (+)dihydroflavonol (3-hydroxyflavanone) 4-reductase from flowers of Dahlia variabilis. Arch. Biochem. Biophys. 264 (1988) 40–47. [DOI] [PMID: 3293532]
4.	Li, H., Qiu, J., Chen, F., Lv, X., Fu, C., Zhao, D., Hua, X. and Zhao, Q. Molecular characterization and expression analysis of dihydroflavonol 4-reductase (DFR) gene in Saussurea medusa. Mol. Biol. Rep. 39 (2012) 2991–2999. [DOI] [PMID: 21701830]

[EC 1.1.1.219 created 1989, modified 2016]

1.1.1.220

Accepted name:

6-pyruvoyltetrahydropterin 2′-reductase

Reaction:

6-lactoyl-5,6,7,8-tetrahydropterin + NADP⁺ = 6-pyruvoyltetrahydropterin + NADPH + H⁺

For diagram of 6-pyruvyltetrahydropterin metabolism, click here

Other name(s):

6-pyruvoyltetrahydropterin reductase; 6PPH4(2′-oxo) reductase; 6-pyruvoyl tetrahydropterin (2′-oxo)reductase; 6-pyruvoyl-tetrahydropterin 2′-reductase; pyruvoyl-tetrahydropterin reductase

Systematic name:

6-lactoyl-5,6,7,8-tetrahydropterin:NADP⁺ 2′-oxidoreductase

Comments:

Not identical with EC 1.1.1.153 sepiapterin reductase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 97089-79-7

References:

1.	Milstien, S. and Kaufman, S. Biosynthesis of tetrahydrobiopterin: conversion of dihydroneopterin triphosphate to tetrahydropterin intermediates. Biochem. Biophys. Res. Commun. 128 (1985) 1099–1107. [DOI] [PMID: 4004850]

[EC 1.1.1.220 created 1989]

1.1.1.221

Accepted name:

vomifoliol dehydrogenase

Reaction:

(6S,9R)-6-hydroxy-3-oxo-α-ionol + NAD⁺ = (6S)-6-hydroxy-3-oxo-α-ionone + NADH + H⁺

For diagram of reaction, click here

Glossary:

(6S,9R)-6-hydroxy-3-oxo-α-ionol = vomifoliol = (4S)-4-hydroxy-4-[(1E,3R)-3-hydroxybut-1-en-1-yl]-3,5,5-trimethylcyclohex-2-en-1-one
(6S)-6-hydroxy-3-oxo-α-ionone = dehydrovomifoliol = (4S)-4-hydroxy-3,5,5-trimethyl-4-[(1E)-3-oxobut-1-en-1-yl]cyclohex-2-en-1-one

Other name(s):

vomifoliol 4′-dehydrogenase; vomifoliol:NAD⁺ 4′-oxidoreductase

Systematic name:

(6S,9R)-6-hydroxy-3-oxo-α-ionol:NAD⁺ oxidoreductase

Comments:

Oxidizes vomifoliol to dehydrovomifoliol; involved in the metabolism of abscisic acid in Corynebacterium sp.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 94949-18-5

References:

1.	Hasegawa, S., Poling, S.M., Maier, V.P. and Bennett, R.D. Metabolism of abscisic-acid bacterial conversion to dehydrovomifoliol and vomifoliol dehydrogenase-activity. Phytochemistry 23 (1984) 2769–2771.

[EC 1.1.1.221 created 1989]

1.1.1.222

Transferred entry:

(R)-4-hydroxyphenyllactate dehydrogenase. Now included with EC 1.1.1.110, aromatic 2-oxoacid reductase

[EC 1.1.1.222 created 1989, deleted 2018]

1.1.1.223

Accepted name:

isopiperitenol dehydrogenase

Reaction:

(-)-trans-isopiperitenol + NAD⁺ = (-)-isopiperitenone + NADH + H⁺

For diagram of (-)-carvone, perillyl aldehyde and pulegone biosynthesis, click here

Systematic name:

(-)-trans-isopiperitenol:NAD⁺ oxidoreductase

Comments:

Acts on (-)-trans-isopiperitenol, (+)-trans-piperitenol and (+)-trans-pulegol. Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 96595-05-0

References:

Kjonaas, R.B., Venkatachalam, K.V. and Croteau, R. Metabolism of monoterpenes: oxidation of isopiperitenol to isopiperitenone, and subsequent isomerization to piperitenone by soluble enzyme preparations from peppermint (Mentha piperita) leaves. Arch. Biochem. Biophys. 238 (1985) 49–60. [DOI] [PMID: 3885858]

[EC 1.1.1.223 created 1989]

1.1.1.224

Accepted name:

mannose-6-phosphate 6-reductase

Reaction:

D-mannitol 1-phosphate + NADP⁺ = D-mannose 6-phosphate + NADPH + H⁺

Other name(s):

NADPH-dependent mannose 6-phosphate reductase; mannose-6-phosphate reductase; 6-phosphomannose reductase; NADP-dependent mannose-6-P:mannitol-1-P oxidoreductase; NADPH-dependent M6P reductase; NADPH-mannose-6-P reductase

Systematic name:

D-mannitol-1-phosphate:NADP⁺ 6-oxidoreductase

Comments:

Involved in the biosynthesis of mannitol in celery (Apium graveolens) leaves.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 88747-79-9

References:

1.	Rumpho, M.E., Edwards, G.E. and Loescher, W.H. A pathway for photosynthetic carbon flow to mannitol in celery leaves. Activity and localization of key enzymes. Plant Physiol. 73 (1983) 869–873. [PMID: 16663332]

[EC 1.1.1.224 created 1989]

1.1.1.225

Accepted name:

chlordecone reductase

Reaction:

chlordecone alcohol + NADP⁺ = chlordecone + NADPH + H⁺

Other name(s):

CDR

Systematic name:

chlordecone-alcohol:NADP⁺ 2-oxidoreductase

Comments:

Chlordecone is an organochlorine pesticide.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102484-73-1

References:

1.	Molowa, D.T., Shayne, A.G. and Guzelian, P.S. Purification and characterization of chlordecone reductase from human liver. J. Biol. Chem. 261 (1986) 12624–12627. [PMID: 2427522]

[EC 1.1.1.225 created 1989]

1.1.1.226

Accepted name:

trans-4-hydroxycyclohexanecarboxylate dehydrogenase

Reaction:

trans-4-hydroxycyclohexane-1-carboxylate + NAD⁺ = 4-oxocyclohexane-1-carboxylate + NADH + H⁺

Glossary:

trans-4-hydroxycyclohexane-1-carboxylate = trans-4-hydroxycyclohexanecarboxylate
4-oxocyclohexane-1-carboxylate = 4-oxocyclohexanecarboxylate

Other name(s):

4-hydroxycyclohexanecarboxylate dehydrogenase (ambiguous); chcB1 (gene name)

Systematic name:

trans-4-hydroxycyclohexane-1-carboxylate:NAD⁺ 4-oxidoreductase

Comments:

The enzyme from Corynebacterium cyclohexanicum is highly specific for the trans-4-hydroxy derivative. cf. EC 1.1.1.438, cis-4-hydroxycyclohexanecarboxylate dehydrogenase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67272-36-0

References:

1.	Obata, H., Uebayashi, M. and Kaneda, T. Purification and properties of 4-hydroxycyclohexanecarboxylate dehydrogenase from Corynebacterium cyclohexanicum. Eur. J. Biochem. 174 (1988) 451–458. [DOI] [PMID: 3292236]
2.	Yamamoto, T., Hasegawa, Y., Lau, P.CK. and Iwaki, H. Identification and characterization of a chc gene cluster responsible for the aromatization pathway of cyclohexanecarboxylate degradation in Sinomonas cyclohexanicum ATCC 51369. J. Biosci. Bioeng. 132 (2021) 621–629. [DOI] [PMID: 34583900]

[EC 1.1.1.226 created 1990, modified 2024]

1.1.1.227

Accepted name:

(-)-borneol dehydrogenase

Reaction:

(-)-borneol + NAD⁺ = (-)-camphor + NADH + H⁺

Systematic name:

(-)-borneol:NAD⁺ oxidoreductase

Comments:

NADP⁺ can also act, but more slowly.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 111940-48-8

References:

1.	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]

[EC 1.1.1.227 created 1990 (EC 1.1.1.182 created 1983, part incorporated 1990)]

1.1.1.228

Accepted name:

(+)-sabinol dehydrogenase

Reaction:

(+)-cis-sabinol + NAD⁺ = (+)-sabinone + NADH + H⁺

For diagram of thujane monoterpenoid biosynthesis, click here

Other name(s):

(+)-cis-sabinol dehydrogenase

Systematic name:

(+)-cis-sabinol:NAD⁺ oxidoreductase

Comments:

NADP⁺ can also act, but more slowly. Involved in the biosynthesis of (+)-3-thujone and (–)-3-isothujone.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 111940-50-2

References:

1.	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]

[EC 1.1.1.228 created 1990 (EC 1.1.1.182 created 1983, part incorporated 1990)]

1.1.1.229

Accepted name:

diethyl 2-methyl-3-oxosuccinate reductase

Reaction:

diethyl (2R,3R)-2-methyl-3-hydroxysuccinate + NADP⁺ = diethyl 2-methyl-3-oxosuccinate + NADPH + H⁺

Systematic name:

diethyl-(2R,3R)-2-methyl-3-hydroxysuccinate:NADP⁺ 3-oxidoreductase

Comments:

Also acts on diethyl (2S,3R)-2-methyl-3-hydroxysuccinate; and on the corresponding dimethyl esters.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 110369-21-6

References:

1.	Furuichi, A., Akita, H., Matsukura, H., Oishi, T. and Horikoshi, K. Purification and properties of an asymmetric reduction of diethyl 2-methyl-3-oxosuccinate in Saccharomyces fermentati. Agric. Biol. Chem. 51 (1987) 293–299.

[EC 1.1.1.229 created 1990]

1.1.1.230

Accepted name:

3α-hydroxyglycyrrhetinate dehydrogenase

Reaction:

3α-hydroxyglycyrrhetinate + NADP⁺ = 3-oxoglycyrrhetinate + NADPH + H⁺

Systematic name:

3α-hydroxyglycyrrhetinate:NADP⁺ 3-oxidoreductase

Comments:

Highly specific to 3α-hydroxy derivatives of glycyrrhetinate and its analogues. Not identical to EC 1.1.1.50 3α-hydroxysteroid dehydrogenase (Si-specific).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 114308-07-5

References:

1.	Akao, T., Akao, T., Hattori, M., Namba, T. and Kobashi, K. Purification and properties of 3α-hydroxyglycyrrhetinate dehydrogenase of Clostridium innocuum from human intestine. J. Biochem. (Tokyo) 103 (1988) 504–507. [PMID: 3164718]

[EC 1.1.1.230 created 1990]

1.1.1.231

Accepted name:

15-hydroxyprostaglandin-I dehydrogenase (NADP⁺)

Reaction:

(5Z,13E)-(15S)-6,9α-epoxy-11α,15-dihydroxyprosta-5,13-dienoate + NADP⁺ = (5Z,13E)-6,9α-epoxy-11α-hydroxy-15-oxoprosta-5,13-dienoate + NADPH + H⁺

Other name(s):

prostacyclin dehydrogenase; PG I₂ dehydrogenase; prostacyclin dehydrogenase; NADP-linked 15-hydroxyprostaglandin (prostacyclin) dehydrogenase; NADP⁺-dependent PGI₂-specific 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostaglandin-I dehydrogenase (NADP)

Systematic name:

(5Z,13E)-(15S)-6,9α-epoxy-11α,15-dihydroxyprosta-5,13-dienoate:NADP⁺ 15-oxidoreductase

Comments:

Specific for prostaglandin I₂.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 79468-49-8

References:

1.	Korff, J.M. and Jarabak, J. Isolation and properties of an NADP⁺-dependent PGI₂-specific 15-hydroxyprostaglandin dehydrogenase from rabbit kidney. Methods Enzymol. 86 (1982) 152–155. [PMID: 6182444]

[EC 1.1.1.231 created 1990]

1.1.1.232

Accepted name:

15-hydroxyicosatetraenoate dehydrogenase

Reaction:

(15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)⁺ = 15-oxo-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)H + H⁺

Other name(s):

15-hydroxyeicosatetraenoate dehydrogenase

Systematic name:

(15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate:NAD(P)⁺ 15-oxidoreductase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 117910-46-0

References:

1.	Sok, D.-E., Kang, J.B. and Shin, H.D. 15-Hydroxyeicosatetraenoic acid dehydrogenase activity in microsomal fraction of mouse liver homogenate. Biochem. Biophys. Res. Commun. 156 (1988) 524–529. [DOI] [PMID: 3052453]

[EC 1.1.1.232 created 1992]

1.1.1.233

Accepted name:

N-acylmannosamine 1-dehydrogenase

Reaction:

N-acyl-D-mannosamine + NAD⁺ = N-acyl-D-mannosaminolactone + NADH + H⁺

Other name(s):

N-acylmannosamine dehydrogenase; N-acetyl-D-mannosamine dehydrogenase; N-acyl-D-mannosamine dehydrogenase; N-acylmannosamine dehydrogenase

Systematic name:

N-acyl-D-mannosamine:NAD⁺ 1-oxidoreductase

Comments:

Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine. Highly specific.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 117698-08-5

References:

1.	Horiuchi, T. and Kurokawa, T. Purification and properties of N-acyl-D-mannosamine dehydrogenase from Flavobacterium sp. 141-8. J. Biochem. (Tokyo) 104 (1988) 466–471. [PMID: 3240988]

[EC 1.1.1.233 created 1992]

1.1.1.234

Accepted name:

flavanone 4-reductase

Reaction:

(2S)-flavan-4-ol + NADP⁺ = (2S)-flavanone + NADPH + H⁺

For diagram of the biosynthesis of naringenin derivatives, click here

Systematic name:

(2S)-flavan-4-ol:NADP⁺ 4-oxidoreductase

Comments:

Involved in the biosynthesis of 3-deoxyanthocyanidins from flavanones such as naringenin or eriodictyol.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 115232-53-6

References:

1.	Stich, K. and Forkmann, G. Biosynthesis of 3-deoxyanthocyanins with flower extracts from Sinningia cardinalis. Phytochemistry 27 (1988) 785–789.

[EC 1.1.1.234 created 1992]

1.1.1.235

Accepted name:

8-oxocoformycin reductase

Reaction:

coformycin + NADP⁺ = 8-oxocoformycin + NADPH + H⁺

Other name(s):

8-ketodeoxycoformycin reductase

Systematic name:

coformycin:NADP⁺ 8-oxidoreductase

Comments:

Si-specific with respect to NADPH. Also reduces 8-oxodeoxy-coformycin to the nucleoside antibiotic deoxycoformycin.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 114995-16-3

References:

1.	Hanvey, J.C., Hawkins, E.S., Baker, D.C. and Suhadolnick, R.J. 8-Ketodeoxycoformycin and 8-ketocoformycin as intermediates in the biosynthesis of 2′-deoxycoformycin and coformycin. Biochemistry 27 (1988) 5790–5795. [PMID: 3052586]

[EC 1.1.1.235 created 1992]

1.1.1.236

Accepted name:

tropinone reductase II

Reaction:

pseudotropine + NADP⁺ = tropinone + NADPH + H⁺

For diagram of reaction, click here

Glossary:

pseudotropine = ψ-tropine = 3β-hydroxytropane = tropan-3-exo-ol

Other name(s):

tropinone (ψ-tropine-forming) reductase; pseudotropine forming tropinone reductase; tropinone reductase (ambiguous); TR-II

Systematic name:

pseudotropine:NADP⁺ 3-oxidoreductase

Comments:

This enzyme along with EC 1.1.1.206, tropine dehydrogenase, represents a branch point in tropane alkaloid metabolism [3]. Tropine (the product of EC 1.1.1.206) is incorporated into hyoscyamine and scopolamine whereas pseudotropine (the product of EC 1.1.1.236) is the first specific metabolite on the pathway to the calystegines [3]. Both enzymes are always found together in any given tropane-alkaloid-producing species, have a common substrate, tropinone, and are strictly stereospecific [2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 136111-61-0

References:

1.	Dräger, B., Hashimoto, T. and Yamada, Y. Purification and characterization of pseudotropine forming tropinone reductase from Hyoscyamus niger root cultures. Agric. Biol. Chem. 52 (1988) 2663–2667.
2.	Couladis, M.M, Friesen, J.B., Landgrebe, M.E. and Leete, E. Enzymes catalysing the reduction of tropinone to tropine and ψ-tropine isolated from the roots of Datura innoxia. Pytochemistry 30 (1991) 801–805.
3.	Nakajima, K., Hashimoto, T. and Yamada, Y. Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 9591–9595. [DOI] [PMID: 8415746]
4.	Dräger, B. Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism. Phytochemistry 67 (2006) 327–337. [DOI] [PMID: 16426652]

[EC 1.1.1.236 created 1992, modified 2007]

1.1.1.237

Accepted name:

hydroxyphenylpyruvate reductase

Reaction:

(1) (R)-3-(4-hydroxyphenyl)lactate + NAD(P)⁺ = 3-(4-hydroxyphenyl)pyruvate + NAD(P)H + H⁺
(2) (R)-3-(3,4-dihydroxyphenyl)lactate + NAD(P)⁺ = 3-(3,4-dihydroxyphenyl)pyruvate + NAD(P)H + H⁺

For diagram of 4-hydroxyphenylpyruvate metabolites, click here and for diagram of rosmarinate biosynthesis, click here

Other name(s):

HPPR

Systematic name:

(R)-3-(4-hydroxyphenyl)lactate:NAD(P)⁺ oxidoreductase

Comments:

The enzyme participates in the biosynthesis of rosmarinic acid. It belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases, and prefers NADPH to NADH.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 117590-77-9

References:

1.	Petersen, M. and Alfermann, A.W. Two new enzymes of rosmarinic acid biosynthesis from cell cultures of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic acid synthase. Z. Naturforsch. C: Biosci. 43 (1988) 501–504.
2.	Kim, K.H., Janiak, V. and Petersen, M. Purification, cloning and functional expression of hydroxyphenylpyruvate reductase involved in rosmarinic acid biosynthesis in cell cultures of Coleus blumei. Plant Mol. Biol. 54 (2004) 311–323. [PMID: 15284489]
3.	Kim, Y.B., Uddina, M.R., Kim, Y., Park, C.G. and Park, S.U. Molecular cloning and characterization of tyrosine aminotransferase and hydroxyphenylpyruvate reductase, and rosmarinic acid accumulation in Scutellaria baicalensis. Nat. Prod. Commun. 9 (2014) 1311–1314. [PMID: 25918800]
4.	Wang, G.Q., Chen, J.F., Yi, B., Tan, H.X., Zhang, L. and Chen, W.S. HPPR encodes the hydroxyphenylpyruvate reductase required for the biosynthesis of hydrophilic phenolic acids in Salvia miltiorrhiza. Chin J Nat Med 15 (2017) 917–927. [PMID: 29329649]

[EC 1.1.1.237 created 1992, modified 2018]

1.1.1.238

Accepted name:

12β-hydroxysteroid dehydrogenase

Reaction:

3α,7α,12β-trihydroxy-5β-cholan-24-oate + NADP⁺ = 3α,7α-dihydroxy-12-oxo-5β-cholan-24-oate + NADPH + H⁺

Other name(s):

12β-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) dehydrogenase

Systematic name:

12β-hydroxysteroid:NADP⁺ 12-oxidoreductase

Comments:

Acts on a number of bile acids, both in their free and conjugated forms.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 118390-62-8

References:

1.	Edenharder, R. and Pfützner, A. Characterization of NADP-dependent 12β-hydroxysteroid dehydrogenase from Clostridium paraputrificum. Biochim. Biophys. Acta 962 (1988) 362–370. [DOI] [PMID: 3167086]

[EC 1.1.1.238 created 1992]

1.1.1.239

Accepted name:

3α(17β)-hydroxysteroid dehydrogenase (NAD⁺)

Reaction:

testosterone + NAD⁺ = androstenedione + NADH + H⁺

Glossary:

androstenedione = androst-4-ene-3,17-dione

Other name(s):

3α,17β-hydroxy steroid dehydrogenase; 3α(17β)-HSD; 17-ketoreductase (ambiguous); 17β-HSD (ambiguous); HSD17B6 (gene name); HSD17B8 (gene name)

Systematic name:

3α(or 17β)-hydroxysteroid:NAD⁺ oxidoreductase

Comments:

Also acts on other 17β-hydroxysteroids and on the 3α-hydroxy group of pregnanes and bile acids. Different from EC 1.1.1.50 3α-hydroxysteroid dehydrogenase (Si-specific) or EC 1.1.1.213 3α-hydroxysteroid dehydrogenase (Re-specific).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 126469-82-7

References:

1.	Sweat, M.L., Samuels, L.T. and Lumry, R. Preparation and characterisation of the enzyme which converts testosterone to androstendione. J. Biol. Chem. 185 (1950) 75–84. [PMID: 15436478]
2.	Villee, C.A. and Spencer, J.M. Some properties of the pyridine nucleotide-specific 17β-hydroxy steroid dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 3615–3619. [PMID: 13781425]
3.	Endahl, G.L., Kochakia, C.D. and Hamm, D. Separation of a triphosphopyridine nucleotide-specific from a diphosphopyridine-specific 17β-hydroxy (testosterone) dehydrogenase of guinea pig liver. J. Biol. Chem. 235 (1960) 2792–2796. [PMID: 13696735]
4.	Ohmura, M., Hara, A., Nakagawa, M. and Sawada, H. Demonstration of 3α(17β)-hydroxysteroid dehydrogenase distinct from 3α-hydroxysteroid dehydrogenase in hamster liver. Biochem. J. 266 (1990) 583–589. [PMID: 2317205]

[EC 1.1.1.239 created 1992, modified 2012 (EC 1.1.1.63 created 1965, incorporated 2012)]

1.1.1.240

Accepted name:

N-acetylhexosamine 1-dehydrogenase

Reaction:

N-acetyl-α-D-glucosamine + NAD⁺ = N-acetyl-D-glucosaminate + NADH + H⁺

Other name(s):

N-acetylhexosamine dehydrogenase; N-acetyl-D-hexosamine dehydrogenase

Systematic name:

N-acetyl-D-hexosamine:NAD⁺ 1-oxidoreductase

Comments:

Also acts on N-acetylgalactosamine and, more slowly, on N-acetylmannosamine. Anomeric specificity was tested with N-acetyl-D-glucosamine, and it was shown that the enzyme is specific for the α anomer.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122785-18-6

References:

1.	Horiuchi, T. and Kurokawa, T. Purification and characterization of N-acetyl-D-hexosamine dehydrogenase from Pseudomonas sp no 53. Agric. Biol. Chem. 53 (1989) 1919–1925.

[EC 1.1.1.240 created 1992]

1.1.1.241

Accepted name:

6-endo-hydroxycineole dehydrogenase

Reaction:

6-endo-hydroxycineole + NAD⁺ = 6-oxocineole + NADH + H⁺

For diagram of 1,8-cineole catabolism, click here

Systematic name:

6-endo-hydroxycineole:NAD⁺ 6-oxidoreductase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122933-68-0

References:

1.	Williams, D.R., Trudgill, P.W. and Taylor, D.G. Metabolism of 1,8-cineole by Rhodococcus species: ring cleavage reactions. J. Gen. Microbiol. 135 (1989) 1957–1967.

[EC 1.1.1.241 created 1992]

1.1.1.242

Transferred entry:

zeatin reductase. Now EC 1.3.1.69, zeatin reductase

[EC 1.1.1.242 created 1992, deleted 2001]

1.1.1.243

Accepted name:

carveol dehydrogenase

Reaction:

(–)-trans-carveol + NADP⁺ = (–)-carvone + NADPH + H⁺

For diagram of (–)-carvone, perillyl aldehyde and pulegone biosynthesis, click here

Other name(s):

(–)-trans-carveol dehydrogenase

Systematic name:

(–)-trans-carveol:NADP⁺ oxidoreductase

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 122653-66-1

References:

1.	Gershenzon, J., Maffei, M. and Croteau, R. Biochemical and histochemical-localization of monoterpene biosynthesis in the glandular trichomes of spearmint (Mentha spicata). Plant Physiol. 89 (1989) 1351–1357. [PMID: 16666709]

[EC 1.1.1.243 created 1992]

1.1.1.244

Accepted name:

methanol dehydrogenase

Reaction:

methanol + NAD⁺ = formaldehyde + NADH + H⁺

Systematic name:

methanol:NAD⁺ oxidoreductase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74506-37-9

References:

Arfman, N., Watling, E.M., Clement, W., van Oosterwijk, R.J., de Vries, G.E., Harder, W., Attwood, M.M. and Dijkhuizen, L. Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme. Arch. Microbiol. 152 (1989) 280–288. [PMID: 2673121]

[EC 1.1.1.244 created 1992]

1.1.1.245

Accepted name:

cyclohexanol dehydrogenase

Reaction:

cyclohexanol + NAD⁺ = cyclohexanone + NADH + H⁺

Systematic name:

cyclohexanol:NAD⁺ oxidoreductase

Comments:

Also oxidizes some other alicyclic alcohols and diols.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 63951-98-4

References:

1.	Dangel, W., Tschech, A. and Fuchs, G. Enzyme-reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species. Arch. Microbiol. 152 (1989) 273–279. [PMID: 2505723]
2.	Donoghue, N.A. and Trudgill, P.W. The metabolism of cyclohexanol by Acinetobacter NCIB 9871. Eur. J. Biochem. 60 (1975) 1–7. [DOI] [PMID: 1261]
3.	Trower, M.K., Buckland, R.M., Higgins, R. and Griffin, M. Isolation and characterization of a cyclohexane-metabolizing Xanthobacter sp. Appl. Environ. Microbiol. 49 (1985) 1282–1289. [PMID: 16346796]

[EC 1.1.1.245 created 1992]

1.1.1.246

Transferred entry:

pterocarpin synthase. This activity is now known to be catalysed by two enzymes, vestitone reductase (EC 1.1.1.348) and medicarpin synthase (EC 4.2.1.139).

[EC 1.1.1.246 created 1992, deleted 2013]

1.1.1.247

Accepted name:

codeinone reductase (NADPH)

Reaction:

codeine + NADP⁺ = codeinone + NADPH + H⁺

For diagram of morphine biosynthesis, click here

Systematic name:

codeine:NADP⁺ oxidoreductase

Comments:

Catalyses the reversible reduction of codeinone to codeine, which is a direct precursor of morphine in the opium poppy plant, Papaver somniferum.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 153302-41-1

References:

1.	Lenz, R. and Zenk, M.H. Stereoselective reduction of codeinone, the penultimate step during morphine biosynthesis in Papaver somniferum. Tetrahedron Lett. 36 (1995) 2449–2452.
2.	Lenz, R. and Zenk, M.H. Purification and properties of codeinone reductase (NADPH) from Papaver somniferum cell cultures. Eur. J. Biochem. 233 (1995) 132–139. [DOI] [PMID: 7588736]

[EC 1.1.1.247 created 1999, modified 2001]

1.1.1.248

Accepted name:

salutaridine reductase (NADPH)

Reaction:

salutaridinol + NADP⁺ = salutaridine + NADPH + H⁺

For diagram of thebaine biosynthesis, click here

Systematic name:

salutaridinol:NADP⁺ 7-oxidoreductase

Comments:

Catalyses the reversible reduction of salutaridine to salutaridinol, which is a direct precursor of morphinan alkaloids in the poppy plant.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 152743-95-8

References:

1.	Gerady, R. and Zenk, M.H. Purification and characterization of salutaridine:NADPH 7-oxidoreductase from Papaver somniferum. Phytochemistry 34 (1993) 125–132.

[EC 1.1.1.248 created 1999, modified 2001]

1.1.1.249

Deleted entry:

Provisional entry deleted. Revised and reinstated as EC 2.5.1.46 deoxyhypusine synthase

[EC 1.1.1.249 provisional version created 1999, deleted 1999 (reinstated 2001 as EC 2.5.1.46)]

1.1.1.250

Accepted name:

D-arabinitol 2-dehydrogenase

Reaction:

D-arabinitol + NAD⁺ = D-ribulose + NADH + H⁺

Other name(s):

D-arabinitol 2-dehydrogenase (ribulose-forming)

Systematic name:

D-arabinitol:NAD⁺ 2-oxidoreductase (D-ribulose-forming)

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 336883-93-3

References:

1.	Wong, B., Murray, J.S., Castellanos, M. and Croen, K.D. D-Arabitol metabolism in Candida albicans: studies of the biosynthetic pathway and the gene that encodes NAD-dependent D-arabitol dehydrogenase. J. Bacteriol. 175 (1993) 6314–6320. [DOI] [PMID: 8407803]
2.	Quong, M.W., Miyada, C.G., Switchenko, A.C. and Goodman, T.C. Identification, purification, and characterization of a D-arabinitol-specific dehydrogenase from Candida tropicalis. Biochem. Biophys. Res. Commun. 196 (1993) 1323–1329. [DOI] [PMID: 8250887]

[EC 1.1.1.250 created 1999]