Continued from EC 1.3.1.1 to EC 1.3.1.50
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 1.3.1.52 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)]
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]
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; 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, 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. [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 1.3.1.55 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)]
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, KEGG, Metacyc, PDB, 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]
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, 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]
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, EAWAG-BBD, EXPASY, 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. [PMID: 8631713]
[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)]
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, EAWAG-BBD, EXPASY, KEGG, Metacyc, 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 1.3.1.61 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)]
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, EAWAG-BBD, EXPASY, 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. [PMID: 8180704]
[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)]
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, KEGG, Metacyc, 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]
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, 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]
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, 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]
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, 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]
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, 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]
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.
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, 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. [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]
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]
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]
Accepted name: 1,2-dihydrovomilenine 19,20-reductase
Reaction: 17-O-acetylnorajmaline + NADP+ = (2R)-1,2-dihydrovomilenine + NADPH + H+
For diagram of reaction, 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, 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]
2. Guo, J., Gao, D., Lian, J. and Qu, Y. De novo biosynthesis of antiarrhythmic alkaloid ajmaline. Nat. Commun. 15 (2024) 457. [PMID: 38212296]
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]
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]
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]
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]
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]
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 (ambiguous); 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 1.3.1.80 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)]
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, PDB, 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]
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, PDB, 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]
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, PDB, 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]
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, PDB, 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]
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]
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]
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, EAWAG-BBD, EXPASY, KEGG, Metacyc, 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]
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]
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]
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]
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, PDB, 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]
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, PDB, 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]
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-CoA 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]
Accepted name: polyprenal reductase
Reaction: a dolichal + NADP+ = a ditrans,polycis-polyprenal + NADPH + H+
Other name(s): SRD5A3 (gene name); DFG10 (gene name); polyprenol reductase (incorrect); ditrans,polycis-dolichol:NADP+ 2,3-oxidoreductase (incorrect)
Systematic name: dolichal:NADP+ 2,3-oxidoreductase
Comments: The enzyme, isolated from human fetal brain tissue but present in all eukaryotes, catalyses the reduction of the terminal double bond next to the aldehyde group in ditrans,polycis-polyprenal, as part of the pathway that produces dolichol. 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]
3. Wilson, M.P., Kentache, T., Althoff, C.R., Schulz, C., de Bettignies, G., Mateu Cabrera, G., Cimbalistiene, L., Burnyte, B., Yoon, G., Costain, G., Vuillaumier-Barrot, S., Cheillan, D., Rymen, D., Rychtarova, L., Hansikova, H., Bury, M., Dewulf, J.P., Caligiore, F., Jaeken, J., Cantagrel, V., Van Schaftingen, E., Matthijs, G., Foulquier, F. and Bommer, G.T. A pseudoautosomal glycosylation disorder prompts the revision of dolichol biosynthesis. Cell (2024) . [PMID: 38821050]
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]
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]
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]
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 1.3.1.99 Deleted entry: iridoid synthase. Now known to be catalyzed by two different enzymes, EC 1.3.1.122, (S)-8-oxocitronellyl enol synthase, and EC 5.5.1.34, (+)-cis,trans-nepetalactol synthase (EC 1.3.1.99 created 2013, deleted 2019)]
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, PDB, 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]
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, PDB, 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]
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, PDB, 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.
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, PDB, 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]
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]
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, PDB, 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]
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, which participates in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis, catalyses the reduction of the double bond between C-18 and C-19 of cobalt-precorrin-6A. The enzyme from the bacterium Bacillus megaterium has no activity with NADPH. See EC 1.3.1.54, precorrin-6A reductase, for the corresponding enzyme that participates in the aerobic cobalamin biosynthesis pathway.
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]
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]
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, PDB, 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]
Accepted name: butanoyl-CoA dehydrogenase complex (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; butanoyl-CoA dehydrogenase (NAD+, ferredoxin)
Systematic name: butanoyl-CoA:NAD+, ferredoxin oxidoreductase
Comments: The enzyme is a complex of a flavin-containing dehydrogenase component (Bcd) and an electron-transfer flavoprotein dimer (EtfAB). The enzyme complex, isolated from the bacteria Acidaminococcus fermentans and butanoate-producing Clostridia species, couples the exergonic reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA by 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]
4. Chowdhury, N.P., Kahnt, J. and Buckel, W. Reduction of ferredoxin or oxygen by flavin-based electron bifurcation in Megasphaera elsdenii. FEBS J. 282 (2015) 3149-3160. [PMID: 25903584]
[EC 1.3.1.110 Transferred entry: lactate dehydrogenase (NAD+, ferredoxin). Now EC 1.1.1.436, lactate dehydrogenase (NAD+,ferredoxin) (EC 1.3.1.110 created 2015, deleted 2022)]
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]
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, PDB, 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]
Accepted name: (4-alkanoyl-5-oxo-2,5-dihydrofuran-3-yl)methyl phosphate reductase
Reaction: a [(3S,4R)-4-alkanoyl-5-oxooxolan-3-yl]methyl phosphate + NADP+ = a (4-alkanoyl-5-oxo-2,5-dihydrofuran-3-yl)methyl phosphate + NADPH + H+
Other name(s): bprA (gene name); scbC (gene name)
Systematic name: [(3S,4R)-4-alkanoyl-5-oxooxolan-3-yl]methyl-phosphate:NADP+ oxidoreductase
Comments: The enzyme, characterized from the bacteria Streptomyces griseus and Streptomyces coelicolor, is involved in the biosynthesis of γ-butyrolactone autoregulators that control secondary metabolism and morphological development in Streptomyces bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kato, J.Y., Funa, N., Watanabe, H., Ohnishi, Y. and Horinouchi, S. Biosynthesis of γ-butyrolactone autoregulators that switch on secondary metabolism and morphological development in Streptomyces. Proc. Natl Acad. Sci. USA 104 (2007) 2378-2383. [PMID: 17277085]
2. Biarnes-Carrera, M., Lee, C.K., Nihira, T., Breitling, R. and Takano, E. Orthogonal regulatory circuits for Escherichia coli based on the γ-butyrolactone system of Streptomyces coelicolor. ACS Synth. Biol. 7 (2018) 1043-1055. [PMID: 29510026]
Accepted name: 3-dehydro-bile acid Δ4,6-reductase
Reaction: (1) 3-oxocholan-24-oyl-CoA + NAD+ = 3-oxochol-4-en-24-oyl-CoA + NADH + H+
(2) 3-oxochol-4-en-24-oyl-CoA + NAD+ = 3-oxochol-4,6-dien-24-oyl-CoA + NADH + H+
(3) 12α-hydroxy-3-oxocholan-24-oyl-CoA + NAD+ = 12α-hydroxy-3-oxochol-4-en-24-oyl-CoA + NADH + H+
(4) 12α-hydroxy-3-oxochol-4-en-24-oyl-CoA + NAD+ = 12α-hydroxy-3-oxochol-4,6-dien-24-oyl-CoA + NADH + H+
Other name(s): baiN (gene name)
Systematic name: 3-oxocholan-24-oyl-CoA Δ4,6-oxidoreductase
Comments: Contains flavin. The enzyme, characterized from the bacterium Clostridium scindens, participates in the bile acid 7α-dehydroxylation pathway. The enzyme catalyses two subsequent reductions of the double bonds within the bile acid A/B rings, following 7α-dehydration.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Harris, S.C., Devendran, S., Alves, J.MP., Mythen, S.M., Hylemon, P.B. and Ridlon, J.M. Identification of a gene encoding a flavoprotein involved in bile acid metabolism by the human gut bacterium Clostridium scindens ATCC 35704. Biochim. Biophys. Acta 1863 (2018) 276-283. [PMID: 29217478]
Accepted name: 3-oxocholoyl-CoA 4-desaturase
Reaction: (1) 7α,12α-dihydroxy-3-oxochol-24-oyl-CoA + NAD+ = 7α,12α-dihydroxy-3-oxochol-4-en-24-oyl-CoA + NADH + H+
(2) 7α-hydroxy-3-oxochol-24-oyl-CoA + NAD+ = 7α-hydroxy-3-oxochol-4-en-24-oyl-CoA + NADH + H+
Glossary: 7α,12α-dihydroxy-3-oxochol-24-oyl-CoA = 3-oxocholoyl-CoA
7α-hydroxy-3-oxochol-24-oyl-CoA = 3-oxochenodeoxycholoyl-CoA
Other name(s): baiCD (gene name); 3-oxo-choloyl-CoA dehydrogenase
Systematic name: 3-oxocholoyl-CoA Δ4-oxidoreductase
Comments: Contains flavin. The enzyme, characterized from the bacterium Clostridium scindens, participates in the bile acid 7α-dehydroxylation pathway. The enzyme catalyses the stereo-specific oxidation of its substrates and has no activity with the 7β anomers. cf. EC 1.3.1.116, 7β-hydroxy-3-oxochol-24-oyl-CoA 4-desaturase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kang, D.J., Ridlon, J.M., Moore, D.R., 2nd, Barnes, S. and Hylemon, P.B. Clostridium scindens baiCD and baiH genes encode stereo-specific 7α/7β-hydroxy-3-oxo-Δ4-cholenoic acid oxidoreductases. Biochim. Biophys. Acta 1781 (2008) 16-25. [PMID: 18047844]
Accepted name: 7β-hydroxy-3-oxochol-24-oyl-CoA 4-desaturase
Reaction: 7β-hydroxy-3-oxochol-24-oyl-CoA + NAD+ = 7β-hydroxy-3-oxochol-4-en-24-oyl-CoA + NADH + H+
Other name(s): baiH (gene name)
Systematic name: 7β-hydroxy-3-oxochol-24-oyl-CoA Δ4-oxidoreductase
Comments: Contains FAD and FMN. The enzyme, characterized from the bacterium Clostridium scindens, participates in the bile acid 7α-dehydroxylation pathway. The enzyme catalyses the stereo-specific oxidation of its substrate and has no activity with the 7α anomer. cf. EC 1.3.1.115, 3-oxocholoyl-CoA 4-desaturase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Baron, S.F. and Hylemon, P.B. Expression of the bile acid-inducible NADH:flavin oxidoreductase gene of Eubacterium sp. VPI 12708 in Escherichia coli. Biochim. Biophys. Acta 1249 (1995) 145-154. [PMID: 7599167]
2. Franklund, C.V., Baron, S.F. and Hylemon, P.B. Characterization of the baiH gene encoding a bile acid-inducible NADH:flavin oxidoreductase from Eubacterium sp. strain VPI 12708. J. Bacteriol. 175 (1993) 3002-3012. [PMID: 8491719]
3. Kang, D.J., Ridlon, J.M., Moore, D.R., 2nd, Barnes, S. and Hylemon, P.B. Clostridium scindens baiCD and baiH genes encode stereo-specific 7α/7β-hydroxy-3-oxo-Δ4-cholenoic acid oxidoreductases. Biochim. Biophys. Acta 1781 (2008) 16-25. [PMID: 18047844]
Accepted name: hydroxycinnamoyl-CoA reductase
Reaction: (1) dihydro-4-coumaroyl-CoA + NADP+ = trans-4-coumaroyl-CoA + NADPH + H+
(2) dihydroferuloyl-CoA + NADP+ = trans-feruloyl-CoA + NADPH + H+
For diagram of reaction click here.
Glossary: trans-4-coumaroyl-CoA = (E)-3-(4-hydroxyphenyl)prop-2-enoyl-CoA
trans-feruloyl-CoA = (E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoyl-CoA
dihydro-4-coumaroyl-CoA = 3-(4-hydroxyphenyl)propanoyl-CoA
dihydroferuloyl-CoA = 3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
Other name(s): MdHCDBR; hydroxycinnamoyl-CoA double bond reductase
Systematic name: dihydro-4-coumaroyl-CoA:NADP+ 2,3-oxidoreductase
Comments: Isolated from Malus X domestica (apple). Involved in dihydrochalcone biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ibdah, M., Berim, A., Martens, S., Valderrama, A.L.H., Palmieri, L., Lewinsohn, E. and Gang, D.R. Identification and cloning of an NADPH-dependant hydroxycinnamoyl-CoA double bond reductase involved in dihydrochalcone formation in Malus X domestica Borkh. Phytochemistry 107 (2014) 24-31. [PMID: 25152451]
Accepted name: meromycolic acid enoyl-[acyl-carrier-protein] reductase
Reaction: a meromycolyl-[acyl-carrier protein] + NAD+ = a trans-Δ2-meromycolyl-[acyl-carrier protein] + NADH + H+
Glossary: meromycolic acids are one of the two precursors of the mycolic acids produced by Mycobacteria. They consist of a long chain typically of 50-60 carbons, which is functionalized by different groups.
Other name(s): inhA (gene name)
Systematic name: meromycolyl-[acyl-carrier protein]:NAD+ oxidoreductase
Comments: InhA is a component of the fatty acid synthase (FAS) II system of Mycobacterium tuberculosis, catalysing an enoyl-[acyl-carrier-protein] reductase step. The enzyme acts on very long and unsaturated fatty acids that form the meromycolic component of mycolic acids. It extends FASI-derived C20 fatty acids to form C60 to C90 mycolic acids. The enzyme, which forms a homotetramer, is the target of the preferred antitubercular drug isoniazid.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Quemard, A., Sacchettini, J.C., Dessen, A., Vilcheze, C., Bittman, R., Jacobs, W.R., Jr. and Blanchard, J.S. Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis. Biochemistry 34 (1995) 8235-8241. [PMID: 7599116]
2. Rozwarski, D.A., Vilcheze, C., Sugantino, M., Bittman, R. and Sacchettini, J.C. Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate. J. Biol. Chem. 274 (1999) 15582-15589. [PMID: 10336454]
3. Marrakchi, H., Laneelle, G. and Quemard, A. InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II. Microbiology 146 (2000) 289-296. [PMID: 10708367]
4. Vilcheze, C., Morbidoni, H.R., Weisbrod, T.R., Iwamoto, H., Kuo, M., Sacchettini, J.C. and Jacobs, W.R., Jr. Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis. J. Bacteriol. 182 (2000) 4059-4067. [PMID: 10869086]
5. Gurvitz, A., Hiltunen, J.K. and Kastaniotis, A.J. Function of heterologous Mycobacterium tuberculosis InhA, a type 2 fatty acid synthase enzyme involved in extending C20 fatty acids to C60-to-C90 mycolic acids, during de novo lipoic acid synthesis in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 74 (2008) 5078-5085. [PMID: 18552191]
6. Chollet, A., Mourey, L., Lherbet, C., Delbot, A., Julien, S., Baltas, M., Bernadou, J., Pratviel, G., Maveyraud, L. and Bernardes-Genisson, V. Crystal structure of the enoyl-ACP reductase of Mycobacterium tuberculosis (InhA) in the apo-form and in complex with the active metabolite of isoniazid pre-formed by a biomimetic approach. J. Struct. Biol. 190 (2015) 328-337. [PMID: 25891098]
Accepted name: chlorobenzene dihydrodiol dehydrogenase
Reaction: (1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol + NAD+ = 3-chlorocatechol + NADH + H+
For diagram of reaction click here.
Other name(s): tecB (gene name)
Systematic name: (1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol:NAD+ oxidoreductase
Comments: This bacterial enzyme can transform various dihydrodiols of chlorobenzenes into the respective catechols, including the dihydrodiols of mono-, di-, tri-, and tetra-chlorinated benzenes. It also accepts the dihydrodiols of various chlorotoluenes. Substrates for the enzyme are generated by the broad spectrum EC 1.14.12.26, chlorobenzene dioxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Spiess, E. and Gorisch, H. Purification and characterization of chlorobenzene cis-dihydrodiol dehydrogenase from Xanthobacter flavus 14p1. Arch. Microbiol. 165 (1996) 201-205. [PMID: 8599538]
2. Pollmann, K., Beil, S. and Pieper, D.H. Transformation of chlorinated benzenes and toluenes by Ralstonia sp. strain PS12 tecA (tetrachlorobenzene dioxygenase) and tecB (chlorobenzene dihydrodiol dehydrogenase) gene products. Appl. Environ. Microbiol. 67 (2001) 4057-4063. [PMID: 11526005]
3. Pollmann, K., Wray, V. and Pieper, D.H. Chloromethylmuconolactones as critical metabolites in the degradation of chloromethylcatechols: recalcitrance of 2-chlorotoluene. J. Bacteriol. 187 (2005) 2332-2340. [PMID: 15774876]
Accepted name: cyclohexane-1-carbonyl-CoA reductase (NADP+)
Reaction: cyclohexane-1-carbonyl-CoA + NADP+ = cyclohex-1-ene-1-carbonyl-CoA + NADPH + H+
Other name(s): 1-cyclohexenylcarbonyl-CoA reductase (ambiguous); chcA (gene name)
Systematic name: cyclohexane-1-carbonyl-CoA:NADP+ 1-oxidoreductase
Comments: The enzyme, characterized from the bacterium Streptomyces collinus, is involved in a pathway that transforms shikimate to cyclohexane-1-carbonyl-CoA by a series of dehydration and double-bond reduction steps. Most of the steps in this process occur with the carboxylic acid activated as a coenzyme A thioester. The enzyme catalyses three steps in this pathway, also acting on (3R,4R)-3,4-dihydroxycyclohexa-1,5-diene-1-carbonyl-CoA and (5S)-5-hydroxycyclohex-1-ene-1-carbonyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Reynolds, K.A., Wang, P., Fox, K.M., Speedie, M.K., Lam, Y. and Floss, H.G. Purification and characterization of a novel enoyl coenzyme A reductase from Streptomyces collinus. J. Bacteriol. 174 (1992) 3850-3854. [PMID: 1597409]
2. Wang, P., Denoya, C.D., Morgenstern, M.R., Skinner, D.D., Wallace, K.K., Digate, R., Patton, S., Banavali, N., Schuler, G., Speedie, M.K. and Reynolds, K.A. Cloning and characterization of the gene encoding 1-cyclohexenylcarbonyl coenzyme A reductase from Streptomyces collinus. J. Bacteriol. 178 (1996) 6873-6881. [PMID: 8955309]
Accepted name: 4-amino-4-deoxyprephenate dehydrogenase
Reaction: 4-amino-4-deoxyprephenate + NAD+ = 3-(4-aminophenyl)pyruvate + CO2 + NADH + H+
Other name(s): cmlC (gene name); papC (gene name)
Systematic name: 4-amino-4-deoxyprephenate:NAD+ oxidoreductase (decarboxylating)
Comments: The enzyme, characterized from the bacteria Streptomyces venezuelae and Streptomyces pristinaespiralis, participates in the biosynthesis of the antibiotics chloramphenicol and pristinamycin IA, respectively. cf. EC 1.3.1.12, prephenate dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Blanc, V., Gil, P., Bamas-Jacques, N., Lorenzon, S., Zagorec, M., Schleuniger, J., Bisch, D., Blanche, F., Debussche, L., Crouzet, J. and Thibaut, D. Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4-dimethylamino-L-phenylalanine precursor of pristinamycin I. Mol. Microbiol. 23 (1997) 191-202. [PMID: 9044253]
2. He, J., Magarvey, N., Piraee, M. and Vining, L.C. The gene cluster for chloramphenicol biosynthesis in Streptomyces venezuelae ISP5230 includes novel shikimate pathway homologues and a monomodular non-ribosomal peptide synthetase gene. Microbiology 147 (2001) 2817-2829. [PMID: 11577160]
Accepted name: (S)-8-oxocitronellyl enol synthase
Reaction: (S)-8-oxocitronellyl enol + NAD(P)+ = (6E)-8-oxogeranial + NAD(P)H + H+
For diagram of reactionclick here
Glossary: (S)-8-oxocitronellyl enol = (2E,6S,7E)-8-hydroxy-2,6-dimethylocta-2,7-dienal
Other name(s): CrISY; 8-oxogeranial:NAD(P)+ oxidoreductase (cyclizing, cis,trans-nepetalactol forming); iridoid synthase (incorrect)
Systematic name: (S)-8-oxocitronellyl enol:NAD(P)+ oxidoreductase
Comments: Isolated from the plants Catharanthus roseus, Olea europaea (common olive), and several Nepeta species. The enzyme reduces 8-oxogeranial, generating an unstable product that is subsequently cyclized into several possible products, either non-enzymically or by dedicated cyclases. The products, known as iridoids, are involved in the biosynthesis of many indole alkaloids. cf. EC 1.3.1.123, 7-epi-iridoid synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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]
2. Hu, Y., Liu, W., Malwal, S.R., Zheng, Y., Feng, X., Ko, T.P., Chen, C.C., Xu, Z., Liu, M., Han, X., Gao, J., Oldfield, E. and Guo, R.T. Structures of iridoid synthase from Catharanthus roseus with bound NAD(+) , NADPH, or NAD(+) /10-oxogeranial: Reaction mechanisms. Angew. Chem. Int. Ed. Engl. 54 (2015) 15478-15482. [PMID: 26768532]
3. Alagna, F., Geu-Flores, F., Kries, H., Panara, F., Baldoni, L., O'Connor, S.E. and Osbourn, A. Identification and characterization of the iridoid synthase involved in oleuropein biosynthesis in olive (Olea europaea) fruits. J. Biol. Chem 291 (2016) 5542-5554. [PMID: 26709230]
4. Qin, L., Zhu, Y., Ding, Z., Zhang, X., Ye, S. and Zhang, R. Structure of iridoid synthase in complex with NADP(+)/8-oxogeranial reveals the structural basis of its substrate specificity. J. Struct. Biol. 194 (2016) 224-230. [PMID: 26868105]
5. Sherden, N.H., Lichman, B., Caputi, L., Zhao, D., Kamileen, M.O., Buell, C.R. and O'Connor, S.E. Identification of iridoid synthases from Nepeta species: Iridoid cyclization does not determine nepetalactone stereochemistry. Phytochemistry 145 (2018) 48-56. [PMID: 29091815]
6. Lichman, B.R., Kamileen, M.O., Titchiner, G.R., Saalbach, G., Stevenson, C.EM., Lawson, D.M. and O'Connor, S.E. Uncoupled activation and cyclization in catmint reductive terpenoid biosynthesis. Nat. Chem. Biol. 15 (2019) 71-79. [PMID: 30531909]
7. Lichman, B.R., O'Connor, S.E. and Kries, H. Biocatalytic strategies towards [4+2] cycloadditions. Chemistry 25 (2019) 6864-6877. [PMID: 30664302]
Accepted name: 7-epi-iridoid synthase
Reaction: (R)-8-oxocitronellyl enol + NADP+ = (6E)-8-oxogeranial + NADPH + H+
Glossary: (R)-8-oxocitronellyl enol = (2E,6R,7E)-8-hydroxy-2,6-dimethylocta-2,7-dienal
Other name(s): AmISY
Systematic name: (R)-8-oxocitronellyl enol:NADP+ oxidoreductase
Comments: The enzyme, characterized from the plant Antirrhinum majus (snapdragon), is involved in biosynthesis of 7-epi-iridoids such as antirrhinoside. The enzyme catalyses the stereospecific reduction of 8-oxogeranial, forming an unstable product that in the absence of additional cylases undergoes spontaneous cyclization to (–)-cis,trans-nepetalactol. cf. EC 1.3.1.122, (S)-8-oxocitronellyl enol synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Kries, H., Kellner, F., Kamileen, M.O. and O'Connor, S.E. Inverted stereocontrol of iridoid synthase in snapdragon. J. Biol. Chem 292 (2017) 14659-14667. [PMID: 28701463]
2. Lichman, B.R., O'Connor, S.E. and Kries, H. Biocatalytic strategies towards [4+2] cycloadditions. Chemistry 25 (2019) 6864-6877. [PMID: 30664302]
Accepted name: 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]
Reaction: (1) a (3E)-3-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+
(2) a (3E)-3-enoyl-CoA + NADP+ = a (2E,4Z)-2,4-dienoyl-CoA + NADPH + H+
Other name(s): SPS19 (gene name); DECR1 (gene name); DECR2 (gene name); Δ2,Δ4-dienoyl-CoA reductase (ambiguous)
Systematic name: (3E)-3-enoyl-CoA:NADP+ 4-oxidoreductase
Comments: This enzyme, characterized from eukaryotic organisms, catalyses the reduction of either (2E,4E)-2,4-dienoyl-CoA or (2E,4Z)-2,4-dienoyl-CoA to (3E)-3-enoyl-CoA. The best substrates for the enzyme from bovine liver have a chain-length of 8 or 10 carbons. Mammals possess both mitochondrial and peroxisomal variants of this enzyme. cf. EC 1.3.1.34, 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kunau, W.-H. and Dommes, P. Degradation of unsaturated fatty acids. Identification of intermediates in the degradation of cis-4-decenoly-CoA by extracts of beef-liver mitochondria. Eur. J. Biochem. 91 (1978) 533-544. [PMID: 729581]
2. Dommes, V., Luster, W., Cvetanovic, M. and Kunau, W.-H. Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli. Eur. J. Biochem. 125 (1982) 335-341. [PMID: 6749495]
3. Gurvitz, A., Rottensteiner, H., Kilpelainen, S.H., Hartig, A., Hiltunen, J.K., Binder, M., Dawes, I.W. and Hamilton, B. The Saccharomyces cerevisiae peroxisomal 2,4-dienoyl-CoA reductase is encoded by the oleate-inducible gene SPS19. J. Biol. Chem. 272 (1997) 22140-22147. [PMID: 9268358]
4. Geisbrecht, B.V., Liang, X., Morrell, J.C., Schulz, H. and Gould, S.J. The mouse gene PDCR encodes a peroxisomal δ2, δ4-dienoyl-CoA reductase. J. Biol. Chem. 274 (1999) 25814-25820. [PMID: 10464321]
5. De Nys, K., Meyhi, E., Mannaerts, G.P., Fransen, M. and Van Veldhoven, P.P. Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase. Biochim. Biophys. Acta 1533 (2001) 66-72. [PMID: 11514237]
6. Alphey, M.S., Yu, W., Byres, E., Li, D. and Hunter, W.N. Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase: enzyme-ligand interactions in a distinctive short-chain reductase active site. J. Biol. Chem. 280 (2005) 3068-3077. [PMID: 15531764]
Accepted name: acrylate reductase
Reaction: propanoate + NAD+ = acrylate + NADH + H+
Other name(s): ard (gene name); NADH:acrylate oxidoreductase
Systematic name: propanoate:NAD+ oxidoreductase
Comments: The enzyme, characterized from the marine bacterium Vibrio harveyi, enables the organism to utilize acrylate as the terminal electron acceptor for NADH regeneration under anaerobic conditions.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, Metacyc, CAS registry number:
References:
1. Bertsova, Y.V., Serebryakova, M.V., Baykov, A.A. and Bogachev, A.V. A novel, NADH-dependent acrylate reductase in Vibrio harveyi. Appl. Environ. Microbiol. 88 (2022) e0051922. [PMID: 35612301]
Accepted name: 2-epi-5-epi-valiolone dehydrogenase
Reaction: 2-epi-5-epi-valiolone + NAD+ = demethylgadusol + NADH + H+
Glossary: 2-epi-5-epi-valiolone = (2S,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexan-1-one
demethylgadusol = (4R,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one
Other name(s): gadusol synthase
Systematic name: 2-epi-5-epi-valiolone:NAD+ 2,3-oxidoreductase
Comments: The enzyme, present in egg-laying vertebrates, is involved in biosynthesis of the UV absorbing compound gadusol. It is a bifunctional enzyme that also catalyses EC 2.1.1.391, demethylgadusol O-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Osborn, A.R., Almabruk, K.H., Holzwarth, G., Asamizu, S., LaDu, J., Kean, K.M., Karplus, P.A., Tanguay, R.L., Bakalinsky, A.T. and Mahmud, T. De novo synthesis of a sunscreen compound in vertebrates. Elife 4 (2015) . [PMID: 25965179]
Deleted entry: vomilenine 19,20-reductase, now classified under EC 1.3.1.73, 1,2-dihydrovomilenine 19,20-reductase
Accepted name: precondylocarpine acetate reductase
Reaction: dehydrosecondine + acetate + NADP+ = precondylocarpine acetate + NADPH + H+ (overall reaction)
(1a) dihydroprecondylocarpine acetate + NADP+ = precondylocarpine acetate + NADPH + H+
(1b) dihydroprecondylocarpine acetate (enamine form) = dihydroprecondylocarpine acetate (spontaneous)
(1c) dehydrosecondine + acetate = dihydroprecondylocarpine acetate (enamine form) (spontaneous)
For diagram of reaction, click here and part mechanism click here
Other name(s): DPAS (gene name); dihydroprecondylocarpine acetate synthase
Systematic name: precondylocarpine acetate:NADP+ oxidoreductase
Comments: The enzyme, characterized from the plant Catharanthus roseus (Madagascar periwinkle), participates in a pathway that leads to the production of a number of monoterpene alkaloids, as well as the bisindole alkaloids vinblastine and vincristine, which are used as anticancer drugs. The enzyme forms the iminium ion form of dihydroprecondylocarpine acetate, which spontaneously rearranges and undergoes deacylation, producing dehydrosecodine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Caputi, L., Franke, J., Farrow, S.C., Chung, K., Payne, R.ME., Nguyen, T.D., Dang, T.T., Soares Teto Carqueijeiro, I., Koudounas, K., Duge de Bernonville, T., Ameyaw, B., Jones, D.M., Vieira, I.JC., Courdavault, V. and O'Connor, S.E. Missing enzymes in the biosynthesis of the anticancer drug vinblastine in Madagascar periwinkle. Science 360 (2018) 1235-1239. [PMID: 29724909]
2. Caputi, L., Franke, J., Bussey, K., Farrow, S.C., Vieira, I.JC., Stevenson, C.EM., Lawson, D.M. and O'Connor, S.E. Structural basis of cycloaddition in biosynthesis of iboga and aspidosperma alkaloids. Nat. Chem. Biol. 16 (2020) 383–386. [PMID: 32066966]
3. DeMars, M.D., 2nd and O'Connor, S.E. Evolution and diversification of carboxylesterase-like [4+2] cyclases in aspidosperma and iboga alkaloid biosynthesis. Proc. Natl. Acad. Sci. USA 121 (2024) e2318586121. [PMID: 38319969]