| 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 of benzoate metabolism, 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; (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating) |
| Systematic name: |
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating) |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, 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., Hartnett, C., Ornston, L.N., 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. [DOI] [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 shikimate and chorismate biosynthesis, 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 |
| Links to other databases: |
BRENDA, EXPASY, Gene, 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. [DOI] [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 naphthalene metabolism, 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, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, 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, Gene, 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. [DOI] [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 4-nitrophenol metabolism, click here |
| Other name(s): |
maleolylacetate reductase |
| Systematic name: |
3-oxoadipate:NAD(P)+ oxidoreductase |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, 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. [PMID: 7387635] |
| 2. |
Gaal, A.B. and Neujahr, H.Y. Induction of phenol-metabolizing enzymes in Trichosporon cutaneum. Arch. Microbiol. 130 (1981) 54–58. [PMID: 7305599] |
|
| [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 chlorophyll biosynthesis (later stages), click here |
| Other name(s): |
NADPH2-protochlorophyllide oxidoreductase; NADPH-protochlorophyllide oxidoreductase; NADPH-protochlorophyllide reductase; protochlorophyllide oxidoreductase (ambiguous); 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, Gene, KEGG, MetaCyc, PDB, 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. [DOI] [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 [(2E)-enoyl-CoA-producing] |
| Reaction: |
(1) a (2E)-2-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+
(2) a (2E)-2-enoyl-CoA + NADP+ = a (2E,4Z)-2,4-dienoyl-CoA + NADPH + H+ |
| Other name(s): |
fadH (gene name); 4-enoyl-CoA reductase (NADPH) (ambiguous); 4-enoyl coenzyme A (reduced nicotinamide adenine dinucleotide phosphate) reductase (ambiguous); 4-enoyl-CoA reductase (ambiguous); 2,4-dienoyl-CoA reductase (NADPH) (ambiguous); trans-2,3-didehydroacyl-CoA:NADP+ 4-oxidoreductase |
| Systematic name: |
(2E)-2-enoyl-CoA:NADP+ 4-oxidoreductase |
| Comments: |
This bacterial enzyme catalyses the reduction of either (2E,4E)-2,4-dienoyl-CoA or (2E,4Z)-2,4-dienoyl-CoA to (2E)-2-enoyl-CoA. The enzyme from Escherichia coli contains FAD, FMN, and an [4Fe-4S] iron sulfur cluster. cf. EC 1.3.1.124, 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, 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. [DOI] [PMID: 6749495] |
| 2. |
Dommes, V. and Kunau, W.H. 2,4-Dienoyl coenzyme A reductases from bovine liver and Escherichia coli. Comparison of properties. J. Biol. Chem. 259 (1984) 1781–1788. [PMID: 6363415] |
| 3. |
You, S.Y., Cosloy, S. and Schulz, H. Evidence for the essential function of 2,4-dienoyl-coenzyme A reductase in the β-oxidation of unsaturated fatty acids in vivo. Isolation and characterization of an Escherichia coli mutant with a defective 2,4-dienoyl-coenzyme A reductase. J. Biol. Chem. 264 (1989) 16489–16495. [PMID: 2506179] |
| 4. |
He, X.Y., Yang, S.Y. and Schulz, H. Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli. Eur. J. Biochem. 248 (1997) 516–520. [PMID: 9346310] |
| 5. |
Liang, X., Thorpe, C. and Schulz, H. 2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-sulfur flavoprotein that functions in fatty acid β-oxidation. Arch. Biochem. Biophys. 380 (2000) 373–379. [PMID: 10933894] |
| 6. |
Hubbard, P.A., Liang, X., Schulz, H. and Kim, J.J. The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase. J. Biol. Chem. 278 (2003) 37553–37560. [PMID: 12840019] |
| 7. |
Tu, X., Hubbard, P.A., Kim, J.J. and Schulz, H. Two distinct proton donors at the active site of Escherichia coli 2,4-dienoyl-CoA reductase are responsible for the formation of different products. Biochemistry 47 (2008) 1167–1175. [PMID: 18171025] |
|
| [EC 1.3.1.34 created 1984, modified 1986, modified 2020] |
| |
|
| |
|
|
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 of geissoschizine and sarpagine biosynthesis, 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, PDB, 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 (NADPH) |
| 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, Gene, 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); 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 one of the activities of EC 2.3.1.85, fatty-acid synthase system. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH). |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| 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. [DOI] [PMID: 16215233] |
|
| [EC 1.3.1.39 created 1986, modified 2013, modified 2018] |
| |
|
| |
|
| 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: |
(9S,13S,15Z)-12-oxo-10,11-dihydrophyto-15-enoate + NADP+ = (9S,13S,15Z)-12-oxophyto-10,15-dienoate + NADPH + H+ |
| Glossary: |
(9S,13S,15Z)-12-oxo-10,11-dihydrophyto-15-enoate = 8-[(1S,2S)-3-oxo-2-{(Z)-pent-2-en-1-yl}cyclopentyl]octanoate |
| Other name(s): |
12-oxo-phytodienoic acid reductase; 8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate:NADP+ 4-oxidoreductase; (9S,13S)-10,11-dihydro-12-oxo-15-phytoenoate:NADP+ 4-oxidoreductase; (9S,13S)-12-oxophyto-15-enoate:NADP+ 10-oxidoreductase |
| Systematic name: |
(9S,13S,15Z)-12-oxo-10,11-dihydrophyto-15-enoate:NADP+ 10-oxidoreductase |
| Comments: |
The enzyme catalyses the reduction of (9S,13S,15Z)-12-oxophyto-10,15-dienoate during the biosynthesis of jasmonate from α-linolenate in Zea mays. |
| Links to other databases: |
BRENDA, EXPASY, Gene, 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. [PMID: 16664582] |
| 2. |
Schaller, F., Biesgen, C., Mussig, C., Altmann, T. and Weiler, E.W. 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis. Planta 210 (2000) 979–984. [DOI] [PMID: 10872231] |
|
| [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 phenylalanine and tyrosine biosynthesis, 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 (ambiguous); 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, Gene, KEGG, MetaCyc, PDB, 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. [DOI] [PMID: 3967752] |
| 5. |
Lingens, F., Keller, E. and Keller, B. Arogenate dehydrogenase from Phenylobacterium immobile. Methods Enzymol. 142 (1987) 513–518. [DOI] |
| 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, Gene, KEGG, MetaCyc, PDB, 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 of the biosynthesis of formononetin and derivatives, 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, Gene, 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 of the biosynthesis of biochanin A, 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 biosynthesis in cell suspensions 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, Gene, 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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, 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] |
| |
|
| |
|
| EC |
1.3.1.51 |
| Accepted name: |
2′-hydroxydaidzein reductase |
| Reaction: |
2′-hydroxy-2,3-dihydrodaidzein + NADP+ = 2′-hydroxydaidzein + NADPH + H+ |
|
For diagram of glyceollin biosynthesis (part 1), click here |
| Other name(s): |
NADPH:2′-hydroxydaidzein oxidoreductase; HDR; 2′-hydroxydihydrodaidzein:NADP+ 2′-oxidoreductase |
| Systematic name: |
2′-hydroxy-2,3-dihydrodaidzein:NADP+ 2′-oxidoreductase |
| Comments: |
In the reverse reaction, the 2′-hydroxyisoflavone (2′-hydroxydaidzein) is reduced to an isoflavanone. Also acts on 2′-hydroxyformononetin and to a small extent on 2′-hydroxygenistein. Involved in the biosynthesis of the phytoalexin glyceollin. The isoflavones biochanin A, daidzein and genestein as well as the flavonoids apigenin, kaempferol and quercetin do not act as substrates. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 126125-01-7 |
| References: |
| 1. |
Fischer, D., Ebenau-Jehle, C. and Grisebach, H. Phytoalexin synthesis in soybean: purification and characterization of NADPH:2′-hydroxydaidzein oxidoreductase from elicitor-challenged soybean cell cultures. Arch. Biochem. Biophys. 276 (1990) 390–395. [DOI] [PMID: 2306102] |
|
| [EC 1.3.1.51 created 1992, modified 2004] |
| |
|
| |
|
|
EC
|
1.3.1.52
|
| Transferred entry: | 2-methyl-branched-chain-enoyl-CoA reductase. Now EC 1.3.8.5, 2-methyl-branched-chain-enoyl-CoA reductase
|
| [EC 1.3.1.52 created 1992, deleted 2012] |
| |
|
| |
|
| EC |
1.3.1.53 |
| Accepted name: |
(3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase |
| Reaction: |
(3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate + NAD+ = 3,4-dihydroxybenzoate + CO2 + NADH |
| Glossary: |
(3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate = cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate |
| Other name(s): |
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase; terephthalate 1,2-cis-dihydrodiol dehydrogenase; cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate:NAD+ oxidoreductase (decarboxylating) |
| Systematic name: |
(3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate:NAD+ oxidoreductase |
| Comments: |
Requires FeII. Involved in the terephthalate degradation pathway in bacteria [2]. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 162032-77-1 |
| References: |
| 1. |
Saller, E., Laue, H.R., Schläfli Oppenberg, H.R. and Cook, A.M. Purification and some properties of (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase from Comamonas testosteroni T-2. FEMS Microbiol. Lett. 130 (1996) 97–102. |
| 2. |
Wang, Y.Z., Zhou, Y. and Zylstra, G.J. Molecular analysis of isophthalate and terephthalate degradation by Comamonas testosteroni YZW-D. Environ. Health Perspect. 103, Suppl. 5 (1995) 9–12. [PMID: 8565920] |
|
| [EC 1.3.1.53 created 1999 (EC 1.3.1.61 created 2000, incorporated 2007)] |
| |
|
| |
|
| EC |
1.3.1.54 |
| Accepted name: |
precorrin-6A reductase |
| Reaction: |
precorrin-6B + NADP+ = precorrin-6A + NADPH + H+ |
|
For diagram of corrin biosynthesis (part 3), click here |
| Other name(s): |
precorrin-6X reductase; precorrin-6Y:NADP+ oxidoreductase; CobK |
| Systematic name: |
precorrin-6B:NADP+ oxidoreductase |
| Comments: |
The enzyme, which participates in the aerobic (late cobalt insertion) pathway of adenosylcobalamin biosynthesis, catalyses the reduction of the double bond between C-18 and C-19 of precorrin-6A. See EC 1.3.1.106, cobalt-precorrin-6A reductase, for the corresponding enzyme that participates in the anaerobic cobalamin biosynthesis pathway. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 137573-72-9 |
| References: |
| 1. |
Blanche, F., Thibaut, D., Famechon, A., Debussche, L., Cameron, B. and Crouzet, J. Precorrin-6X reductase from Pseudomonas denitrificans: purification and characterization of the enzyme and identification of the structural gene. J. Bacteriol. 174 (1992) 1036–1042. [DOI] [PMID: 1732193] |
| 2. |
Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C. The biosynthesis of adenosylcobalamin (vitamin B12). Nat. Prod. Rep. 19 (2002) 390–412. [PMID: 12195810] |
|
| [EC 1.3.1.54 created 1999, modified 2004] |
| |
|
| |
|
|
EC
|
1.3.1.55
|
| Deleted entry: | cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase. Enzyme is identical to EC 1.3.1.25, 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase |
| [EC 1.3.1.55 created 1999, deleted 2004] |
| |
|
| |
|
| EC |
1.3.1.56 |
| Accepted name: |
cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase |
| Reaction: |
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ = biphenyl-2,3-diol + NADH + H+ |
| Other name(s): |
2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase |
| Systematic name: |
cis-3-phenylcyclohexa-3,5-diene-1,2-diol:NAD+ oxidoreductase |
| Comments: |
Catalyses the second step in the biphenyl degradation pathway in bacteria. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Sylvestre, M., Hurtubise, Y., Barriault, D., Bergeron, J. and Ahmad, D. Characterization of active recombinant 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas testosteroni B-356 and sequence of the encoding gene (bphB). Appl. Environ. Microbiol. 62 (1996) 2710–2715. [PMID: 8702262] |
| 2. |
Fukuda, M., Yasukochi, Y., Kikuchi, Y., Nagata, Y., Kimbara, K., Horiuchi, H., Takagi, M. and Yano, K. Identification of the bphA and bphB genes of Pseudomonas sp. strains KKS102 involved in degradation of biphenyl and polychlorinated biphenyls. Biochem. Biophys. Res. Commun. 202 (1994) 850–856. [DOI] [PMID: 8048958] |
| 3. |
Hofer, B., Eltis, L.D., Dowling, D.N. and Timmis, K.N. Genetic analysis of a Pseudomonas locus encoding a pathway for biphenyl/polychlorinated biphenyl degradation. Gene 130 (1993) 47–55. [DOI] [PMID: 8344527] |
|
| [EC 1.3.1.56 created 2000] |
| |
|
| |
|
| EC |
1.3.1.57 |
| Accepted name: |
phloroglucinol reductase |
| Reaction: |
dihydrophloroglucinol + NADP+ = phloroglucinol + NADPH + H+ |
| Glossary: |
phloroglucinol = 1,3,5-trihydroxybenzene |
| Systematic name: |
dihydrophloroglucinol:NADP+ oxidoreductase |
| Comments: |
Involved in the gallate anaerobic degradation pathway in bacteria. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 80804-59-7 |
| References: |
| 1. |
Haddock, J.D. and Ferry, J.G. Purification and properties of phloroglucinol reductase from Eubacterium oxidoreducens G-41. J. Biol. Chem. 264 (1989) 4423–4427. [PMID: 2925649] |
|
| [EC 1.3.1.57 created 2000] |
| |
|
| |
|
| EC |
1.3.1.58 |
| Accepted name: |
2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase |
| Reaction: |
cis-5,6-dihydroxy-4-isopropylcyclohexa-1,3-dienecarboxylate + NAD+ = 2,3-dihydroxy-p-cumate + NADH + H+ |
|
For diagram of reaction, click here |
| Glossary: |
p-cumic acid = 4-isopropylbenzoic acid
p-cymene = 1-methyl-4-isopropylbenzene |
| Systematic name: |
cis-2,3-dihydroxy-2,3-dihydro-p-cumate:NAD+ oxidoreductase |
| Comments: |
Involved in the p-cymene degradation pathway in Pseudomonas putida. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 176591-33-6 |
| References: |
| 1. |
Eaton, R.W. p-Cumate catabolic pathway in Pseudomonas putida Fl: cloning and characterization of DNA carrying the cmt operon. J. Bacteriol. 178 (1996) 1351–1362. [DOI] [PMID: 8631713] |
|
| [EC 1.3.1.58 created 2000] |
| |
|
| |
|
|
EC
|
1.3.1.59
|
| Deleted entry: | 1,2-dihydroxy-3-methyl-1,2-dihydrobenzoate dehydrogenase. No evidence in the paper cited that the enzyme exists |
| [EC 1.3.1.59 created 2000, deleted 2006] |
| |
|
| |
|
| EC |
1.3.1.60 |
| Accepted name: |
dibenzothiophene dihydrodiol dehydrogenase |
| Reaction: |
cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene + NAD+ = 1,2-dihydroxydibenzothiophene + NADH + H+ |
| Systematic name: |
cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene:NAD+ oxidoreductase |
| Comments: |
Involved in the dibenzothiophene degradation pathway in bacteria. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Laborde, A.L. and Gibson, D.T. Metabolism of dibenzothiophene by a Beijerinckia species. Appl. Environ. Microbiol. 34 (1977) 783–790. [PMID: 596875] |
| 2. |
Denome, S.A., Stanley, D.C., Olson, E.S. and Young, K.D. Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway. J. Bacteriol. 175 (1993) 6890–6901. [DOI] [PMID: 8226631] |
|
| [EC 1.3.1.60 created 2000] |
| |
|
| |
|
|
EC
|
1.3.1.61
|
| Deleted entry: | terephthalate 1,2-cis-dihydrodiol dehydrogenase. Enzyme is identical to EC 1.3.1.53, (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase |
| [EC 1.3.1.61 created 2000, deleted 2007] |
| |
|
| |
|
| EC |
1.3.1.62 |
| Accepted name: |
pimeloyl-CoA dehydrogenase |
| Reaction: |
pimeloyl-CoA + NAD+ = 6-carboxyhex-2-enoyl-CoA + NADH + H+ |
| Glossary: |
pimelic acid = heptanedioic acid |
| Systematic name: |
pimeloyl-CoA:NAD+ oxidoreductase |
| Comments: |
Involved in the benzoate degradation (anaerobic) pathway in bacteria. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 276682-23-6 |
| References: |
| 1. |
Gallus, C. and Schink, B. Anaerobic degradation of pimelate by newly isolated denitrifying bacteria. Microbiology 140 (1994) 409–416. [DOI] [PMID: 8180704] |
|
| [EC 1.3.1.62 created 2000] |
| |
|
| |
|
|
EC
|
1.3.1.63
|
| Transferred entry: | 2,4-dichlorobenzoyl-CoA reductase. Now EC 1.21.1.2, 2,4-dichlorobenzoyl-CoA reductase
|
| [EC 1.3.1.63 created 2000, modified 2011, deleted 2015] |
| |
|
| |
|
| EC |
1.3.1.64 |
| Accepted name: |
phthalate 4,5-cis-dihydrodiol dehydrogenase |
| Reaction: |
cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+ = 4,5-dihydroxyphthalate + NADH + H+ |
| Systematic name: |
cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate:NAD+ oxidoreductase |
| Comments: |
Involved in the phthalate degradation pathway in bacteria. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Batie, C.J., LaHaie, E. and Ballou, D.P. Purification and characterization of phthalate oxygenase and phthalate oxygenase reductase from Pseudomonas cepacia. J. Biol. Chem. 262 (1987) 1510–1518. [PMID: 3805038] |
|
| [EC 1.3.1.64 created 2000] |
| |
|
| |
|
| EC |
1.3.1.65 |
| Accepted name: |
5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase |
| Reaction: |
5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline + NAD+ = 5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline + NADH + H+ |
| Systematic name: |
5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline:NAD+ oxidoreductase |
| Comments: |
Acts in the reverse direction to form part of the 3-methylquinoline degradation pathway in bacteria. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Schach, S., Schwarz, G., Fetzner, S. and Lingens, F. Microbial metabolism of quinoline and related compounds. XVII. Degradation of 3-methylquinoline by Comamonas testosteroni 63. Biol. Chem. Hoppe Seyler 374 (1993) 175–181. [PMID: 8489738] |
|
| [EC 1.3.1.65 created 2000] |
| |
|
| |
|
| EC |
1.3.1.66 |
| Accepted name: |
cis-dihydroethylcatechol dehydrogenase |
| Reaction: |
cis-1,2-dihydro-3-ethylcatechol + NAD+ = 3-ethylcatechol + NADH + H+ |
| Systematic name: |
cis-1,2-dihydro-3-ethylcatechol:NAD+ oxidoreductase |
| Comments: |
Involved in the ethylbenzene degradation pathway in bacteria. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Gibson, D.T., Gschwendt, B., Yeh, W.K. and Kobal, V.M. Initial reactions in the oxidation of ethylbenzene by Pseudomonas putida. Biochemistry 12 (1973) 1520–1528. [PMID: 4699984] |
|
| [EC 1.3.1.66 created 2000] |
| |
|
| |
|
| EC |
1.3.1.67 |
| Accepted name: |
cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase |
| Reaction: |
cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + NAD(P)+ = 4-methylcatechol + NAD(P)H + CO2 |
| Systematic name: |
cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate:NAD(P)+ oxidoreductase (decarboxylating) |
| Comments: |
Involved in the p-xylene degradation pathway in bacteria. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Whited, G.M., McCombie, W.R., Kwart, L.D. and Gibson, D.T. Identification of cis-diols as intermediates in the oxidation of aromatic acids by a strain of Pseudomonas putida that contains a TOL plasmid. J. Bacteriol. 166 (1986) 1028–1039. [DOI] [PMID: 3711022] |
|
| [EC 1.3.1.67 created 2000] |
| |
|
| |
|
| EC |
1.3.1.68 |
| Accepted name: |
1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase |
| Reaction: |
1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate + NAD+ = 3-methylcatechol + NADH + CO2 |
| Systematic name: |
1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate:NAD+ oxidoreductase (decarboxylating) |
| Comments: |
Involved in the o-xylene degradation pathway in bacteria. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Higson, F.K. and Focht, D.D. Degradation of 2-methylbenzoic acid by Pseudomonas cepacia MB2. Appl. Environ. Microbiol. 58 (1992) 194–200. [PMID: 1371658] |
|
| [EC 1.3.1.68 created 2000] |
| |
|
| |
|
| EC |
1.3.1.69 |
| Accepted name: |
zeatin reductase |
| Reaction: |
dihydrozeatin + NADP+ = zeatin + NADPH + H+ |
| Glossary: |
zeatin = (E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol = (E)-N6-(4-hydroxy-3-methylbut-2-enyl)adenine |
| Systematic name: |
dihydrozeatin:NADP+ oxidoreductase |
| Comments: |
Previously classified erroneously as EC 1.1.1.242. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123644-82-6 |
| References: |
| 1. |
Martin, R.C., Mok, M.C., Shaw, G. and Mok, D.W.S. An enzyme mediating the conversion of zeatin to dihydrozeatin in Phaseolus embryos. Plant Physiol. 90 (1989) 1630–1635. [PMID: 16666974] |
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| [EC 1.3.1.69 created 1992 as EC 1.1.1.242, transferred 2001 to EC 1.3.1.69] |
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|
| EC |
1.3.1.70 |
| Accepted name: |
Δ14-sterol reductase |
| Reaction: |
4,4-dimethyl-5α-cholesta-8,24-dien-3β-ol + NADP+ = 4,4-dimethyl-5α-cholesta-8,14,24-trien-3β-ol + NADPH + H+ |
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For diagram of the modification of sterol rings B, C and D, click here |
| Systematic name: |
4,4-dimethyl-5α-cholesta-8,24-dien-3β-ol:NADP+ Δ14-oxidoreductase |
| Comments: |
This enzyme acts on a range of steroids with a 14(15)-double bond. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 69403-07-2 |
| References: |
| 1. |
Bottema, C.K. and Parks, L.W. Δ14-Sterol reductase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 531 (1978) 301–307. [DOI] [PMID: 32908] |
| 2. |
Paik, Y.K., Trzaskos, J.M., Shafice, A. and Gaylor, J.L. Microsomal enzymes of cholesterol biosynthesis from lanosterol. Characterization, solubilization, and partial purification of NADPH-dependent Δ8,14-steroid 14-reductase. J. Biol. Chem. 259 (1984) 13413–13423. [PMID: 6444198] |
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| [EC 1.3.1.70 created 2001] |
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| EC |
1.3.1.71 |
| Accepted name: |
Δ24(241)-sterol reductase |
| Reaction: |
ergosterol + NADP+ = ergosta-5,7,22,24(241)-tetraen-3β-ol + NADPH + H+ |
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For diagram of sterol-sidechain modification, click here |
| Other name(s): |
sterol Δ24(28)-methylene reductase; sterol Δ24(28)-reductase |
| Systematic name: |
ergosterol:NADP+ Δ24(241)-oxidoreductase |
| Comments: |
Acts on a range of steroids with a 24(241)-double bond. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Neal, W.D. and Parks, L.W. Sterol 24(28) methylene reductase in Saccharomyces cerevisiae. J. Bacteriol. 129 (1977) 1375–1378. [PMID: 14922] |
| 2. |
Zweytick, D., Hrastnik, C., Kohlwein. S.D. and Daum, G. Biochemical characterization and subcellular localization of the sterol C-24(28) reductase, erg4p, from the yeast Saccharomyces cerevisiae. FEBS Lett. 470 (2000) 83–87. [DOI] [PMID: 10722850] |
|
| [EC 1.3.1.71 created 2001, modified 2002] |
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| EC |
1.3.1.72 |
| Accepted name: |
Δ24-sterol reductase |
| Reaction: |
5α-cholest-7-en-3β-ol + NADP+ = 5α-cholesta-7,24-dien-3β-ol + NADPH + H+ |
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For diagram of sterol-sidechain modification, click here |
| Glossary: |
desmosterol = cholesta-5,24-dien-3β-ol
lanosterol = 4,4,14-trimethyl-5α-cholesta-8,24-dien-3β-ol
zymostrol = 5α-cholesta-8,24-dien-3β-ol |
| Other name(s): |
lanosterol Δ24-reductase |
| Systematic name: |
sterol:NADP+ Δ24-oxidoreductase |
| Comments: |
Acts on a range of steroids with a 24(25)-double bond, including lanosterol, desmosterol and zymosterol. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9033-57-2 |
| References: |
| 1. |
Bae, S.H. and Paik, Y.K. Cholesterol biosynthesis from lanosterol: development of a novel assay method and characterization of rat liver microsomal lanosterol Δ24-reductase. Biochem. J. 326 (1997) 609–616. [PMID: 9291139] |
|
| [EC 1.3.1.72 created 2001] |
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|
| EC |
1.3.1.73 |
| Accepted name: |
1,2-dihydrovomilenine 19,20-reductase |
| Reaction: |
17-O-acetylnorajmaline + NADP+ = (2R)-1,2-dihydrovomilenine + NADPH + H+ |
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For diagram of ajmaline, vinorine, vomilenine and raucaffricine biosynthesis, click here |
| Other name(s): |
1,2-dihydrovomilenine reductase; DHVR; RR4 (gene name); 17-O-acetylnorajmaline:NADP+ oxidoreductase |
| Systematic name: |
17-O-acetylnorajmaline:NADP+ 19,20-oxidoreductase |
| Comments: |
The enzyme, characterized from the plant Rauvolfia serpentina, participates in the ajmaline biosynthesis pathway. It has a much lower activity on vomilenine. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Gao, S., von Schumann, G. and Stöckigt, J. A newly-detected reductase from Rauvolfia closes a gap in the biosynthesis of the antiarrhythmic alkaloid ajmaline. Planta Med. 68 (2002) 906–911. [DOI] [PMID: 12391554] |
| 2. |
Guo, J., Gao, D., Lian, J. and Qu, Y. De novo biosynthesis of antiarrhythmic alkaloid ajmaline. Nat. Commun. 15:457 (2024). [DOI] [PMID: 38212296] |
|
| [EC 1.3.1.73 created 2002, modified 2024] |
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|
| EC |
1.3.1.74 |
| Accepted name: |
2-alkenal reductase [NAD(P)+] |
| Reaction: |
a n-alkanal + NAD(P)+ = an alk-2-enal + NAD(P)H + H+ |
| Other name(s): |
NAD(P)H-dependent alkenal/one oxidoreductase; NADPH:2-alkenal α,β-hydrogenase; 2-alkenal reductase |
| Systematic name: |
n-alkanal:NAD(P)+ 2-oxidoreductase |
| Comments: |
Highly specific for 4-hydroxynon-2-enal and non-2-enal. Alk-2-enals of shorter chain have lower affinities. Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one. Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid. Involved in the detoxication of α,β-unsaturated aldehydes and ketones [cf. EC 1.3.1.102, 2-alkenal reductase (NADP+)]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 52227-95-9 |
| References: |
| 1. |
Mano, J., Torii, Y., Hayashi, S., Takimoto, K., Matsui, K., Nakamura, K., Inzé, D., Babiychuk, E., Kushnir, S. and Asada, K. The NADPH:quinone oxidoreductase P1-ζ-crystallin in Arabidopsis catalyzes the α,β-hydrogenation of 2-alkenals: detoxication of the lipid peroxide-derived reactive aldehydes. Plant Cell Physiol. 43 (2002) 1445–1455. [PMID: 12514241] |
| 2. |
Dick, R.A., Kwak, M.K., Sutter, T.R. and Kensler, T.W. Antioxidative function and substrate specificity of NAD(P)H-dependent alkenal/one oxidoreductase. A new role for leukotriene B4 12-hydroxydehydrogenase/15-oxoprostaglandin 13-reductase. J. Biol. Chem. 276 (2001) 40803–40810. [DOI] [PMID: 11524419] |
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| [EC 1.3.1.74 created 2003, modified 2014] |
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