Enzyme Nomenclature

Continued from EC 1.3.1.1 to EC 1.3.1.50

EC 1.3.1 (continued)

Contents

EC 1.3.1.51 2'-hydroxydaidzein reductase
EC 1.3.1.52 now EC 1.3.8.5
EC 1.3.1.53 (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase
EC 1.3.1.54 precorrin-6A reductase
EC 1.3.1.55 now EC 1.3.1.25
EC 1.3.1.56 cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase
EC 1.3.1.57 phloroglucinol reductase
EC 1.3.1.58 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase
EC 1.3.1.59 deleted entry.
EC 1.3.1.60 dibenzothiophene dihydrodiol dehydrogenase
EC 1.3.1.61 deleted, identical to EC 1.3.1.53
EC 1.3.1.62 pimeloyl-CoA dehydrogenase
EC 1.3.1.35 now EC 1.14.19.22
EC 1.3.1.64 phthalate 4,5-cis-dihydrodiol dehydrogenase
EC 1.3.1.65 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase
EC 1.3.1.66 cis-dihydroethylcatechol dehydrogenase
EC 1.3.1.67 cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase
EC 1.3.1.68 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase
EC 1.3.1.69 zeatin reductase
EC 1.3.1.70Δ14-sterol reductase
EC 1.3.1.71Δ24(241)-sterol reductase
EC 1.3.1.72Δ24-sterol reductase
EC 1.3.1.73 1,2-dihydrovomilenine reductase
EC 1.3.1.74 2-alkenal reductase [NAD(P)+]
EC 1.3.1.75 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH)
EC 1.3.1.76 precorrin-2 dehydrogenase
EC 1.3.1.77 anthocyanidin reductase [(2R,3R)-flavan-3-ol-forming]
EC 1.3.1.78 arogenate dehydrogenase (NADP+)
EC 1.3.1.79 arogenate dehydrogenase [NAD(P)+]
EC 1.3.1.80 now EC 1.3.7.12
EC 1.3.1.81 (+)-pulegone reductase
EC 1.3.1.82 (–)-isopiperitenone reductase
EC 1.3.1.83 geranylgeranyl diphosphate reductase
EC 1.3.1.84 acrylyl-CoA reductase (NADPH)
EC 1.3.1.85 crotonyl-CoA carboxylase/reductase
EC 1.3.1.86 crotonyl-CoA reductase
EC 1.3.1.87 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate dehydrogenase
EC 1.3.1.88 tRNA-dihydrouridine16/17 synthase [NAD(P)+]
EC 1.3.1.89 tRNA-dihydrouridine47 synthase [NAD(P)+]
EC 1.3.1.90 tRNA-dihydrouridine20a/20b synthase [NAD(P)+]
EC 1.3.1.91 tRNA-dihydrouridine20 synthase [NAD(P)+]
EC 1.3.1.92 artemisinic aldehyde Δ11(13)-reductase
EC 1.3.1.93 very-long-chain enoyl-CoA reductase
EC 1.3.1.94 polyprenol reductase
EC 1.3.1.95 acrylyl-CoA reductase (NADH)
EC 1.3.1.96 Botryococcus squalene synthase
EC 1.3.1.97 botryococcene synthase
EC 1.3.1.98 UDP-N-acetylmuramate dehydrogenase
EC 1.3.1.99 iridoid synthase
EC 1.3.1.100 chanoclavine-I aldehyde reductase
EC 1.3.1.101 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H]
EC 1.3.1.102 2-alkenal reductase (NADP+)
EC 1.3.1.103 2-haloacrylate reductase
EC 1.3.1.104 enoyl-[acyl-carrier-protein] reductase
EC 1.3.1.105 2-methylene-furan-3-one reductase
EC 1.3.1.106 cobalt-precorrin-6A reductase
EC 1.3.1.107 sanguinarine reductase
EC 1.3.1.108 caffeoyl-CoA reductase
EC 1.3.1.109 butanoyl-CoA dehydrogenase (NAD+, ferredoxin)
EC 1.3.1.110 lactate dehydrogenase (NAD+, ferredoxin)
EC 1.3.1.111 geranylgeranyl-bacteriochlorophyllide a reductase
EC 1.3.1.112 anthocyanidin reductase [(2S)-flavan-3-ol-forming]


EC 1.3.1.51

Accepted name: 2'-hydroxydaidzein reductase

Reaction: 2'-hydroxy-2,3-dihydrodaidzein + NADP+ = 2'-hydroxydaidzein + NADPH + H+

For diagram 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. [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, EXPASY, KEGG, Metacyc, UM-BBD, 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 click here.

Other name(s): precorrin-6X reductase; precorrin-6Y:NADP+ oxidoreductase

Systematic name: precorrin-6B:NADP+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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. [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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number:

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. [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. [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 entries:
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, EXPASY, KEGG, Metacyc, UM-BBD, 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 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, EXPASY, KEGG, Metacyc, UM-BBD, 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. [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 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, KEGG, Metacyc, UM-BBD, CAS registry number:

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. [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 entries:
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, EXPASY, KEGG, Metacyc, UM-BBD, 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. [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, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:

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, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:

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, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:

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, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:

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. [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, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:

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

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.

[EC 1.3.1.69 created 1992 as EC 1.1.1.242, transferred 2001 to EC 1.3.1.69]

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+

For diagram 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, KEGG, Metacyc, 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. [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]

[EC 1.3.1.70 created 2001]

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+

For diagram click here.

Other names: 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, KEGG, Metacyc, CAS registry number:

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. [PMID: 10722850]

[EC 1.3.1.71 created 2001, modified 2002]

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+

For diagram 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 names: 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, 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]

EC 1.3.1.73

Accepted name: 1,2-dihydrovomilenine reductase

Reaction: 17-O-acetylnorajmaline + NADP+ = 1,2-dihydrovomilenine + NADPH + H+

For diagram click here.

Systematic name: 17-O-acetylnorajmaline:NADP+ oxidoreductase

Comments: Forms part of the ajmaline biosynthesis pathway.

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

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. [PMID: 12391554 ]

[EC 1.3.1.73 created 2002]

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, 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. [PMID: 11524419]

[EC 1.3.1.74 created 2003, modified 2014]

EC 1.3.1.75

Accepted name: 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH)

Reaction: protochlorophyllide a + NADP+ = 3,8-divinyl protochlorophyllide a + NADPH + H+

For diagram of reaction click here.

Other name(s): DVR (gene name); bciA (gene name); [4-vinyl]chlorophyllide a reductase; 4VCR; chlorophyllide-a:NADP+ oxidoreductase; divinyl chlorophyllide a 8-vinyl-reductase; plant-type divinyl chlorophyllide a 8-vinyl-reductase

Systematic name: protochlorophyllide-a:NADP+ C-81-oxidoreductase

Comments: The enzyme, found in higher plants, green algae, and some phototrophic bacteria, is involved in the production of monovinyl versions of (bacterio)chlorophyll pigments from their divinyl precursors. It can also act on 3,8-divinyl chlorophyllide a. cf. EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc

References:

1. Tripathy, B.C. and Rebeiz, C.A. Chloroplast biogenesis 60. Conversion of divinyl protochlorophyllide to monovinyl protochlorophyllide in green(ing) barley, a dark monovinyl/light divinyl plant species. Plant Physiol. 87 (1988) 89-94. [PMID: 16666133]

2. Parham, R. and Rebeiz, C.A. Chloroplast biogenesis: [4-vinyl] chlorophyllide a reductase is a divinyl chlorophyllide a-specific, NADPH-dependent enzyme. Biochemistry 31 (1992) 8460-8464. [PMID: 1390630]

3. Parham, R. and Rebeiz, C.A. Chloroplast biogenesis 72: a [4-vinyl]chlorophyllide a reductase assay using divinyl chlorophyllide a as an exogenous substrate. Anal. Biochem. 231 (1995) 164-169. [PMID: 8678296]

4. Kolossov, V.L. and Rebeiz, C.A. Chloroplast biogenesis 84: solubilization and partial purification of membrane-bound [4-vinyl]chlorophyllide a reductase from etiolated barley leaves. Anal. Biochem. 295 (2001) 214-219. [PMID: 11488624]

5. Nagata, N., Tanaka, R., Satoh, S. and Tanaka, A. Identification of a vinyl reductase gene for chlorophyll synthesis in Arabidopsis thaliana and implications for the evolution of Prochlorococcus species. Plant Cell 17 (2005) 233-240. [PMID: 15632054]

6. Chew, A.G. and Bryant, D.A. Characterization of a plant-like protochlorophyllide a divinyl reductase in green sulfur bacteria. J. Biol. Chem. 282 (2007) 2967-2975. [PMID: 17148453]

[EC 1.3.1.75 created 2003, modified 2016]

EC 1.3.1.76

Accepted name: precorrin-2 dehydrogenase

Reaction: precorrin-2 + NAD+ = sirohydrochlorin + NADH + H+

For diagram click here.

Other name(s): Met8p; SirC; CysG

Systematic name: precorrin-2:NAD+ oxidoreductase

Comments: This enzyme catalyses the second of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 227184-47-6

References:

1. Schubert, H.L., Raux, E., Brindley, A.A., Leech, H.K., Wilson, K.S., Hill, C.P. and Warren, M.J. The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase. EMBO J. 21 (2002) 2068-2075. [PMID: 11980703]

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 1.3.1.76 created 2004]

EC 1.3.1.77

Accepted name: anthocyanidin reductase [(2R,3R)-flavan-3-ol-forming]

Reaction: a (2R,3R)-flavan-3-ol + 2 NAD(P)+ = an anthocyanidin with a 3-hydroxy group + 2 NAD(P)H + H+

For diagram of reaction click here.

Other name(s): ANR (gene name) (ambiguous); flavan-3-ol:NAD(P)+ oxidoreductase; anthocyanidin reductase (ambiguous)

Systematic name: (2R,3R)-flavan-3-ol:NAD(P)+ 3,4-oxidoreductase

Comments: The enzyme participates in the flavonoid biosynthesis pathway found in plants. It catalyses the double reduction of anthocyanidins, producing (2R,3R)-flavan-3-ol monomers required for the formation of proanthocyanidins. While the enzyme from the legume Medicago truncatula (MtANR) can use both NADPH and NADH as reductant, that from the crucifer Arabidopsis thaliana (AtANR) uses only NADPH. Also, while the substrate preference of MtANR is cyanidin>pelargonidin>delphinidin, the reverse preference is found with AtANR. cf. EC 1.3.1.112, anthocyanidin reductase [(2S)-flavan-3-ol-forming].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 93389-48-1

References:

1. Xie, D.Y., Sharma, S.B., Paiva, N.L., Ferreira, D. and Dixon, R.A. Role of anthocyanidin reductase, encoded by BANYULS in plant flavonoid biosynthesis. Science 299 (2003) 396-399. [PMID: 12532018]

2. Xie, D.Y., Sharma, S.B. and Dixon, R.A. Anthocyanidin reductases from Medicago truncatula and Arabidopsis thaliana. Arch. Biochem. Biophys. 422 (2004) 91-102. [PMID: 14725861]

3. Pang, Y., Abeysinghe, I.S., He, J., He, X., Huhman, D., Mewan, K.M., Sumner, L.W., Yun, J. and Dixon, R.A. Functional characterization of proanthocyanidin pathway enzymes from tea and their application for metabolic engineering. Plant Physiol. 161 (2013) 1103-1116. [PMID: 23288883]

[EC 1.3.1.77 created 2004, modified 2016]

EC 1.3.1.78

Accepted name: arogenate dehydrogenase (NADP+)

Reaction: L-arogenate + NADP+ = L-tyrosine + NADPH + CO2

For diagram click here.

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

Other name(s): arogenic dehydrogenase (ambiguous); pretyrosine dehydrogenase (ambiguous); TyrAAT1; TyrAAT2; TyrAa

Systematic name: L-arogenate:NADP+ 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). NADP+-dependent enzymes usually predominate in higher plants.The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 and the TyrAAT1 isoform of the plant Arabidopsis thaliana cannot use prephenate as a substrate, while the Arabidopsis isoform TyrAAT2 can use it very poorly [2,3].

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

References:

1. Gaines, C.G., Byng, G.S., Whitaker, R.J. and Jensen, R.A. L-Tyrosine regulation and biosynthesis via arogenate dehydrogenase in suspension-cultured cells of Nicotiana silvestris Speg. et Comes. Planta 156 (1982) 233-240.

2. Rippert, P. and Matringe, M. Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana. Eur. J. Biochem. 269 (2002) 4753-4761. [PMID: 12354100]

3. Bonner, C.A., Jensen, R.A., Gander, J.E. and Keyhani, N.O. A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis. Biochem. J. 382 (2004) 279-291. [PMID: 15171683]

[EC 1.3.1.78 created 2005]

EC 1.3.1.79

Accepted name: arogenate dehydrogenase [NAD(P)+]

Reaction: L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + CO2

For diagram 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)

Systematic name: L-arogenate:NAD(P)+ 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). Enzymes that can utilize both cofactors have been reported from some Proteobacteria, including Burkholderia caryophylli, Burkholderia cepacia, Pseudomonas marginata and Delftia acidovorans.

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

References:

1. 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]

[EC 1.3.1.79 created 2005]

[EC 1.3.1.80 Transferred entry: red chlorophyll catabolite reductase, now classified as EC 1.3.7.12, red chlorophyll catabolite reductase (EC 1.3.1.80 created 2007, deleted 2016)]

EC 1.3.1.81

Accepted name: (+)-pulegone reductase

Reaction: (1) (–)-menthone + NADP+ = (+)-pulegone + NADPH + H+
(2) (+)-isomenthone + NADP+ = (+)-pulegone + NADPH + H+

For diagram of reaction click here.

Systematic name: (–)-menthone:NADP+ oxidoreductase

Comments: NADH cannot replace NADPH as reductant. The Δ8,9-double bond of (+)-cis-isopulegone and the Δ1,2-double bond of (±)-piperitone are not substrates. The enzyme from peppermint (Mentha x piperita) converts (+)-pulegone into both (–)-menthone and (+)-isomenthone at a ratio of 70:30 for native enzyme but it does not catalyse the reverse reaction. This enzyme is a member of the medium-chain dehydrogenase/reductase superfamily.

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

References:

1. Ringer, K.L., McConkey, M.E., Davis, E.M., Rushing, G.W. and Croteau, R. Monoterpene double-bond reductases of the (–)-menthol biosynthetic pathway: isolation and characterization of cDNAs encoding (–)-isopiperitenone reductase and (+)-pulegone reductase of peppermint. Arch. Biochem. Biophys. 418 (2003) 80-92. [PMID: 13679086]

[EC 1.3.1.81 created 2008]

EC 1.3.1.82

Accepted name: (–)-isopiperitenone reductase

Reaction: (+)-cis-isopulegone + NADP+ = (–)-isopiperitenone + NADPH + H+

For diagram of reaction click here.

Systematic name: (+)-cis-isopulegone:NADP+ oxidoreductase

Comments: The reaction occurs in the opposite direction to that shown above. The enzyme participates in the menthol-biosynthesis pathway of Mentha plants. (+)-Pulegone, (+)-cis-isopulegone and (–)-menthone are not substrates. The enzyme has a preference for NADPH as the reductant, with NADH being a poor substitute [2]. The enzyme is highly regioselective for the reduction of the endocyclic 1,2-double bond, and is stereoselective, producing only the 1R-configured product. It is a member of the short-chain dehydrogenase/reductase superfamily.

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

References:

1. Croteau, R. and Venkatachalam, K.V. Metabolism of monoterpenes: demonstration that (+)-cis-isopulegone, not piperitenone, is the key intermediate in the conversion of (–)-isopiperitenone to (+)-pulegone in peppermint (Mentha piperita). Arch. Biochem. Biophys. 249 (1986) 306-315. [PMID: 3755881]

2. Ringer, K.L., McConkey, M.E., Davis, E.M., Rushing, G.W. and Croteau, R. Monoterpene double-bond reductases of the (–)-menthol biosynthetic pathway: isolation and characterization of cDNAs encoding (–)-isopiperitenone reductase and (+)-pulegone reductase of peppermint. Arch. Biochem. Biophys. 418 (2003) 80-92. [PMID: 13679086]

[EC 1.3.1.82 created 2008]

EC 1.3.1.83

Accepted name: geranylgeranyl diphosphate reductase

Reaction: phytyl diphosphate + 3 NADP+ = geranylgeranyl diphosphate + 3 NADPH + 3 H+

For diagram click here.

Other name(s): geranylgeranyl reductase; CHL P

Systematic name: geranylgeranyl-diphosphate:NADP+ oxidoreductase

Comments: This enzyme also acts on geranylgeranyl-chlorophyll a. The reaction occurs in three steps. Which order the three double bonds are reduced is not known.

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

References:

1. Soll, J., Schultz, G., Rüdiger, W. and Benz, J. Hydrogenation of geranylgeraniol: two pathways exist in spinach chloroplasts. Plant Physiol. 71 (1983) 849-854. [PMID: 16662918]

2. Tanaka, R., Oster, U., Kruse, E., Rüdiger, W. and Grimm, B. Reduced activity of geranylgeranyl reductase leads to loss of chlorophyll and tocopherol and to partially geranylgeranylated chlorophyll in transgenic tobacco plants expressing antisense RNA for geranylgeranyl reductase Plant Physiol. 120 (1999) 695-704. [PMID: 10398704]

3. Keller, Y., Bouvier, F., d'Harlingue, A. and Camara, B. Metabolic compartmentation of plastid prenyllipid biosynthesis - evidence for the involvement of a multifunctional geranylgeranyl reductase. Eur. J. Biochem. 251 (1998) 413-417. [PMID: 9492312]

[EC 1.3.1.83 created 2009]

EC 1.3.1.84

Accepted name: acrylyl-CoA reductase (NADPH)

Reaction: propanoyl-CoA + NADP+ = acryloyl-CoA + NADPH + H+

For diagram of reaction click here (another example and another example.

Glossary: acrylyl-CoA = acryloyl-CoA
propanoyl-CoA = propionyl-CoA

Systematic name: propanoyl-CoA:NADP+ oxidoreductase

Comments: Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [1]. The enzyme from Sulfolobus tokodaii does not act on either NADH or crotonyl-CoA [2]. Different from EC 1.3.1.8, which acts only on enoyl-CoA derivatives of carbon chain length 4 to 16. Contains Zn2+.

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

References:

1. Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782-1786. [PMID: 18079405]

2. Teufel, R., Kung, J.W., Kockelkorn, D., Alber, B.E. and Fuchs, G. 3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales. J. Bacteriol. 191 (2009) 4572-4581. [PMID: 19429610]

[EC 1.3.1.84 created 2009]

EC 1.3.1.85

Accepted name: crotonyl-CoA carboxylase/reductase

Reaction: (2S)-ethylmalonyl-CoA + NADP+ = (E)-but-2-enoyl-CoA + CO2 + NADPH + H+

Glossary: (E)-but-2-enoyl-CoA = crotonyl-CoA

Other name(s): CCR; crotonyl-CoA reductase (carboxylating)

Systematic name: (2S)-ethylmalonyl-CoA:NADP+ oxidoreductase (decarboxylating)

Comments: The reaction is catalysed in the reverse direction. This enzyme, isolated from the bacterium Rhodobacter sphaeroides, catalyses (E)-but-2-enoyl-CoA-dependent oxidation of NADPH in the presence of CO2. When CO2 is absent, the enzyme catalyses the reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA, but with only 10% of maximal activity (relative to (E)-but-2-enoyl-CoA carboxylation).

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

References:

1. Erb, T.J., Berg, I.A., Brecht, V., Muller, M., Fuchs, G. and Alber, B.E. Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway. Proc. Natl. Acad. Sci. USA 104 (2007) 10631-10636. [PMID: 17548827]

2. Erb, T.J., Brecht, V., Fuchs, G., Muller, M. and Alber, B.E. Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase. Proc. Natl. Acad. Sci. USA 106 (2009) 8871-8876. [PMID: 19458256]

[EC 1.3.1.85 created 2011]

EC 1.3.1.86

Accepted name: crotonyl-CoA reductase

Reaction: butanoyl-CoA + NADP+ = (E)-but-2-enoyl-CoA + NADPH + H+

For diagram of reaction click here.

Glossary: (E)-but-2-enoyl-CoA = crotonyl-CoA, butanoyl-CoA = butyryl-CoA

Other name(s): butyryl-CoA dehydrogenase; butyryl dehydrogenase; unsaturated acyl-CoA reductase; ethylene reductase; enoyl-coenzyme A reductase; unsaturated acyl coenzyme A reductase; butyryl coenzyme A dehydrogenase; short-chain acyl CoA dehydrogenase; short-chain acyl-coenzyme A dehydrogenase; 3-hydroxyacyl CoA reductase; butanoyl-CoA:(acceptor) 2,3-oxidoreductase; CCR

Systematic name: butanoyl-CoA:NADP+ 2,3-oxidoreductase

Comments: Catalyses the reaction in the reverse direction. This enzyme from Streptomyces collinus is specific for (E)-but-2-enoyl-CoA, and is proposed to provide butanoyl-CoA as a starter unit for straight-chain fatty acid biosynthesis.

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

References:

1. Wallace, K.K., Bao, Z.Y., Dai, H., Digate, R., Schuler, G., Speedie, M.K. and Reynolds, K.A. Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli. Eur. J. Biochem. 233 (1995) 954-962. [PMID: 8521864]

[EC 1.3.1.86 created 2011]

EC 1.3.1.87

Accepted name: 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate dehydrogenase

Reaction: (1) 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+ = 3-(2,3-dihydroxyphenyl)propanoate + NADH + H+
(2) (2E)-3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)prop-2-enoate + NAD+ = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NADH + H+

For diagram of reaction click here and another click here.

Glossary: (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate = trans-2,3-dihydroxycinnamate

Other name(s): hcaB (gene name); cis-dihydrodiol dehydrogenase; 2,3-dihydroxy-2,3-dihydro-phenylpropionate dehydrogenase

Systematic name: 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate:NAD+ oxidoreductase

Comments: This enzyme catalyses a step in the pathway of phenylpropanoid compounds degradation.

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

References:

1. Díaz, E., Ferrández, A. and García, J.L. Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12. J. Bacteriol. 180 (1998) 2915-2923. [PMID: 9603882]

[EC 1.3.1.87 created 2011]

EC 1.3.1.88

Accepted name: tRNA-dihydrouridine16/17 synthase [NAD(P)+]

Reaction: (1) 5,6-dihydrouracil16 in tRNA + NAD(P)+ = uracil16 in tRNA + NAD(P)H + H+
(2) 5,6-dihydrouracil17 in tRNA + NAD(P)+ = uracil17 in tRNA + NAD(P)H + H+

Other name(s): Dus1p; tRNA-dihydrouridine synthase 1

Systematic name: tRNA-5,6-dihydrouracil16/17:NAD(P)+ oxidoreductase

Comments: A flavoprotein. The enzyme specifically modifies uracil16 and uracil17 in tRNA.

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

References:

1. Xing, F., Hiley, S.L., Hughes, T.R. and Phizicky, E.M. The specificities of four yeast dihydrouridine synthases for cytoplasmic tRNAs. J. Biol. Chem. 279 (2004) 17850-17860. [PMID: 14970222]

2. Xing, F., Martzen, M.R. and Phizicky, E.M. A conserved family of Saccharomyces cerevisiae synthases effects dihydrouridine modification of tRNA. RNA 8 (2002) 370-381. [PMID: 12003496]

[EC 1.3.1.88 created 2011]

EC 1.3.1.89

Accepted name: tRNA-dihydrouridine47 synthase [NAD(P)+]

Reaction: 5,6-dihydrouracil47 in tRNA + NAD(P)+ = uracil47 in tRNA + NAD(P)H + H+

Other name(s): Dus3p; tRNA-dihydrouridine synthase 3

Systematic name: tRNA-5,6-dihydrouracil47:NAD(P)+ oxidoreductase

Comments: A flavoenzyme. The enzyme specifically modifies uracil47 in tRNA.

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

References:

1. Xing, F., Hiley, S.L., Hughes, T.R. and Phizicky, E.M. The specificities of four yeast dihydrouridine synthases for cytoplasmic tRNAs. J. Biol. Chem. 279 (2004) 17850-17860. [PMID: 14970222]

[EC 1.3.1.89 created 2011]

EC 1.3.1.90

Accepted name: tRNA-dihydrouridine20a/20b synthase [NAD(P)+]

Reaction: (1) 5,6-dihydrouracil20a in tRNA + NAD(P)+ = uracil20a in tRNA + NAD(P)H + H+
(2) 5,6-dihydrouracil20b in tRNA + NAD(P)+ = uracil20b in tRNA + NAD(P)H + H+

Other name(s): Dus4p

Systematic name: tRNA-5,6-dihydrouracil20a/20b:NAD(P)+ oxidoreductase

Comments: A flavoenzyme. The enzyme specifically modifies uracil20a and uracil20b in tRNA.

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

References:

1. Xing, F., Hiley, S.L., Hughes, T.R. and Phizicky, E.M. The specificities of four yeast dihydrouridine synthases for cytoplasmic tRNAs. J. Biol. Chem. 279 (2004) 17850-17860. [PMID: 14970222]

[EC 1.3.1.90 created 2011]

EC 1.3.1.91

Accepted name: tRNA-dihydrouridine20 synthase [NAD(P)+]

Reaction: 5,6-dihydrouracil20 in tRNA + NAD(P)+ = uracil20 in tRNA + NAD(P)H + H+

Other name(s): Dus2p; tRNA-dihydrouridine synthase 2

Systematic name: tRNA-5,6-dihydrouracil20:NAD(P)+ oxidoreductase

Comments: A flavoenzyme [3]. The enzyme specifically modifies uracil20 in tRNA.

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

References:

1. Xing, F., Hiley, S.L., Hughes, T.R. and Phizicky, E.M. The specificities of four yeast dihydrouridine synthases for cytoplasmic tRNAs. J. Biol. Chem. 279 (2004) 17850-17860. [PMID: 14970222]

2. Xing, F., Martzen, M.R. and Phizicky, E.M. A conserved family of Saccharomyces cerevisiae synthases effects dihydrouridine modification of tRNA. RNA 8 (2002) 370-381. [PMID: 12003496]

3. Rider, L.W., Ottosen, M.B., Gattis, S.G. and Palfey, B.A. Mechanism of dihydrouridine synthase 2 from yeast and the importance of modifications for efficient tRNA reduction. J. Biol. Chem. 284 (2009) 10324-10333. [PMID: 19139092]

4. Kato, T., Daigo, Y., Hayama, S., Ishikawa, N., Yamabuki, T., Ito, T., Miyamoto, M., Kondo, S. and Nakamura, Y. A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis. Cancer Res. 65 (2005) 5638-5646. [PMID: 15994936]

[EC 1.3.1.91 created 2011]

EC 1.3.1.92

Accepted name: artemisinic aldehyde Δ11(13)-reductase

Reaction: (11R)-dihydroartemisinic aldehyde + NADP+ = artemisinic aldehyde + NADPH + H+

For diagram of reaction click here.

Other name(s): Dbr2

Systematic name: artemisinic aldehyde:NADP+ oxidoreductase

Comments: Cloned from Artemisia annua. In addition to the reduction of artemisinic aldehyde it is also able to a lesser extent to reduce artemisinic alcohol and artemisinic acid. Part of the biosyntheis of artemisinin.

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

References:

1. Bertea, C.M., Freije, J.R., van der Woude, H., Verstappen, F.W., Perk, L., Marquez, V., De Kraker, J.W., Posthumus, M.A., Jansen, B.J., de Groot, A., Franssen, M.C. and Bouwmeester, H.J. Identification of intermediates and enzymes involved in the early steps of artemisinin biosynthesis in Artemisia annua. Planta Med. 71 (2005) 40-47. [PMID: 15678372]

2. Zhang, Y., Teoh, K.H., Reed, D.W., Maes, L., Goossens, A., Olson, D.J., Ross, A.R. and Covello, P.S. The molecular cloning of artemisinic aldehyde Δ11(13) reductase and its role in glandular trichome-dependent biosynthesis of artemisinin in Artemisia annua. J. Biol. Chem. 283 (2008) 21501-21508. [PMID: 18495659]

[EC 1.3.1.92 created 2012]

EC 1.3.1.93

Accepted name: very-long-chain enoyl-CoA reductase

Reaction: a very-long-chain acyl-CoA + NADP+ = a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+

Glossary: a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms.

Other name(s): TSC13 (gene name); CER10 (gene name)

Systematic name: very-long-chain acyl-CoA:NADP+ oxidoreductase

Comments: This is the fourth component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase.

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

References:

1. Kohlwein, S.D., Eder, S., Oh, C.S., Martin, C.E., Gable, K., Bacikova, D. and Dunn, T. Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae. Mol. Cell Biol. 21 (2001) 109-125. [PMID: 11113186]

2. Gable, K., Garton, S., Napier, J.A. and Dunn, T.M. Functional characterization of the Arabidopsis thaliana orthologue of Tsc13p, the enoyl reductase of the yeast microsomal fatty acid elongating system. J. Exp. Bot. 55 (2004) 543-545. [PMID: 14673020]

3. Kvam, E., Gable, K., Dunn, T.M. and Goldfarb, D.S. Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles. Mol. Biol. Cell 16 (2005) 3987-3998. [PMID: 15958487]

4. Zheng, H., Rowland, O. and Kunst, L. Disruptions of the Arabidopsis Enoyl-CoA reductase gene reveal an essential role for very-long-chain fatty acid synthesis in cell expansion during plant morphogenesis. Plant Cell 17 (2005) 1467-1481. [PMID: 15829606]

[EC 1.3.1.93 created 2012]

EC 1.3.1.94

Accepted name: polyprenol reductase

Reaction: ditrans,polycis-dolichol + NADP+ = ditrans,polycis-polyprenol + NADPH + H+

Other name(s): SRD5A3 (gene name); DFG10 (gene name)

Systematic name: ditrans,polycis-dolichol:NADP+ 2,3-oxidoreductase

Comments: The reaction occurs in the reverse direction with reduction of the terminal double bond next to the alcohol group. Isolated from human fetal brain tissue but present in all eukaryotes. In mammalian cells dolichols are predominantly 18-21 isoprene units in length.

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

References:

1. Sagami, H., Kurisaki, A. and Ogura, K. Formation of dolichol from dehydrodolichol is catalyzed by NADPH-dependent reductase localized in microsomes of rat liver. J. Biol. Chem. 268 (1993) 10109-10113. [PMID: 8486680]

2. Cantagrel, V., Lefeber, D.J., Ng, B.G., Guan, Z., Silhavy, J.L., Bielas, S.L., Lehle, L., Hombauer, H., Adamowicz, M., Swiezewska, E., De Brouwer, A.P., Blumel, P., Sykut-Cegielska, J., Houliston, S., Swistun, D., Ali, B.R., Dobyns, W.B., Babovic-Vuksanovic, D., van Bokhoven, H., Wevers, R.A., Raetz, C.R., Freeze, H.H., Morava, E., Al-Gazali, L. and Gleeson, J.G. SRD5A3 is required for converting polyprenol to dolichol and is mutated in a congenital glycosylation disorder. Cell 142 (2010) 203-217. [PMID: 20637498]

[EC 1.3.1.94 created 2012]

EC 1.3.1.95

Accepted name: acrylyl-CoA reductase (NADH)

Reaction: propanoyl-CoA + NAD+ = acrylyl-CoA + NADH + H+

For diagram of reaction click here.

Glossary: propanoyl-CoA = propionyl-CoA

Systematic name: propanoyl-CoA:NAD+ oxidoreductase

Comments: Contains FAD. The reaction is catalysed in the opposite direction to that shown. The enzyme from the bacterium Clostridium propionicum is a complex that includes an electron-transfer flavoprotein (ETF). The ETF is reduced by NADH and transfers the electrons to the active site. Catalyses a step in a pathway for L-alanine fermentation to propanoate [1]. cf. EC 1.3.1.84, acrylyl-CoA reductase (NADPH).

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

References:

1. Hetzel, M., Brock, M., Selmer, T., Pierik, A.J., Golding, B.T. and Buckel, W. Acryloyl-CoA reductase from Clostridium propionicum. An enzyme complex of propionyl-CoA dehydrogenase and electron-transferring flavoprotein. Eur. J. Biochem. 270 (2003) 902-910. [PMID: 12603323]

2. Kandasamy, V., Vaidyanathan, H., Djurdjevic, I., Jayamani, E., Ramachandran, K.B., Buckel, W., Jayaraman, G. and Ramalingam, S. Engineering Escherichia coli with acrylate pathway genes for propionic acid synthesis and its impact on mixed-acid fermentation. Appl. Microbiol. Biotechnol. (2012) . [PMID: 22810300]

[EC 1.3.1.95 created 2012]

EC 1.3.1.96

Accepted name: Botryococcus squalene synthase

Reaction: squalene + diphosphate + NADP+ = presqualene diphosphate + NADPH + H+

For diagram of reaction click here.

Other name(s): SSL-2 (gene name)

Systematic name: squalene:NADP+ oxidoreductase

Comments: Isolated from the green alga Botryococcus braunii BOT22. Acts in the reverse direction. cf. EC 2.5.1.21, squalene synthase, where squalene is formed directly from farnesyl diphosphate.

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

References:

1. Niehaus, T.D., Okada, S., Devarenne, T.P., Watt, D.S., Sviripa, V. and Chappell, J. Identification of unique mechanisms for triterpene biosynthesis in Botryococcus braunii. Proc. Natl. Acad. Sci. USA 108 (2011) 12260-12265. [PMID: 21746901]

[EC 1.3.1.96 created 2012]

EC 1.3.1.97

Accepted name: botryococcene synthase

Reaction: C30 botryococcene + NADP+ + diphosphate = presqualene diphosphate + NADPH + H+

For diagram of reaction click here.

Glossary: C30 botryococcene = (10S,13R)-10-ethenyl-2,6,10,13,17,21-hexamethyldocosa-2,5,11,16,20-pentaene

Other name(s): SSL-3 (gene name)

Systematic name: C30 botryococcene:NADP+ oxidoreductase

Comments: Isolated from the green alga Botryococcus braunii BOT22. Acts in the reverse direction. Involved in the production of botryococcenes, which are triterpenoid hydrocarbons of isoprenoid origin produced in large amount by this alga.

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

References:

1. Niehaus, T.D., Okada, S., Devarenne, T.P., Watt, D.S., Sviripa, V. and Chappell, J. Identification of unique mechanisms for triterpene biosynthesis in Botryococcus braunii. Proc. Natl. Acad. Sci. USA 108 (2011) 12260-12265. [PMID: 21746901]

[EC 1.3.1.97 created 2012]

EC 1.3.1.98

Accepted name: UDP-N-acetylmuramate dehydrogenase

Reaction: UDP-N-acetyl-α-D-muramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-α-D-glucosamine + NADPH + H+

Other name(s): MurB reductase; UDP-N-acetylenolpyruvoylglucosamine reductase; UDP-N-acetylglucosamine-enoylpyruvate reductase; UDP-GlcNAc-enoylpyruvate reductase; uridine diphosphoacetylpyruvoylglucosamine reductase; uridine diphospho-N-acetylglucosamine-enolpyruvate reductase; uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase

Systematic name: UDP-N-acetyl-α-D-muramate:NADP+ oxidoreductase

Comments: A flavoprotein (FAD). NADH can to a lesser extent replace NADPH.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 39307-28-3

References:

1. Taku, A. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. IV. Activation of uridine diphospho-N-acetylenolpyruvylglucosamine reductase by monovalent cations. J. Biol. Chem. 248 (1973) 4971. [PMID: 4717533]

2. Taku, A., Gunetileke, K.G. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3. Purification and properties of uridine diphospho-N-acetylenolpyruvyl-glucosamine reductase. J. Biol. Chem. 245 (1970) 5012-5016. [PMID: 4394163]

3. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]

[EC 1.3.1.98 created 1976 as EC 1.1.1.158, modified 1983, modified 2002, transferred 2013 to EC 1.3.1.98]

EC 1.3.1.99

Accepted name: iridoid synthase

Reaction: (6E)-8-oxogeranial + NAD(P)H + H+ = cis-trans-nepetalactol + NAD(P)+

For diagram of reaction click here.

Glossary: cis-trans-nepetalactol = (4aS,7S,7aR)-4,7-dimethyl-1,4a,5,6,7,7a-hexahydrocyclopenta[c]pyran-1-ol

Systematic name: 8-oxogeranial:NAD(P)+ oxidoreductase (cyclizing, cis-trans-nepetalactol forming)

Comments: Isolated from the plant Catharanthus roseus. The reaction may involve cyclization via a Diels-Alder or Michael reaction. Iridoids are involved in the biosynthesis of many indole alkaloids. The cyclic hemiacetal is readily hydrolysed to the corresponding dial.

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

References:

1. Geu-Flores, F., Sherden, N.H., Courdavault, V., Burlat, V., Glenn, W.S., Wu, C., Nims, E., Cui, Y. and O'Connor, S.E. An alternative route to cyclic terpenes by reductive cyclization in iridoid biosynthesis. Nature 492 (2012) 138-142. [PMID: 23172143]

[EC 1.3.1.99 created 2013]

EC 1.3.1.100

Accepted name: chanoclavine-I aldehyde reductase

Reaction: dihydrochanoclavine-I aldehyde + NADP+ = chanoclavine-I aldehyde + NADPH + H+

For diagram of reaction click here.

Glossary: chanoclavine-I aldehyde = (1E)-2-methyl-3-[(4R,5R)-4-(methylamino)-1,3,4,5-tetrahydrobenz[cd]indol-5-yl]prop-2-enal

Other name(s): FgaOx3; easA (gene name)

Systematic name: chanoclavine-I aldehyde:NAD+ oxidoreductase

Comments: Contains FMN. The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family. The enzyme catalyses the reduction of chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde. This hydrolyses spontaneously to form 6,8-dimethyl-6,7-didehydroergoline, which is converted to festuclavine by EC 1.5.1.44, festuclavine dehydrogenase.

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

References:

1. Coyle, C.M., Cheng, J.Z., O'Connor, S.E. and Panaccione, D.G. An old yellow enzyme gene controls the branch point between Aspergillus fumigatus and Claviceps purpurea ergot alkaloid pathways. Appl. Environ. Microbiol. 76 (2010) 3898-3903. [PMID: 20435769]

2. Cheng, J.Z., Coyle, C.M., Panaccione, D.G. and O'Connor, S.E. A role for Old Yellow Enzyme in ergot alkaloid biosynthesis. J. Am. Chem. Soc. 132 (2010) 1776-1777. [PMID: 20102147]

3. Wallwey, C., Matuschek, M., Xie, X.L. and Li, S.M. Ergot alkaloid biosynthesis in Aspergillus fumigatus: Conversion of chanoclavine-I aldehyde to festuclavine by the festuclavine synthase FgaFS in the presence of the old yellow enzyme FgaOx3. Org. Biomol. Chem. 8 (2010) 3500-3508. [PMID: 20526482]

4. Xie, X., Wallwey, C., Matuschek, M., Steinbach, K. and Li, S.M. Formyl migration product of chanoclavine-I aldehyde in the presence of the old yellow enzyme FgaOx3 from Aspergillus fumigatus: a NMR structure elucidation. Magn. Reson. Chem. 49 (2011) 678-681. [PMID: 21898587]

[EC 1.3.1.100 created 2013]

EC 1.3.1.101

Accepted name: 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H]

Reaction: 2,3-bis-(O-phytanyl)-sn-glycerol 1-phosphate + 8 NAD(P)+ = 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+

For diagram of reaction click here.

Glossary: phytanol = (7R,11R,15R)-3,7,11,15-tetramethylhexadecan-1-ol

Other name(s): digeranylgeranylglycerophospholipid reductase; Ta0516m (gene name); DGGGPL reductase; 2,3-digeranylgeranylglycerophospholipid reductase

Systematic name: 2,3-bis-(O-phytany)l-sn-glycerol 1-phosphate:NAD(P)+ oxidoreductase

Comments: A flavoprotein (FAD). The enzyme from the archaeon Thermoplasma acidophilum is involved in the biosynthesis of membrane lipids. In vivo the reaction occurs in the reverse direction with the formation of 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate. cf. EC 1.3.99.34, 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase (donor).

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

References:

1. Nishimura, Y. and Eguchi, T. Biosynthesis of archaeal membrane lipids: digeranylgeranylglycerophospholipid reductase of the thermoacidophilic archaeon Thermoplasma acidophilum. J. Biochem. 139 (2006) 1073-1081. [PMID: 16788058]

2. Nishimura, Y. and Eguchi, T. Stereochemistry of reduction in digeranylgeranylglycerophospholipid reductase involved in the biosynthesis of archaeal membrane lipids from Thermoplasma acidophilum. Bioorg. Chem. 35 (2007) 276-283. [PMID: 17275067]

3. Xu, Q., Eguchi, T., Mathews, I.I., Rife, C.L., Chiu, H.J., Farr, C.L., Feuerhelm, J., Jaroszewski, L., Klock, H.E., Knuth, M.W., Miller, M.D., Weekes, D., Elsliger, M.A., Deacon, A.M., Godzik, A., Lesley, S.A. and Wilson, I.A. Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme in the biosynthesis of archaeal membrane lipids. J. Mol. Biol. 404 (2010) 403-417. [PMID: 20869368]

[EC 1.3.1.101 created 2013]

EC 1.3.1.102

Accepted name: 2-alkenal reductase (NADP+)

Reaction: an n-alkanal + NADP+ = an alk-2-enal + NADPH + H+

Other name(s): NADPH-dependent alkenal/one oxidoreductase; NADPH:2-alkenal α,β-hydrogenase

Systematic name: n-alkanal:NADP+ 2-oxidoreductase

Comments: Shows highest activity with 1-nitrocyclohexene but also has significant activity with 2-methylpentenal and trans-cinnamaldehyde [3]. Involved in the detoxication of α,β-unsaturated aldehydes and ketones. Has very low activity with NAD as reductant (cf. EC 1.3.1.74, 2-alkenal reductase [NAD(P)+]).

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

References:

1. Hirata, T., Tamura, Y., Yokobatake, N., Shimoda, K. and Ashida, Y. A 38 kDa allylic alcohol dehydrogenase from the cultured cells of Nicotiana tabacum. Phytochemistry 55 (2000) 297-303. [PMID: 11117876]

2. Matsushima, A., Sato, Y., Otsuka, M., Watanabe, T., Yamamoto, H. and Hirata, T. An enone reductase from Nicotiana tabacum: cDNA cloning, expression in Escherichia coli, and reduction of enones with the recombinant proteins. Bioorg. Chem. 36 (2008) 23-28. [PMID: 17945329]

3. Mansell, D.J., Toogood, H.S., Waller, J., Hughes, J.M.X., Levy, C.W., Gardiner, J.M., and Scrutton, N.S. Biocatalytic asymmetric alkene reduction: crystal structure and characterization of a double bond reductase from Nicotiana tabacum. ACS Catal. 3 (2013) 370-379.

[EC 1.3.1.102 created 2013]

EC 1.3.1.103

Accepted name: 2-haloacrylate reductase

Reaction: (S)-2-chloropropanoate + NADP+ = 2-chloroacrylate + NADPH + H+

Other name(s): CAA43 (gene name)

Systematic name: (S)-2-chloropropanoate:NADP+ oxidoreductase

Comments: The enzyme acts in the degradation pathway of unsaturated organohalogen compounds by the bacterium Burkholderia sp. WS.

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

References:

1. Kurata, A., Kurihara, T., Kamachi, H. and Esaki, N. 2-Haloacrylate reductase, a novel enzyme of the medium chain dehydrogenase/reductase superfamily that catalyzes the reduction of a carbon-carbon double bond of unsaturated organohalogen compounds. J. Biol. Chem. 280 (2005) 20286-20291. [PMID: 15781461]

[EC 1.3.1.103 created 2013]

EC 1.3.1.104

Accepted name: enoyl-[acyl-carrier-protein] reductase

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-ACP reductase (ambiguous); fabL (gene name)

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

Comments: The 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 the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)].

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

References:

1. 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]

2. Kim, K.H., Park, J.K., Ha, B.H., Moon, J.H. and Kim, E.E. Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 (2007) 246-248. [PMID: 17329825]

3. 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 1.3.1.104 created 2013]

EC 1.3.1.105

Accepted name: 2-methylene-furan-3-one reductase

Reaction: 4-hydroxy-2,5-dimethylfuran-3(2H)-one + NAD(P)+ = 4-hydroxy-5-methyl-2-methylenefuran-3(2H)-one + NAD(P)H + H+

Other name(s): FaEO; SIEO; enone oxidoreductase; 4-hydroxy-2,5-dimethylfuran-3(2H)-one:NAD(P)+ oxidoreductase

Systematic name: 4-hydroxy-2,5-dimethylfuran-3(2H)-one:NAD(P)+ oxidoreductase

Comments: In the fruit-ripening process of strawberry (Fragaria x ananassa) the reaction is catalysed in the reverse direction from that shown. 4-hydroxy-2,5-dimethylfuran-3(2H)-one is one of the major aroma compounds in the fruits. The enzyme has also been detected in tomato (Solanum lycopersicum) fruits [2]. NADPH is the preferred cofactor.

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

References:

1. Raab, T., Lopez-Raez, J.A., Klein, D., Caballero, J.L., Moyano, E., Schwab, W. and Munoz-Blanco, J. FaQR, required for the biosynthesis of the strawberry flavor compound 4-hydroxy-2,5-dimethyl-3(2H)-furanone, encodes an enone oxidoreductase. Plant Cell 18 (2006) 1023-1037. [PMID: 16517758]

2. Klein, D., Fink, B., Arold, B., Eisenreich, W. and Schwab, W. Functional characterization of enone oxidoreductases from strawberry and tomato fruit. J. Agric. Food Chem. 55 (2007) 6705-6711. [PMID: 17636940]

3. Schiefner, A., Sinz, Q., Neumaier, I., Schwab, W. and Skerra, A. Structural basis for the enzymatic formation of the key strawberry flavor compound 4-hydroxy-2,5-dimethyl-3(2H)-furanone. J. Biol. Chem. 288 (2013) 16815-16826. [PMID: 23589283]

4. Uehara, K., Watanabe, J., Mogi, Y. and Tsukioka, Y. Identification and characterization of an enzyme involved in the biosynthesis of the 4-hydroxy-2(or 5)-ethyl-5(or 2)-methyl-3(2H)-furanone in yeast. J. Biosci. Bioeng. 123 (2017) 333-341. [PMID: 27865643]

[EC 1.3.1.105 created 2013]

EC 1.3.1.106

Accepted name: cobalt-precorrin-6A reductase

Reaction: cobalt-precorrin-6B + NAD+ = cobalt-precorrin-6A + NADH + H+

For diagram of reaction click here.

Other name(s): cbiJ (gene name)

Systematic name: cobalt-precorrin-6B:NAD+ oxidoreductase

Comments: The enzyme catalyses a step in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis. The enzyme from the bacterium Bacillus megaterium has no activity with NADPH. The equivalent enzyme in the aerobic pathway is EC 1.3.1.54, precorrin-6A reductase.

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

References:

1. Kim, W., Major, T.A. and Whitman, W.B. Role of the precorrin 6-X reductase gene in cobamide biosynthesis in Methanococcus maripaludis. Archaea 1 (2005) 375-384. [PMID: 16243778]

2. Moore, S.J., Lawrence, A.D., Biedendieck, R., Deery, E., Frank, S., Howard, M.J., Rigby, S.E. and Warren, M.J. Elucidation of the anaerobic pathway for the corrin component of cobalamin (vitamin B12). Proc. Natl. Acad. Sci. USA 110 (2013) 14906-14911. [PMID: 23922391]

[EC 1.3.1.106 created 2014]

EC 1.3.1.107

Accepted name: sanguinarine reductase

Reaction: (1) dihydrosanguinarine + NAD(P)+ = sanguinarine + NAD(P)H + H+
(2) dihydrochelirubine + NAD(P)+ = chelirubine + NAD(P)H + H+

For diagram of reaction click here.

Glossary: sanguinarine = 13-methyl-2H,10H-[1,3]dioxolo[4,5-i][1,3]dioxolo[4',5':4,5]benzo[1,2-c]phenanthridinium
dihydrosanguinarine = 13-methyl-13,14-dihydro-2H,10H-[1,3]dioxolo[4,5-i][1,3]dioxolo[4',5':4,5]benzo[1,2-c]phenanthridine
chelirubine = 5-methoxy-13-methyl-2H,10H-[1,3]dioxolo[4,5-i][1,3]dioxolo[4',5':4,5]benzo[1,2-c]phenanthridinium
dihydrochelirubine = 5-methoxy-13-methyl-13,14-dihydro-2H,10H-[1,3]dioxolo[4,5-i][1,3]dioxolo[4',5':4,5]benzo[1,2-c]phenanthridinium

Systematic name: dihydrosanguinarine:NAD(P)+ oxidoreductase

Comments: The enzyme, purified from the California poppy (Eschscholzia californica), is involved in detoxifying the phytoalexin sanguinarine produced by poppy itself (cf. EC 1.5.3.12, dihydrobenzophenanthridine oxidase), when it binds to the cell wall of the poppy cell. The reaction with NADPH is up to three times faster than that with NADH at low concentrations (<10 μM) of the dinucleotide. At higher concentrations the reaction with NADPH is inhibited but not that with NADH [1].

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

References:

1. Weiss, D., Baumert, A., Vogel, M. and Roos, W. Sanguinarine reductase, a key enzyme of benzophenanthridine detoxification. Plant Cell Environ 29 (2006) 291-302. [PMID: 17080644]

2. Vogel, M., Lawson, M., Sippl, W., Conrad, U. and Roos, W. Structure and mechanism of sanguinarine reductase, an enzyme of alkaloid detoxification. J. Biol. Chem. 285 (2010) 18397-18406. [PMID: 20378534]

[EC 1.3.1.107 created 2014]

EC 1.3.1.108

Accepted name: caffeoyl-CoA reductase

Reaction: 3-(3,4-dihydroxyphenyl)propanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster = (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster

Glossary: (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA = (2E)-3-(3,4-dihydroxyphenyl)acryloyl-CoA = trans-caffeoyl-CoA
3-(3,4-dihydroxyphenyl)propanoyl-CoA = hydrocaffeoyl-CoA

Other name(s): electron-bifurcating caffeoyl-CoA reductase; caffeoyl-CoA reductase-Etf complex; hydrocaffeoyl-CoA:NAD+,ferredoxin oxidoreductase

Systematic name: 3-(3,4-dihydroxyphenyl)propanoyl-CoA:NAD+,ferredoxin oxidoreductase

Comments: The enzyme, characterized from the bacterium Acetobacterium woodii, contains two [4Fe-4S] clusters and FAD. The enzyme couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant. It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. It also reduces 4-coumaroyl-CoA and feruloyl-CoA.

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

References:

1. Bertsch, J., Parthasarathy, A., Buckel, W. and Muller, V. An electron-bifurcating caffeyl-CoA reductase. J. Biol. Chem. 288 (2013) 11304-11311. [PMID: 23479729]

[EC 1.3.1.108 created 2015]

EC 1.3.1.109

Accepted name: butanoyl-CoA dehydrogenase (NAD+, ferredoxin)

Reaction: butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster = (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster

Glossary: (E)-but-2-enoyl-CoA = crotonyl-CoA

Other name(s): bifurcating butyryl-CoA dehydrogenase; butyryl-CoA dehydrogenase/Etf complex; Etf-Bcd complex; bifurcating butanoyl-CoA dehydrogenase; butanoyl-CoA dehydrogenase/Etf complex

Systematic name: butanoyl-CoA:NAD+,ferredoxin oxidoreductase

Comments: This flavin containg enzyme, isolated from the bacteria Acidaminococcus fermentans and butanoate-producing Clostridia species, couples the exergonic reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA with NADH to the endergonic reduction of ferredoxin by NADH, using electron bifurcation to overcome the steep energy barrier in ferredoxin reduction.

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

References:

1. Li, F., Hinderberger, J., Seedorf, H., Zhang, J., Buckel, W. and Thauer, R.K. Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri. J. Bacteriol. 190 (2008) 843-850. [PMID: 17993531]

2. Aboulnaga el,-H., Pinkenburg, O., Schiffels, J., El-Refai, A., Buckel, W. and Selmer, T. Effect of an oxygen-tolerant bifurcating butyryl coenzyme A dehydrogenase/electron-transferring flavoprotein complex from Clostridium difficile on butyrate production in Escherichia coli. J. Bacteriol. 195 (2013) 3704-3713. [PMID: 23772070]

3. Chowdhury, N.P., Mowafy, A.M., Demmer, J.K., Upadhyay, V., Koelzer, S., Jayamani, E., Kahnt, J., Hornung, M., Demmer, U., Ermler, U. and Buckel, W. Studies on the mechanism of electron bifurcation catalyzed by electron transferring flavoprotein (Etf) and butyryl-CoA dehydrogenase (Bcd) of Acidaminococcus fermentans. J. Biol. Chem. 289 (2014) 5145-5157. [PMID: 24379410]

[EC 1.3.1.109 created 2015]

EC 1.3.1.110

Accepted name: lactate dehydrogenase (NAD+, ferredoxin)

Reaction: lactate + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster = pyruvate + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster

Other name(s): electron bifurcating LDH/Etf complex

Systematic name: lactate:NAD+, ferredoxin oxidoreductase

Comments: The enzyme, isolated from the bacterium Acetobacterium woodii, uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+.

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

References:

1. Weghoff, M.C., Bertsch, J. and Muller, V. A novel mode of lactate metabolism in strictly anaerobic bacteria. Environ Microbiol 17 (2015) 670-677. [PMID: 24762045]

[EC 1.3.1.110 created 2015]

EC 1.3.1.111

Accepted name: geranylgeranyl-bacteriochlorophyllide a reductase

Reaction: bacteriochlorophyll a + 3 NADP+ = geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+

Other name(s): bchP (gene name)

Systematic name: bacteriochlorophyll a:NADP+ oxidoreductase (geranylgeranyl-reducing)

Comments: The enzyme catalyses the successive reduction of the geranylgeraniol esterifying group to phytol, reducing three out of four double bonds, and transforming geranylgeranyl bacteriochlorophyllide a via dihydrogeranylgeranyl bacteriochlorophyllide a and tetrahydrogeranylgeranyl bacteriochlorophyllide a to bacteriochlorophyll a. The enzyme can also accept the pheophytin derivative geranylgeranyl bacteriopheophytin, converting it to bacteriopheophytin a.

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

References:

1. Bollivar, D.W., Wang, S., Allen, J.P. and Bauer, C.E. Molecular genetic analysis of terminal steps in bacteriochlorophyll a biosynthesis: characterization of a Rhodobacter capsulatus strain that synthesizes geranylgeraniol-esterified bacteriochlorophyll a, Biochemistry 33 (1994) 12763-12768. [PMID: 7947681]

2. Addlesee, H.A. and Hunter, C.N. Physical mapping and functional assignment of the geranylgeranyl-bacteriochlorophyll reductase gene, bchP, of Rhodobacter sphaeroides, J. Bacteriol. 181 (1999) 7248-7255. [PMID: 10572128]

3. Addlesee, H.A. and Hunter, C.N. Rhodospirillum rubrum possesses a variant of the bchP gene, encoding geranylgeranyl-bacteriopheophytin reductase. J. Bacteriol. 184 (2002) 1578-1586. [PMID: 11872709]

4. Harada, J., Miyago, S., Mizoguchi, T., Azai, C., Inoue, K., Tamiaki, H. and Oh-oka, H. Accumulation of chlorophyllous pigments esterified with the geranylgeranyl group and photosynthetic competence in the CT2256-deleted mutant of the green sulfur bacterium Chlorobium tepidum, Photochem Photobiol Sci 7 (2008) 1179-1187. [PMID: 18846281]

[EC 1.3.1.111 created 2016]

EC 1.3.1.112

Accepted name: anthocyanidin reductase [(2S)-flavan-3-ol-forming]

Reaction: (1) a (2S,3R)-flavan-3-ol + 2 NADP+ = an anthocyanidin with a 3-hydroxy group + 2 NADPH + H+
(2) a (2S,3S)-flavan-3-ol + 2 NADP+ = an anthocyanidin with a 3-hydroxy group + 2 NADPH + H+

Systematic name: (2S)-flavan-3-ol:NAD(P)+ oxidoreductase

Comments: The enzyme, characterized from Vitis vinifera (grape), participates in the flavonoid biosynthesis pathway. It catalyses the double reduction of anthocyanidins, producing a mixture of (2S,3S)- and (2S,3R)-flavan-3-ols. The enzyme catalyses sequential hydride transfers to C-2 and C-4, respectively. Epimerization at C-3 is achieved by tautomerization that occurs between the two hydride transfers. cf. EC 1.3.1.77, anthocyanidin reductase [(2R,3R)-flavan-3-ol-forming].

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

References:

1. Gargouri, M., Manigand, C., Mauge, C., Granier, T., Langlois d'Estaintot, B., Cala, O., Pianet, I., Bathany, K., Chaudiere, J. and Gallois, B. Structure and epimerase activity of anthocyanidin reductase from Vitis vinifera. Acta Crystallogr. D Biol. Crystallogr. 65 (2009) 989-1000. [PMID: 19690377]

2. Gargouri, M., Chaudiere, J., Manigand, C., Mauge, C., Bathany, K., Schmitter, J.M. and Gallois, B. The epimerase activity of anthocyanidin reductase from Vitis vinifera and its regiospecific hydride transfers. Biol. Chem. 391 (2010) 219-227. [PMID: 20030585]

[EC 1.3.1.112 created 2016]


Continued with EC 1.3.2 to EC 1.3.99
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