Enzyme Nomenclature

Continued from EC 1.2.2 to EC 1.2.99

EC 1.3

ACTING ON THE CH-CH GROUP OF DONORS

Sections

EC 1.3.1 With NAD+ or NADP+ as acceptor
EC 1.3.2 With a cytochrome as acceptor
EC 1.3.3 With oxygen as acceptor
EC 1.3.5 With a quinone or related compound as acceptor
EC 1.3.7 With an iron-sulfur protein as acceptor
EC 1.3.98 With other, known, physiological acceptors

EC 1.3.99 With unknown physiological acceptors


EC 1.3.1 With NAD+ or NADP+ as acceptor

See separate file for EC 1.3.1.51 to EC 1.3.1.111

Contents

EC 1.3.1.1 dihydropyrimidine dehydrogenase (NAD+)
EC 1.3.1.2 dihydropyrimidine dehydrogenase (NADP+)
EC 1.3.1.3 Δ4-3-oxosteroid 5β-reductase
EC 1.3.1.4 now EC 1.3.1.22
EC 1.3.1.5 cucurbitacin Δ23-reductase
EC 1.3.1.6 fumarate reductase (NADH)
EC 1.3.1.7 meso-tartrate dehydrogenase
EC 1.3.1.8 acyl-CoA dehydrogenase (NADP+)
EC 1.3.1.9 enoyl-[acyl-carrier-protein] reductase (NADH)
EC 1.3.1.10 enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)
EC 1.3.1.11 coumarate reductase
EC 1.3.1.12 prephenate dehydrogenase
EC 1.3.1.13 prephenate dehydrogenase (NADP+)
EC 1.3.1.14 dihydroorotate dehydrogenase (NAD+)
EC 1.3.1.15 dihydroorotate dehydrogenase (NADP+)
EC 1.3.1.16 β-nitroacrylate reductase
EC 1.3.1.17 3-methyleneoxindole reductase
EC 1.3.1.18 kynurenate-7,8-dihydrodiol dehydrogenase
EC 1.3.1.19 cis-1,2-dihydrobenzene-1,2-diol dehydrogenase
EC 1.3.1.20 trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
EC 1.3.1.21 7-dehydrocholesterol reductase
EC 1.3.1.22 3-oxo-5α-steroid 4-dehydrogenase (NADP+)
EC 1.3.1.23 deleted now EC 1.3.1.3
EC 1.3.1.24 biliverdin reductase
EC 1.3.1.25 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase
EC 1.3.1.26 transferred now EC 1.17.1.8
EC 1.3.1.27 2-hexadecenal reductase
EC 1.3.1.28 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
EC 1.3.1.29 cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase
EC 1.3.1.30 progesterone 5α-reductase
EC 1.3.1.31 2-enoate reductase
EC 1.3.1.32 maleylacetate reductase
EC 1.3.1.33 protochlorophyllide reductase
EC 1.3.1.34 2,4-dienoyl-CoA reductase (NADPH)
EC 1.3.1.35 transferred now EC 1.14.19.22
EC 1.3.1.36 geissoschizine dehydrogenase
EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH)
EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH)
EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)
EC 1.3.1.40 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate reductase
EC 1.3.1.41 xanthommatin reductase
EC 1.3.1.42 12-oxophytodienoate reductase
EC 1.3.1.43 arogenate dehydrogenase
EC 1.3.1.44 trans-2-enoyl-CoA reductase (NAD+)
EC 1.3.1.45 2'-hydroxyisoflavone reductase
EC 1.3.1.46 biochanin-A reductase
EC 1.3.1.47 α-santonin 1,2-reductase
EC 1.3.1.48 13,14-dehydro-15-oxoprostaglandin 13-reductase
EC 1.3.1.49 cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase
EC 1.3.1.50 now EC 1.1.1.252

See the following files for:

EC 1.3.1.51 to EC 1.3.1.111

EC 1.3.1.1

Accepted name: dihydropyrimidine dehydrogenase (NAD+)

Reaction: (1) 5,6-dihydrouracil + NAD+ = uracil + NADH + H+
(2) 5,6-dihydrothymine + NAD+ = thymine + NADH + H+

For diagram of reaction click here.

Other name(s): dihydropyrimidine dehydrogenase; dihydrothymine dehydrogenase; pyrimidine reductase; thymine reductase; uracil reductase; dihydrouracil dehydrogenase (NAD+)

Systematic name: 5,6-dihydropyrimidine:NAD+ oxidoreductase

Comments: An iron-sulfur flavoenzyme. The enzyme was originally discovered in the uracil-fermenting bacterium, Clostridium uracilicum, which utilizes uracil and thymine as nitrogen and carbon sources for growth [1]. Since then the enzyme was found in additional organisms including Alcaligenes eutrophus [2], Pseudomonas strains [3,4] and Escherichia coli [5,6].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-89-5

References:

1. Campbell, L.L. Reductive degradation of pyrimidines. III. Purificaion and properties of dihydrouracil dehydrogenase. J. Biol. Chem. 227 (1957) 693-700. [PMID: 13462991]

2. Schmitt, U., Jahnke, K., Rosenbaum, K., Cook, P.F. and Schnackerz, K.D. Purification and characterization of dihydropyrimidine dehydrogenase from Alcaligenes eutrophus. Arch. Biochem. Biophys. 332 (1996) 175-182. [PMID: 8806723]

3. Kim, S. and West, T.P. Pyrimidine catabolism in Pseudomonas aeruginosa. FEMS Microbiol. Lett. 61 (1991) 175-179. [PMID: 1903745]

4. West, T.P. Pyrimidine base catabolism in Pseudomonas putida biotype B. Antonie Van Leeuwenhoek 80 (2001) 163-167. [PMID: 11759049]

5. West, T.P. Isolation and characterization of an Escherichia coli B mutant strain defective in uracil catabolism. Can. J. Microbiol. 44 (1998) 1106-1109. [PMID: 10030006]

6. Hidese, R., Mihara, H., Kurihara, T. and Esaki, N. Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil. J. Bacteriol. 193 (2011) 989-993. [PMID: 21169495]

[EC 1.3.1.1 created 1961, modified 2011]

EC 1.3.1.2

Accepted name: dihydropyrimidine dehydrogenase (NADP+)

Reaction: 5,6-dihydrouracil + NADP+ = uracil + NADPH + H+

For diagram of reaction click here.

Other name(s): dihydrothymine dehydrogenase; dihydrouracil dehydrogenase (NADP); 4,5-dihydrothymine: oxidoreductase; DPD; DHPDH; dehydrogenase, dihydrouracil (nicotinamide adenine dinucleotide phosphate); dihydrouracil dehydrogenase (NADP); DHU dehydrogenase; hydropyrimidine dehydrogenase; dihydropyrimidine dehydrogenase (NADP)

Systematic name: 5,6-dihydrouracil:NADP+ 5-oxidoreductase

Comments: Also acts on dihydrothymine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-01-0

References:

1. Fritzson, P. Properties and assay of dihydrouracil dehydrogenase of rat liver. J. Biol. Chem. 235 (1960) 719-725.

2. Shiotani, T. and Weber, G. Purification and properties of dihydrothymine dehydrogenase from rat liver. J. Biol. Chem. 256 (1981) 219-224. [PMID: 7451435]

[EC 1.3.1.2 created 1961, modified 1986]

EC 1.3.1.3

Accepted name: Δ4-3-oxosteroid 5β-reductase

Reaction: (1) 5β-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH + H+

(2) 17,21-dihydroxy-5β-pregnane-3,11,20-trione + NADP+ = cortisone + NADPH + H+

Glossary: cortisone = 17,21-dihydroxypregn-4-ene-3,11,20-trione

For diagram click here.

Other name(s): 3-oxo-Δ4-steroid 5β-reductase; 5β-reductase; androstenedione 5β-reductase; cholestenone 5β-reductase; cortisone 5β-reductase; cortisone β-reductase; cortisone Δ4-5β-reductase; steroid 5β-reductase; testosterone 5β-reductase; Δ4-3-ketosteroid 5β-reductase; Δ4-5β-reductase; Δ4-hydrogenase; 4,5β-dihydrocortisone:NADP+ Δ4-oxidoreductase; 3-oxo-5β-steroid:NADP+ Δ4-oxidoreductase

Systematic name: 5β-cholestan-3-one:NADP+ 4,5-oxidoreductase

Comments: The enzyme from human efficiently catalyses the reduction of progesterone, androstenedione, 17α-hydroxyprogesterone and testosterone to 5β-reduced metabolites; it can also act on aldosterone, corticosterone and cortisol, but to a lesser extent [8]. The bile acid intermediates 7α,12α-dihydroxy-4-cholesten-3-one and 7α-hydroxy-4-cholesten-3-one can also act as substrates [9].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-08-7

References:

1. Forchielli, E. and Dorfman, R.I. Separation of Δ4-5α- and Δ4-5β-hydrogenases from rat liver homogenates. J. Biol. Chem. 223 (1956) 443-448. [PMID: 13376613]

2. Brown-Grant, K., Forchielli, E. and Dorfman, R.I. The Δ4-hydrogenases of guinea pig adrenal gland. J. Biol. Chem. 235 (1960) 1317-1320. [PMID: 13805063]

3. Levy, H.R. and Talalay, P. Enzymatic introduction of double bonds into steroid ring A. J. Am. Chem. Soc. 79 (1957) 2658-2659.

4. Tomkins, G.M. The enzymatic reduction of Δ4-3-ketosteroids. J. Biol. Chem. 225 (1957) 13-24. [PMID: 13416214]

5. Sugimoto, Y., Yoshida, M. and Tamaoki, B. Purification of 5β-reductase from hepatic cytosol fraction of chicken. J. Steroid Biochem. Mol. Biol. 37 (1990) 717-724. [PMID: 2278855]

6. Furuebisu, M., Deguchi, S. and Okuda, K. Identification of cortisone 5β-reductase as Δ4-3-ketosteroid 5β-reductase. Biochim. Biophys. Acta 912 (1987) 110-114. [PMID: 3828348]

7. Okuda, A. and Okuda, K. Purification and characterization of Δ4-3-ketosteroid 5β-reductase. J. Biol. Chem. 259 (1984) 7519-7524. [PMID: 6736016]

8. Charbonneau, A. and The, V.L. Genomic organization of a human 5β-reductase and its pseudogene and substrate selectivity of the expressed enzyme. Biochim. Biophys. Acta 1517 (2001) 228-235. [PMID: 11342103]

9. Kondo, K.H., Kai, M.H., Setoguchi, Y., Eggertsen, G., Sjöblom, P., Setoguchi, T., Okuda, K.I. and Björkhem, I. Cloning and expression of cDNA of human Δ4-3-oxosteroid 5β-reductase and substrate specificity of the expressed enzyme. Eur. J. Biochem. 219 (1994) 357-363. [PMID: 7508385]

[EC 1.3.1.3 created 1961 (EC 1.3.1.23 created 1972, incorporated 2005), modified 2005]

[EC 1.3.1.4 Transferred entry: EC 1.3.1.4, cortisone α-reductase, transferred to EC 1.3.1.22, 3-oxo-5α-steroid 4-dehydrogenase (NADP+) (EC 1.3.1.4 created 1965, deleted 2012)]

EC 1.3.1.5

Accepted name: cucurbitacin Δ23-reductase

Reaction: 23,24-dihydrocucurbitacin B + NAD(P)+ = cucurbitacin B + NAD(P)H + H+

Other name(s): NAD(P)H: cucurbitacin B Δ23-oxidoreductase

Systematic name: 23,24-dihydrocucurbitacin:NAD(P)+ Δ23-oxidoreductase

Comments: Requires Mn2+. Fe2+ or Zn2+ can replace Mn2+ to some extent.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-38-5

References:

1. Schabort, J.C. and Potgieter, D.J.J. Cucurbitacin B Δ23-reductase from Cucurbita maxima. II. Cofactor requirements, enzyme kinetics, substrate specificity and other characteristics. Biochim. Biophys. Acta 151 (1968) 47-53. [PMID: 4384331]

2. Schabort, J.C., Potgieter, D.J.J. and de Villiers, V. Cucurbitacin B Δ23-reductase from Cucurbita maxima. I. Assay methods, isolation and purification. Biochim. Biophys. Acta 151 (1968) 33-46. [PMID: 5640163]

[EC 1.3.1.5 created 1965]

EC 1.3.1.6

Accepted name: fumarate reductase (NADH)

Reaction: succinate + NAD+ = fumarate + NADH + H+

Other name(s): NADH-fumarate reductase; NADH-dependent fumarate reductase; fumarate reductase (NADH2)

Systematic name: succinate:NAD+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9076-99-7

References:

1. Hopgood, M.F. and Walker, D.J. Succinic acid production by rumen bacteria. III. Enzymic studies on the formation of succinate by Ruminococcus flavefaciens. Aust. J. Biol. Sci. 22 (1969) 1413-1424.

[EC 1.3.1.6 created 1972]

EC 1.3.1.7

Accepted name: meso-tartrate dehydrogenase

Reaction: meso-tartrate + NAD+ = dihydroxyfumarate + NADH + H+

Systematic name: meso-tartrate:NAD+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37251-06-2

References:

1. Kohn, L.D. and Jakoby, W.B. L- and mesotartaric acid dehydrogenase (crystalline). Methods Enzymol. 9 (1966) 236-240.

[EC 1.3.1.7 created 1972]

EC 1.3.1.8

Accepted name: acyl-CoA dehydrogenase (NADP+)

Reaction: acyl-CoA + NADP+ = 2,3-dehydroacyl-CoA + NADPH + H+

Other name(s): 2-enoyl-CoA reductase; dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide phosphate); enoyl coenzyme A reductase; crotonyl coenzyme A reductase; crotonyl-CoA reductase; acyl-CoA dehydrogenase (NADP)

Systematic name: acyl-CoA:NADP+ 2-oxidoreductase

Comments: The liver enzyme acts on enoyl-CoA derivatives of carbon chain length 4 to 16, with optimum activity on 2-hexenoyl-CoA. In Escherichia coli, cis-specific and trans-specific enzymes exist [EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) and EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH)].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37251-07-3

References:

1. Dommes, V., Luster, W., Cvetanovic, M. and Kunau, W.-H. Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli. Eur. J. Biochem. 125 (1982) 335-341. [PMID: 6749495]

2. Seubert, W., Lamberts, I., Kramer, R. and Ohly, B. On the mechanism of malonyl-CoA-independent fatty acid synthesis. I. The mechanism of elongation of long-chain fatty acids by acetyl-CoA. Biochim. Biophys. Acta 164 (1968) 498-517. [PMID: 4387390]

[EC 1.3.1.8 created 1972, modified 1986]

EC 1.3.1.9

Accepted name: enoyl-[acyl-carrier-protein] reductase (NADH)

Reaction: an acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+

Other name(s): enoyl-[acyl carrier protein] reductase; enoyl-ACP reductase; NADH-enoyl acyl carrier protein reductase; NADH-specific enoyl-ACP reductase; acyl-[acyl-carrier-protein]:NAD+ oxidoreductase; fabI (gene name); inhA (gene name)

Systematic name: acyl-[acyl-carrier protein]:NAD+ oxidoreductase

Comments: The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18 [3]. The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons [4,5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37251-08-4

References:

1. Shimakata, T. and Stumpf, P.K. Purification and characterizations of β-ketoacyl-[acyl-carrier-protein] reductase, β-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves. Arch. Biochem. Biophys. 218 (1982) 77-91. [PMID: 6756317]

2. Weeks, G. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli. J. Biol. Chem. 243 (1968) 1180-1189. [PMID: 4384650]

3. Yu, X., Liu, T., Zhu, F. and Khosla, C. In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli. Proc. Natl. Acad. Sci. USA 108 (2011) 18643-18648. [PMID: 22042840]

4. Quemard, A., Sacchettini, J.C., Dessen, A., Vilcheze, C., Bittman, R., Jacobs, W.R., Jr. and Blanchard, J.S. Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis. Biochemistry 34 (1995) 8235-8241. [PMID: 7599116]

5. Rozwarski, D.A., Vilcheze, C., Sugantino, M., Bittman, R. and Sacchettini, J.C. Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate. J. Biol. Chem. 274 (1999) 15582-15589. [PMID: 10336454]

[EC 1.3.1.9 created 1972, modified 2013]

EC 1.3.1.10

Accepted name: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

Reaction: an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+

Other name(s): acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl acyl-carrier-protein reductase (ambiguous); enoyl-ACP reductase (ambiguous); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (B-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)

Systematic name: acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Si-specific)

Comments: One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase, an enzyme found in yeasts (Ascomycota and the Basidiomycota). Catalyses the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16. The yeast enzyme is Si-specific with respect to NADP+. cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH), which describes enzymes whose stereo-specificity towards NADPH is not known. See also EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37251-09-5

References:

1. Seyama, T., Kasama, T., Yamakawa, T., Kawaguchi, A., Saito, K. and Okuda, S. Origin of hydrogen atoms in the fatty acids synthesized with yeast fatty acid synthetase. J. Biochem. (Tokyo) 82 (1977) 1325-1329. [PMID: 338601]

[EC 1.3.1.10 created 1972, modified 1986, modified 2013, modified 2014]

EC 1.3.1.11

Accepted name: 2-coumarate reductase

Reaction: 3-(2-hydroxyphenyl)propanoate + NAD+ = 2-coumarate + NADH + H+

Other name(s): melilotate dehydrogenase

Systematic name: 3-(2-hydroxyphenyl)propanoate:NAD+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37251-10-8

References:

1. Levy, C.C. and Weinstein, G.D. The metabolism of coumarin by a microorganism. II. The reduction of o-coumaric acid to melilotic acid. Biochemistry 3 (1964) 1944-1947.

[EC 1.3.1.11 created 1972]

EC 1.3.1.12

Accepted name: prephenate dehydrogenase

Reaction: prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH

For diagram click here.

Other name(s): hydroxyphenylpyruvate synthase; chorismate mutase—prephenate dehydrogenase

Systematic name: prephenate:NAD+ oxidoreductase (decarboxylating)

Comments: This enzyme in the enteric bacteria also possesses chorismate mutase activity (EC 5.4.99.5 chorismate mutase) and converts chorismate into prephenate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9044-92-2

References:

1. Koch, G.L.E., Shaw, D.C. and Gibson, F. Tyrosine biosynthesis in Aerobacter aerogenes. Purification and properties of chorismate mutase-prephenate dehydrogenase. Biochim. Biophys. Acta 212 (1970) 375-386. [PMID: 5456988]

[EC 1.3.1.12 created 1972]

EC 1.3.1.13

Accepted name: prephenate dehydrogenase (NADP+)

Reaction: prephenate + NADP+ = 4-hydroxyphenylpyruvate + CO2 + NADPH

For diagram click here.

Other name(s): prephenate dehydrogenase; prephenate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; prephenate dehydrogenase (NADP)

Systematic name: prephenate:NADP+ oxidoreductase (decarboxylating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37251-11-9

References:

1. Gamborg, O.L. and Keeley, F.W. Aromatic metabolism in plants. I. A study of the prephenate dehydrogenase from bean plants. Biochim. Biophys. Acta 115 (1966) 65-72. [PMID: 4379953]

[EC 1.3.1.13 created 1972]

EC 1.3.1.14

Accepted name: dihydroorotate dehydrogenase (NAD+)

Reaction: (S)-dihydroorotate + NAD+ = orotate + NADH + H+

Other name(s): orotate reductase (NADH); orotate reductase (NADH2); DHOdehase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); dihydroorotate oxidase, pyrD (gene name)

Systematic name: (S)-dihydroorotate:NAD+ oxidoreductase

Comments: Binds FMN, FAD and a [2Fe-2S] cluster. The enzyme consists of two subunits, an FMN binding catalytic subunit and a FAD and iron-sulfur binding electron transfer subunit [4]. The reaction, which takes place in the cytosol, is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NADP+ (EC 1.3.1.15) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37255-26-8

References:

1. Friedmann, H.C. and Vennesland, B. Purification and properties of dihydroorotic acid dehydrogenase. J. Biol. Chem. 233 (1958) 1398-1406. [PMID: 13610849]

2. Friedmann, H.C. and Vennesland, B. Crystalline dihydroorotic dehydrogenase. J. Biol. Chem. 235 (1960) 1526-1532. [PMID: 13825167]

3. Lieberman, I. and Kornberg, A. Enzymic synthesis and breakdown of a pyrimidine, orotic acid. I. Dihydro-orotic dehydrogenase. Biochim. Biophys. Acta 12 (1953) 223-234. [PMID: 13115431]

4. Nielsen, F.S., Andersen, P.S. and Jensen, K.F. The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers. J. Biol. Chem. 271 (1996) 29359-29365. [PMID: 8910599]

5. Rowland, P., Nørager, S., Jensen, K.F. and Larsen, S. Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster. Structure 8 (2000) 1227-1238. [PMID: 11188687]

6. Kahler, A.E., Nielsen, F.S. and Switzer, R.L. Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits. Arch. Biochem. Biophys. 371 (1999) 191-201. [PMID: 10545205]

7. Marcinkeviciene, J., Tinney, L.M., Wang, K.H., Rogers, M.J. and Copeland, R.A. Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism. Biochemistry 38 (1999) 13129-13137. [PMID: 10529184]

[EC 1.3.1.14 created 1972, modified 2011]

EC 1.3.1.15

Accepted name: dihydroorotate dehydrogenase (NADP+)

Reaction: (S)-dihydroorotate + NADP+ = orotate + NADPH + H+

Other name(s): orotate reductase; dihydro-orotic dehydrogenase; L-5,6-dihydro-orotate:NAD+ oxidoreductase; orotate reductase (NADPH)

Systematic name: (S)-dihydroorotate:NADP+ oxidoreductase

Comments: Binds FMN and FAD [2]. Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NAD+ (EC 1.3.1.14) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor .

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-27-9

References:

1. Taylor, W.H., Taylor, M.L. and Eames, D.F. Two functionally different dihydroorotic dehydrogenases in bacteria. J. Bacteriol. 91 (1966) 2251-2256. [PMID: 4380263]

2. Udaka, S. and Vennesland, B. Properties of triphosphopyridine nucleotide-linked dihydroorotic dehydrogenase. J. Biol. Chem. 237 (1962) 2018-2024. [PMID: 13923427]

[EC 1.3.1.15 created 1972, modified 2011]

EC 1.3.1.16

Accepted name: β-nitroacrylate reductase

Reaction: 3-nitropropanoate + NADP+ = 3-nitroacrylate + NADPH + H+

Systematic name: 3-nitropropanoate:NADP+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-28-0

References:

1. Shaw, P.D. Biosynthesis of nitro compounds. III. The enzymatic reduction of β-nitroacrylic acid to β-nitropropionic acid. Biochemistry 6 (1967) 2253-2260.

[EC 1.3.1.16 created 1972]

EC 1.3.1.17

Accepted name: 3-methyleneoxindole reductase

Reaction: 3-methyl-1,3-dihydroindol-2-one + NADP+ = 3-methylene-1,3-dihydro-2H-indol-2-one + NADPH + H+

Other name(s): 3-methyloxindole:NADP+ oxidoreductase

Systematic name: 3-methyl-1,3-dihydroindol-2-one:NADP+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-29-1

References:

1. Moyed, H.S. and Williamson, V. Multiple 3-methyleneoxindole reductases of peas, differential inhibition by synthetic auxins. J. Biol. Chem. 242 (1967) 1075-1077. [PMID: 6021071]

[EC 1.3.1.17 created 1972]

EC 1.3.1.18

Accepted name: kynurenate-7,8-dihydrodiol dehydrogenase

Reaction: 7,8-dihydro-7,8-dihydroxykynurenate + NAD+ = 7,8-dihydroxykynurenate + NADH + H+

Other name(s): 7,8-dihydro-7,8-dihydroxykynurenate dehydrogenase; 7,8-dihydroxykynurenic acid 7,8-diol dehydrogenase

Systematic name: 7,8-dihydro-7,8-dihydroxykynurenate:NAD+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-30-4

References:

1. Taniuchi, H. and Hayaishi, O. Studies on the metabolism of kynurenic acid. III. Enzymatic formation of 7,8-dihydroxykynurenic acid from kynurenic acid. J. Biol. Chem. 238 (1963) 283-293.

[EC 1.3.1.18 created 1972]

EC 1.3.1.19

Accepted name: cis-1,2-dihydrobenzene-1,2-diol dehydrogenase

Reaction: cis-1,2-dihydrobenzene-1,2-diol + NAD+ = catechol + NADH + H+

Other name(s): cis-benzene glycol dehydrogenase; cis-1,2-dihydrocyclohexa-3,5-diene (nicotinamide adenine dinucleotide) oxidoreductase;

Systematic name: cis-1,2-dihydrobenzene-1,2-diol:NAD+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 51923-03-6

References:

1. Axcell, B.C. and Geary, P.J. The metabolism of benzene by bacteria. Purification and some properties of the enzyme cis-1,2-dihydroxycyclohexa-3,5-diene (nicotinamide adenine dinucleotide) oxidoreductase (cis-benzene glycol dehydrogenase). Biochem. J. 136 (1973) 927-934. [PMID: 4362337]

2. Gibson, D.T., Koch, J.R. and Kallio, R.E. Oxidative degradation of aromatic hydrocarbons by microorganisms. I. Enzymatic formation of catechol from benzene. Biochemistry 7 (1968) 2653-2662. [PMID: 4298226]

[EC 1.3.1.19 created 1972]

EC 1.3.1.20

Accepted name: trans-1,2-dihydrobenzene-1,2-diol dehydrogenase

Reaction: trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+

Other name(s): dihydrodiol dehydrogenase

Systematic name: trans-1,2-dihydrobenzene-1,2-diol:NADP+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37255-32-6

References:

1. Ayengar, P.K., Hayaishi, O., Nakajima, M. and Tomida, I. Enzymic aromatization of 3,5-cyclohexadiene-1,2-diol. Biochim. Biophys. Acta 33 (1959) 111-119.

[EC 1.3.1.20 created 1972]

Accepted name: 7-dehydrocholesterol reductase

Reaction: cholesterol + NADP+ = cholesta-5,7-dien-3β-ol + NADPH + H+

For diagram of reaction click here.

Other name(s): DAF-36 (gene name); DHCR7 (gene name); 7-DHC reductase; 7-dehydrocholesterol dehydrogenase/cholesterol oxidase; Δ7-sterol reductase

Systematic name: cholesterol:NADP+ Δ7-oxidoreductase

Comments: The enzyme is part of the cholesterol biosynthesis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9080-21-1

References:

1. Dempsey, M.E., Seaton, J.D., Schroepfer, G.J. and Trockman, R.W. The intermediary role of Δ5,7-cholestadien-3β-ol in cholesterol biosynthesis. J. Biol. Chem. 239 (1964) 1381-1387. [PMID: 14189869]

2. Moebius, F.F., Fitzky, B.U., Lee, J.N., Paik, Y.K. and Glossmann, H. Molecular cloning and expression of the human Δ7-sterol reductase. Proc. Natl. Acad. Sci. USA 95 (1998) 1899-1902. [PMID: 9465114]

[EC 1.3.1.21 created 1972, modified 2013]

EC 1.3.1.22

Accepted name: 3-oxo-5α-steroid 4-dehydrogenase (NADP+)

Reaction: a 3-oxo-5α-steroid + NADP+ = a 3-oxo-Δ4-steroid + NADPH + H+

Other name(s): cholestenone 5α-reductase; testosterone Δ4-5α-reductase; steroid 5α-reductase; 3-oxosteroid Δ4-dehydrogenase; 5α-reductase; steroid 5α-hydrogenase; 3-oxosteroid 5α-reductase; testosterone Δ4-hydrogenase; 4-ene-3-oxosteroid 5α-reductase; reduced nicotinamide adenine dinucleotide phosphate:Δ4-3-ketosteroid 5α-oxidoreductase; 4-ene-5α-reductase; Δ4-3-ketosteroid 5α-oxidoreductase; cholest-4-en-3-one 5α-reductase; testosterone 5α-reductase; 3-oxo-5α-steroid 4-dehydrogenase

Systematic name: 3-oxo-5α-steroid:NADP+ Δ4-oxidoreductase

Comments: The enzyme catalyses the conversion of assorted 3-oxo-Δ4 steroids into their corresponding 5α form. Substrates for the mammalian enzyme include testosterone, progesterone, and corticosterone. Substrates for the plant enzyme are brassinosteroids such as campest-4-en-3-one and (22α)-hydroxy-campest-4-en-3-one. cf. EC 1.3.99.5, 3-oxo-5α-steroid 4-dehydrogenase (acceptor).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-34-8

References:

1. Levy, H.R. and Talalay, P. Bacterial oxidation of steroids. II. Studies on the enzymatic mechanisms of ring A dehydrogenation. J. Biol. Chem. 234 (1959) 2014-2021. [PMID: 13673006]

2. Shefer, S., Hauser, S. and Mosbach, E.H. Studies on the biosynthesis of 5α-cholestan-3β-ol. I. Cholestenone 5α-reductase of rat liver. J. Biol. Chem. 241 (1966) 946-952. [PMID: 5907469]

3. Cheng, Y.-J. and Karavolas, H.J. Properties and subcellular distribution of Δ4-steroid (progesterone) 5α-reductase in rat anterior pituitary. Steroids 26 (1975) 57-71. [PMID: 1166484]

4. Sargent, N.S. and Habib, F.K. Partial purification of human prostatic 5α-reductase (3-oxo-5α-steroid:NADP+ 4-ene-oxido-reductase; EC 1.3.1.22) in a stable and active form. J. Steroid Biochem. Mol. Biol. 38 (1991) 73-77. [PMID: 1705142]

5. Quemener, E., Amet, Y., di Stefano, S., Fournier, G., Floch, H.H. and Abalain, J.H. Purification of testosterone 5α-reductase from human prostate by a four-step chromatographic procedure. Steroids 59 (1994) 712-718. [PMID: 7900170]

6. Poletti, A., Celotti, F., Rumio, C., Rabuffetti, M. and Martini, L. Identification of type 1 5α-reductase in myelin membranes of male and female rat brain. Mol. Cell. Endocrinol. 129 (1997) 181-190. [PMID: 9202401]

7. Li, J., Biswas, M.G., Chao, A., Russell, D.W. and Chory, J. Conservation of function between mammalian and plant steroid 5α-reductases. Proc. Natl. Acad. Sci. USA 94 (1997) 3554-3559. [PMID: 9108014]

8. Rosati, F., Bardazzi, I., De Blasi, P., Simi, L., Scarpi, D., Guarna, A., Serio, M., Racchi, M.L. and Danza, G. 5α-Reductase activity in Lycopersicon esculentum: cloning and functional characterization of LeDET2 and evidence of the presence of two isoenzymes. J. Steroid Biochem. Mol. Biol. 96 (2005) 287-299. [PMID: 15993049]

[EC 1.3.1.22 created 1972, modified 2012]

[EC 1.3.1.23 Deleted entry: cholestenone β-reductase. The enzyme is identical to EC 1.3.1.3, Δ4-3-oxosteroid 5β-reductase. (EC 1.3.1.23 created 1972, deleted 2005)]

EC 1.3.1.24

Accepted name: biliverdin reductase

Reaction: bilirubin + NAD(P)+ = biliverdin + NAD(P)H + H+

For diagram click here.

Systematic name: bilirubin:NAD(P)+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9074-10-6

References:

1. Singleton, J.W. and Laster, L. Biliverdin reductase of guinea pig liver. J. Biol. Chem. 240 (1965) 4780-4789. [PMID: 4378982]

[EC 1.3.1.24 created 1972]

EC 1.3.1.25

Accepted name: 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase

Reaction: (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ = catechol + CO2 + NADH + H+

For diagram click here.

Other name(s): 3,5-cyclohexadiene-1,2-diol-1-carboxylate dehydrogenase; 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase; dihydrodihydroxybenzoate dehydrogenase; DHBDH; cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase; 2-hydro-1,2-dihydroxybenzoate dehydrogenase; cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate:NAD+ oxidoreductase; dihydrodihydroxybenzoate dehydrogenase

Systematic name: (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 60496-16-4

References:

1. Reiner, A.M. Metabolism of aromatic compounds in bacteria. Purification and properties of the catechol-forming enzyme, 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid (NAD+) oxidoreductase (decarboxylating). J. Biol. Chem. 247 (1972) 4960-4965. [PMID: 4341530]

2. Neidle, E.L., Hartnett, C., Ornston, N.L., Bairoch, A., Rekik, M. and Harayama, S. cis-Diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 204 (1992) 113-120. [PMID: 1740120]

[EC 1.3.1.25 created 1976, modified 2004 (EC 1.3.1.55 created 1999, incorporated 2004)]

[EC 1.3.1.26 Transferred entry: dihydrodipicolinate reductase. Now EC 1.17.1.8, 4-hydroxy-tetrahydrodipicolinate reductase. (EC 1.3.1.26 created 1976, modified 2011, deleted 2013)]

EC 1.3.1.27

Accepted name: 2-hexadecenal reductase

Reaction: hexadecanal + NADP+ = 2-trans-hexadecenal + NADPH + H+

Other name(s): 2-alkenal reductase; hexadecanal: NADP+ oxidoreductase

Systematic name: hexadecanal:NADP+ Δ2-oxidoreductase

Comments: Specific for long chain 2-trans- and 2-cis-alkenals, with chain length optimum around 14 to 16 carbon atoms.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52227-95-9

References:

1. Stoffel, W. and Därr, W. 2-Alkenal reductase isolation, properties and specificities. Hoppe-Seyler's Z. Physiol. Chem. 355 (1974) 54-60. [PMID: 4154890]

[EC 1.3.1.27 created 1976]

EC 1.3.1.28

Accepted name: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase

Reaction: (2S,3S)-2,3-dihydro-2,3-dihydroxybenzoate + NAD+ = 2,3-dihydroxybenzoate + NADH + H+

For diagram of reaction, click here.

Other name(s): 2,3-DHB dehydrogenase; 2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase

Systematic name: (2S,3S)-2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase

Comments: Formerly EC 1.1.1.109.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-40-1

References:

1. Young, I.G. and Gibson, F. Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli. Biochim. Biophys. Acta 177 (1969) 401-411. [PMID: 4306838]

[EC 1.3.1.28 created 1972 as EC 1.1.1.109, transferred 1976 to EC 1.3.1.28]

EC 1.3.1.29

Accepted name: cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase

Reaction: (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ = naphthalene-1,2-diol + NADH + H+

For diagram of reaction click here.

Other name(s): (+)-cis-naphthalene dihydrodiol dehydrogenase; naphthalene dihydrodiol dehydrogenase; cis-dihydrodiol naphthalene dehydrogenase; cis-1,2-dihydronaphthalene-1,2-diol:NAD+ 1,2-oxidoreductase

Systematic name: (1R,2S)-1,2-dihydronaphthalene-1,2-diol:NAD+ 1,2-oxidoreductase

Comments: Also acts, at half the rate, on cis-anthracene dihydrodiol and cis-phenanthrene dihydrodiol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 53986-49-5

References:

1. Patel, T.R. and Gibson, D.T. Purification and properties of (+)-cis-naphthalene dihydrodiol dehydrogenase of Pseudomonas putida. J. Bacteriol. 119 (1974) 879-888. [PMID: 4369091]

[EC 1.3.1.29 created 1976]

[EC 1.3.1.30 Transferred entry: EC 1.3.1.30, progesterone 5α-reductase, transferred to EC 1.3.1.22, 3-oxo-5α-steroid 4-dehydrogenase (NADP+). (EC 1.3.1.30 created 1978, deleted 2012)]

EC 1.3.1.31

Accepted name: 2-enoate reductase

Reaction: butanoate + NAD+ = but-2-enoate + NADH + H+

Other name(s): enoate reductase

Systematic name: butanoate:NAD+ Δ2-oxidoreductase

Comments: An iron-sulfur-flavoprotein (FAD). Acts (in the reverse direction) on a wide range of alkyl and aryl αβ-unsaturated carboxylate ions; but-2-enoate was the best substrate tested.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 70712-51-5

References:

1. Tischer, W., Bader, J. and Simon, H. Purification and some properties of a hitherto-unknown enzyme reducing the carbon-carbon double bond of α,β-unsaturated carboxylate anions. Eur. J. Biochem. 97 (1979) 103-112. [PMID: 477658]

[EC 1.3.1.31 created 1982]

EC 1.3.1.32

Accepted name: maleylacetate reductase

Reaction: 3-oxoadipate + NAD(P)+ = 2-maleylacetate + NAD(P)H + H+

For diagram of reaction click here.

Other name(s): maleoylacetate reductase

Systematic name: 3-oxoadipate:NAD(P)+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 69669-65-4

References:

1. Gaal, A.B. and Neujahr, H.Y. Maleylacetate reductase from Trichosporon cutaneum. Biochem. J. 185 (1980) 783-786.

2. Gaal, A.B. and Neujahr, H.Y. Induction of phenol-metabolizing enzymes in Trichosporon cutaneum. Arch. Microbiol. 130 (1981) 54-58.

[EC 1.3.1.32 created 1983]

EC 1.3.1.33

Accepted name: protochlorophyllide reductase

Reaction: chlorophyllide a + NADP+ = protochlorophyllide + NADPH + H+

For diagram of reaction click here.

Other name(s): NADPH2-protochlorophyllide oxidoreductase; NADPH—protochlorophyllide oxidoreductase; NADPH-protochlorophyllide reductase; protochlorophyllide oxidoreductase; protochlorophyllide photooxidoreductase; light-dependent protochlorophyllide reductase

Systematic name: chlorophyllide-a:NADP+ 7,8-oxidoreductase

Comments: The enzyme catalyses a light-dependent trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 68518-04-7

References:

1. Apel, K., Santel, H.-J., Redlinger, T.E. and Falk, H. The protochlorophyllide holochrome of barley (Hordeum vulgare L.). Isolation and characterization of the NADPH:protochlorophyllide oxidoreductase. Eur. J. Biochem. 111 (1980) 251-258. [PMID: 7439188]

2. Griffiths, W.T. Reconstitution of chlorophyllide formation by isolated etioplast membranes. Biochem. J. 174 (1978) 681-692. [PMID: 31865]

[EC 1.3.1.33 created 1984]

EC 1.3.1.34

Accepted name: 2,4-dienoyl-CoA reductase (NADPH)

Reaction: trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH + H+

Other name(s): 4-enoyl-CoA reductase (NADPH2); 4-enoyl coenzyme A (reduced nicotinamide adenine dinucleotide phosphate) reductase; 4-enoyl-CoA reductase; 2,4-dienoyl-CoA reductase (NADPH2)

Systematic name: trans-2,3-didehydroacyl-CoA:NADP+ 4-oxidoreductase

Comments: Best substrates for reduction contain a 2,4-diene structure with a chain-length of 8 or 10

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 82869-38-3

References:

1. Dommes, V., Luster, W., Cvetanovic, M. and Kunau, W.-H. Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli. Eur. J. Biochem. 125 (1982) 335-341. [PMID: 6749495]

2. Kunau, W.-H. and Dommes, P. Degradation of unsaturated fatty acids. Identification of intermediates in the degradation of cis-4-decenoly-CoA by extracts of beef-liver mitochondria. Eur. J. Biochem. 91 (1978) 533-544. [PMID: 729581]

[EC 1.3.1.34 created 1984, modified 1986]

[EC 1.3.1.35 Transferred entry: phosphatidylcholine desaturase. Now EC 1.14.19.22, microsomal oleoyl-lipid 12-desaturase (EC 1.3.1.35 created 1984, deleted 2015)]

EC 1.3.1.36

Accepted name: geissoschizine dehydrogenase

Reaction: geissoschizine + NADP+ = 4,21-didehydrogeissoschizine + NADPH

For diagram click here.

Systematic name: geissoschizine:NADP+ 4,21-oxidoreductase

Comments: Involved in the interconversion of heteroyohimbine alkaloids in Catharanthus roseus.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 84399-94-0

References:

1. Pfitzner, A. and Stöckigt, J. Partial-purification and characterization of geissoschizine dehydrogenase from suspension-cultures of Catharanthus roseus. Phytochemistry 21 (1982) 1585-1588.

[EC 1.3.1.36 created 1986]

EC 1.3.1.37

Accepted name: cis-2-enoyl-CoA reductase (NADPH)

Reaction: acyl-CoA + NADP+ = cis-2,3-dehydroacyl-CoA + NADPH + H+

Other name(s): NADPH-dependent cis-enoyl-CoA reductase; reductase, cis-2-enoyl coenzyme A; cis-2-enoyl-coenzyme A reductase; cis-2-enoyl-CoA reductase (NADPH2)

Systematic name: acyl-CoA:NADP+ cis-2-oxidoreductase

Comments: Not identical with EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH) [cf. EC 1.3.1.8 acyl-CoA dehydrogenase (NADP+)].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72841-00-0

References:

1. Mizugaki, M., Nishimaki, T., Shiraishi, T., Kawaguchi, A., Okuda, S. and Yamanaka, H. Studies on the metabolism of unsaturated fatty acids. IX. Stereochemical studies of the reaction catalyzed by trans-2-enoyl-coenzyme A reductase of Escherichia coli. J. Biochem. (Tokyo) 92 (1982) 1649-1654. [PMID: 6759504]

[EC 1.3.1.37 created 1986]

EC 1.3.1.38

Accepted name: trans-2-enoyl-CoA reductase (NADPH)

Reaction: acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+

Other name(s): NADPH-dependent trans-2-enoyl-CoA reductase; reductase, trans-enoyl coenzyme A; trans-2-enoyl-CoA reductase (NADPH2)

Systematic name: acyl-CoA:NADP+ trans-2-oxidoreductase

Comments: Not identical with EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) [cf. EC 1.3.1.8 acyl-CoA dehydrogenase (NADP+)].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 77649-64-0

References:

1. Mizugaki, M., Nishimaki, T., Shiraishi, T., Kawaguchi, A., Okuda, S. and Yamanaka, H. Studies on the metabolism of unsaturated fatty acids. IX. Stereochemical studies of the reaction catalyzed by trans-2-enoyl-coenzyme A reductase of Escherichia coli. J. Biochem. (Tokyo) 92 (1982) 1649-1654. [PMID: 6759504]

[EC 1.3.1.38 created 1986]

EC 1.3.1.39

Accepted name: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)

Reaction: an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+

Other name(s): acyl-ACP dehydrogenase; enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACp reductase; enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific); fabL (gene name); enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (A-specific)

Systematic name: acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Re-specific)

Comments: This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is also one of the activities of EC 2.3.1.85, animal fatty-acid synthase. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH) and EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Dugan, R.E., Slakey, L.L. and Porter, L.W. Stereospecificity of the transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate to the acyl chain in the dehydrogenase-catalyzed reactions of fatty acid synthesis. J. Biol. Chem. 245 (1970) 6312-6316. [PMID: 4394955]

2. Carlisle-Moore, L., Gordon, C.R., Machutta, C.A., Miller, W.T. and Tonge, P.J. Substrate recognition by the human fatty-acid synthase. J. Biol. Chem. 280 (2005) 42612-42618. [PMID: 16215233]

3. Heath, R.J., Su, N., Murphy, C.K. and Rock, C.O. The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis. J. Biol. Chem. 275 (2000) 40128-40133. [PMID: 11007778]

4. Kim, K.H., Ha, B.H., Kim, S.J., Hong, S.K., Hwang, K.Y. and Kim, E.E. Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis. J. Mol. Biol. 406 (2011) 403-415. [PMID: 21185310]

[EC 1.3.1.39 created 1986, modified 2013]

EC 1.3.1.40

Accepted name: 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate reductase

Reaction: 2,6-dioxo-6-phenylhexanoate + NADP+ = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + NADPH + H+

Other name(s): 2-hydroxy-6-oxo-phenylhexa-2,4-dienoate (reduced nicotinamide adenine dinucleotide phosphate) reductase

Systematic name: 2,6-dioxo-6-phenylhexanoate:NADP+ Δ2-oxidoreductase

Comments: Broad specificity; reduces a number of compounds produced by Pseudomonas from aromatic hydrocarbons by ring fission.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 104645-83-2

References:

1. Omori, T., Ishigooka, H. and Minoda, Y. Purification and some properties of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid(HOPDA) reducing enzyme from Pseudomonas cruciviae S93B1 involved in the degradation of biphenyl. Agric. Biol. Chem. 50 (1986) 1513-1518.

[EC 1.3.1.40 created 1989]

EC 1.3.1.41

Accepted name: xanthommatin reductase

Reaction: 5,12-dihydroxanthommatin + NAD+ = xanthommatin + NADH + H+

Systematic name: 5,12-dihydroxanthommatin:NAD+ oxidoreductase

Comments: From Drosophila melanogaster.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62972-27-4

References:

1. Santoro, P. and Parisi, G. A new enzyme from Drosophila melanogaster - in vitro conversion of xanthommatin into its dihydroform by means of xanthommatin reductase. J. Exp. Zool. 239 (1986) 169-173.

[EC 1.3.1.41 created 1989]

EC 1.3.1.42

Accepted name: 12-oxophytodienoate reductase

Reaction: 8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate + NADP+ = (15Z)-12-oxophyto-10,15-dienoate + NADPH + H+

Other name(s): 12-oxo-phytodienoic acid reductase

Systematic name: 8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate:NADP+ 4-oxidoreductase

Comments: Involved in the conversion of linolenate into jasmonate in Zea mays.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 101150-03-2

References:

1. Vick, B.A. and Zimmerman, D.C. Characterization of 12-oxo-phytodienoic acid reductase in corn - the jasmonic acid pathway. Plant Physiol. 80 (1986) 202-205.

[EC 1.3.1.42 created 1989]

EC 1.3.1.43

Accepted name: arogenate dehydrogenase

Reaction: L-arogenate + NAD+ = L-tyrosine + NADH + CO2

For diagram of reaction click here.

Glossary: L-arogenate = 1-[(2S)-2-amino-2-carboxyethyl]-4-hydroxycyclohexa-2,5-diene-1-carboxylate

Other name(s): arogenic dehydrogenase (ambiguous); cyclohexadienyl dehydrogenase; pretyrosine dehydrogenase (ambiguous); L-arogenate:NAD+ oxidoreductase; arogenate dehydrogenase (NAD+)

Systematic name: L-arogenate:NAD+ oxidoreductase (decarboxylating)

Comments: Arogenate dehydrogenases may utilize NAD+ (EC 1.3.1.43), NADP+ (EC 1.3.1.78), or both (EC 1.3.1.79). NAD+-specific enzymes have been reported from some bacteria [2] and plants [3]. Some enzymes also possess the activity of EC 1.3.1.12, prephenate dehydrogenase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64295-75-6

References:

1. Stenmark, S.L., Pierson, D.L., Jensen, R.A. and Glover, G.I. Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway. Nature 247 (1974) 290-292. [PMID: 4206476]

2. Byng, G.S., Whitaker, R.J., Gherna, R.L. and Jensen, R.A. Variable enzymological patterning in tyrosine biosynthesis as a means of determining natural relatedness among the Pseudomonadaceae. J. Bacteriol. 144 (1980) 247-257. [PMID: 7419490]

3. Byng, G., Whitaker, R., Flick, C. and Jensen, R.A. Enzymology of L-tyrosine biosynthesis in corn (Zea mays). Phytochemistry 20 (1981) 1289-1292.

4. Mayer, E., Waldner-Sander, S., Keller, B., Keller, E. and Lingens, F. Purification of arogenate dehydrogenase from Phenylobacterium immobile. FEBS Lett. 179 (1985) 208-212. [PMID: 3967752]

5. Lingens, F., Keller, E. and Keller, B. Arogenate dehydrogenase from Phenylobacterium immobile. Methods Enzymol. 142 (1987) 513-518.

6. Zamir, L.O., Tiberio, R., Devor, K.A., Sauriol, F., Ahmad, S. and Jensen, R.A. Structure of D-prephenyllactate. A carboxycyclohexadienyl metabolite from Neurospora crassa. J. Biol. Chem. 263 (1988) 17284-17290. [PMID: 2972718]

[EC 1.3.1.43 created 1989, modified 2003, modified 2005, modified 2015]

EC 1.3.1.44

Accepted name: trans-2-enoyl-CoA reductase (NAD+)

Reaction: acyl-CoA + NAD+ = trans-didehydroacyl-CoA + NADH + H+

Other name(s): trans-2-enoyl-CoA reductase (NAD)

Systematic name: acyl-CoA:NAD+ trans-2-oxidoreductase

Comments: The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 77649-64-0

References:

1. Inui, H., Miyatake, K., Nakano, Y. and Kitaoka, S. Purification and some properties of short chain-length specific trans-2-enoyl-CoA reductase in mitochondria of Euglena gracilis. J. Biochem. (Tokyo) 100 (1986) 995-1000. [PMID: 3102464]

[EC 1.3.1.44 created 1989]

EC 1.3.1.45

Accepted name: 2'-hydroxyisoflavone reductase

Reaction: vestitone + NADP+ = 2'-hydroxyformononetin + NADPH + H+

For diagram click here.

Other name(s): NADPH:2'-hydroxyisoflavone oxidoreductase; isoflavone reductase; 2',7-dihydroxy-4',5'-methylenedioxyisoflavone reductase

Systematic name: vestitone:NADP+ oxidoreductase

Comments: In the reverse reaction, a 2'-hydroxyisoflavone is reduced to an isoflavanone; 2'-hydroxypseudobaptigenin also acts. Involved in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 128449-69-4

References:

1. Tiemann, K., Hinderer, W. and Barz, W. Isolation of NADPH:isoflavone oxidoreductase, a new enzyme of pterocarpan biosynthesis in cell suspensions of Cicer arietinum. FEBS Lett. 213 (1987) 324-328.

[EC 1.3.1.45 created 1990]

EC 1.3.1.46

Accepted name: biochanin-A reductase

Reaction: dihydrobiochanin A + NADP+ = biochanin A + NADPH + H+

For diagram click here.

Systematic name: dihydrobiochanin-A:NADP+ Δ2-oxidoreductase

Comments: Some other isoflavones are reduced to the corresponding isoflavanones.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 112198-90-0

References:

1. Tiemann, K., Hinderer, W. and Barz, W. Isolation of NADPH-isoflavone oxidoreductase, a new enzyme of pterocarpan phytoalexin biosynthesis in cell-suspension cultures of Cicer arietinum. FEBS Lett. 213 (1987) 324-328.

[EC 1.3.1.46 created 1990]

EC 1.3.1.47

Accepted name: α-santonin 1,2-reductase

Reaction: 1,2-dihydrosantonin + NAD(P)+ = α-santonin + NAD(P)H + H+

Systematic name: 1,2-dihydrosantonin:NAD(P)+ 1,2-oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 111070-23-6

References:

1. Naik, U. and Mavuinkurve, S. α-Santonin 1,2-reductase and its role in the formation of dihydrosantonin and lumisantonin by Pseudomonas cichorii S. Can. J. Microbiol. 33 (1987) 658-662. [PMID: 3690421]

[EC 1.3.1.47 created 1990]

EC 1.3.1.48

Accepted name: 13,14-dehydro-15-oxoprostaglandin 13-reductase

Reaction: 11α-hydroxy-9,15-dioxoprostanoate + NAD(P)+ = (13E)-11α-hydroxy-9,15-dioxoprost-13-enoate + NAD(P)H + H+

Other name(s): 15-oxo-Δ13-prostaglandin reductase; Δ13-15-ketoprostaglandin reductase; 15-ketoprostaglandin Δ13-reductase; prostaglandin Δ13-reductase; prostaglandin 13-reductase; (5Z)-(15S)-11α-hydroxy-9,15-dioxoprostanoate:NAD(P)+ Δ13-oxidoreductase; (5Z)-11α-hydroxy-9,15-dioxoprost-5-enoate:NAD(P)+ Δ13-oxidoreductase

Systematic name: 11α-hydroxy-9,15-dioxoprostanoate:NAD(P)+ Δ13-oxidoreductase

Comments: Reduces 13,14-dehydro-15-oxoprostaglandins to 13,14-dihydro derivatives. The enzyme from placenta is specific for NAD+.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 57406-74-3

References:

1. Hansen, H.S. Purification and assay of 15-ketoprostaglandin Δ13-reductase from bovine lung. Methods Enzymol. 86 (1982) 156-163. [PMID: 6290839]

2. Jarabak, J. Isolation and properties of a 15-ketoprostaglandin Δ13-reductase from human placenta. Methods Enzymol. 86 (1982) 163-167. [PMID: 7132753]

[EC 1.3.1.48 created 1990, modified 2014]

EC 1.3.1.49

Accepted name: cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase

Reaction: (+)-cis-3,4-dihydrophenanthrene-3,4-diol + NAD+ = phenanthrene-3,4-diol + NADH + H+

Systematic name: (+)-cis-3,4-dihydrophenanthrene-3,4-diol:NAD+ 3,4-oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 118390-61-7

References:

1. Nagao, K., Takizawa, N. and Kiyahara, H. Purification and properties of cis-phenanthrene dihydrodiol dehydrogenase in Alcaligenes faecalis AFK2. Agric. Biol. Chem. 52 (1988) 2621-2623.

[EC 1.3.1.49 created 1992]

[EC 1.3.1.50 Deleted entry: tetrahydroxynaphthalene reductase. Now EC 1.1.1.252 tetrahydroxynaphthalene reductase (EC 1.3.1.50 created 1992, deleted 1999)]


Continued with EC 1.3.1.51 to EC 1.3.1.111
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