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, 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]
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 1.3.1.55 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, 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]
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]
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 1.3.1.59 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, 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 1.3.1.61 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, 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]
Accepted name: 2,4-dichlorobenzoyl-CoA reductase
Reaction: 4-chlorobenzoyl-CoA + NADP+ + chloride = 2,4-dichlorobenzoyl-CoA + NADPH + H+
Systematic name: 4-chlorobenzoyl-CoA:NADP+ oxidoreductase (halogenating)
Comments: Acts in the reverse direction to form part of the 2,4-dichlorobenzoate degradation pathway in bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:
References:
1. Romanov, V. and Hausinger, R.P. NADPH-dependent reductive ortho dehalogenation of 2,4-dichlorobenzoic acid in Corynebacterium sepedonicum KZ-4 and Coryneform bacterium strain NTB-1 via 2,4-dichlorobenzoyl coenzyme A. J. Bacteriol. 178 (1996) 2656-2661. [PMID: 8626335]
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]
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]
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]
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]
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]
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, 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 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 ]
Accepted name: 2-alkenal reductase
Reaction: n-alkanal + NAD(P)+ = alk-2-enal + NAD(P)H + H+
Other name(s): NAD(P)H-dependent alkenal/one oxidoreductase; NADPH:2-alkenal α,β-hydrogenase
Systematic name: n-alkanal:NAD(P)+ 2-oxidoreductase
Comments: Highly specific for 4-hydroxynon-2-enal and non-2-enal. 2-Alkenals of shorter chain have lower affinities. Exhibits high activities also for 2-alkenones 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.
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: divinyl chlorophyllide a 8-vinyl-reductase
Reaction: chlorophyllide a + NADP+ = divinyl chlorophyllide a + NADPH + H+
For diagram click here.
Other name(s): [4-vinyl]chlorophyllide a reductase; 4VCR
Systematic name: chlorophyllide-a:NADP+ oxidoreductase
Comments: Also reduces divinyl protochlorophyllide to protochlorophyllide in some species, providing an alternative pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
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.
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]
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
Reaction: a flavan-3-ol + 2 NAD(P)+ = an anthocyanidin + 2 NAD(P)H + H+
For diagram click here.
Other name(s): AtANR; MtANR
Systematic name: flavan-3-ol:NAD(P)+ oxidoreductase
Comments: Forms 2,3-cis-flavan-3-ols. The isomeric 2,3-trans-flavan-3-ols are formed from flavan-3,4-diols by EC 1.17.1.3 leucoanthocyanidin reductase. While the enzyme from the legume Medicago truncatula (MtANR) uses 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.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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]
Accepted name: arogenate dehydrogenase (NADP+)
Reaction: L-arogenate + NADP+ = L-tyrosine + NADPH + CO2
For diagram click here.
Other name(s): arogenic dehydrogenase (ambiguous); pretyrosine dehydrogenase (ambiguous); TyrAAT1; TyrAAT2; TyrAa
Systematic name: L-arogenate:NADP+ oxidoreductase (decarboxylating)
Comments: Unlike EC 1.3.1.43 (arogenate dehydrogenase) and EC 1.3.1.79 [arogenate dehydrogenase (NAD(P)+)], this enzyme has a strict requirement for NADP+. The enzyme from Synechocystis sp. PCC 6803 and the isoform TyrAAT1 cannot use prephenate as a substrate, while the isoform TyrAAT2 can use it only very poorly [3,4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 64295-75-6
References:
1. Byng, G., Whitaker, R., Flick, C. and Jensen, R.A. Enzymology of L-tyrosine biosynthesis in corn (Zea mays). Phytochemistry 20 (1981) 1289-1292.
2. 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.
3. 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]
4. 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.
Other name(s): arogenic dehydrogenase (ambiguous); cyclohexadienyl dehydrogenase; pretyrosine dehydrogenase (ambiguous)
Systematic name: L-arogenate:NAD(P)+ oxidoreductase (decarboxylating)
Comments: See also EC 1.3.1.12 (prephenate dehydrogenase), EC 1.3.1.43 (arogenate dehydrogenase), and EC 1.3.1.78 [arogenate dehydrogenase (NADP+)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 64295-75-6
References:
1. Connelly, J.A. and Conn, E.E. Tyrosine biosynthesis in Sorghum bicolor: isolation and regulatory properties of arogenate dehydrogenase. Z. Naturforsch. [C] 41 (1986) 69-78. [PMID: 2939643]
2. Bonner, C. and Jensen, R. Arogenate dehydrogenase. Methods Enzymol. 142 (1987) 488-494. [PMID: 3600376]
Accepted name: red chlorophyll catabolite reductase
Reaction: primary fluorescent chlorophyll catabolite + NADP+ = red chlorophyll catabolite + NADPH + H+
For diagram click here
Glossary: red chlorophyll catabolite = RCC = (7S,8S,101R)-8-(2-carboxyethyl)-17-ethyl-19-formyl-101-(methoxycarbonyl)-3,7,13,18-tetramethyl-2-vinyl-8,23-dihydro-7H-10,12-ethanobiladiene-ab-1,102(21H)-dione
primary fluorescent chlorophyll catabolite = pFCC = (82R,12S,13S)-12-(2-carboxyethyl)-3-ethyl-1-formyl-82-(methoxycarbonyl)-2,7,13,17-tetramethyl-18-vinyl-12,13-dihydro-8,10-ethanobilene-b-81,19(16H)-dione
Other name(s): RCCR; RCC reductase; red Chl catabolite reductase
Systematic name: primary fluorescent chlorophyll catabolite:NADP+ oxidoreductase
Comments: Chlorophyll degradation is a characteristic symptom of leaf senescence and fruit ripening. The reaction catalysed by this enzyme requires reduced ferredoxin, which is generated either by NADPH through the pentose-phosphate pathway or by the action of photosystem I [1,2]. This reaction takes place without release of the substrate from EC 1.14.12.20, pheophorbide a oxygenase [3]. Depending on the plant species used as the source of enzyme, one of two possible C-1 epimers of primary fluorescent chlorophyll catabolite (pFCC), pFCC-1 or pFCC-2, is normally formed, with all genera or species within a family producing the same isomer [3,4]. After modification and export, pFCCs are eventually imported into the vacuole, where the acidic environment causes their non-enzymic conversion into colourless breakdown products called non-fluorescent chlorophyll catabolites (NCCs) [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Rodoni, S., Mühlecker, W., Anderl, M., Kräutler, B., Moser, D., Thomas, H., Matile, P. and Hörtensteiner, S. Chlorophyll breakdown in senescent chloroplasts. Cleavage of pheophorbide a in two enzymic steps. Plant Physiol. 115 (1997) 669-676. [PMID: 12223835]
2. Wüthrich, K.L., Bovet, L., Hunziker, P.E., Donnison, I.S. and Hörtensteiner, S. Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism. Plant J. 21 (2000) 189-198. [PMID: 10743659]
3. Pružinská, A., Anders, I., Aubry, S., Schenk, N., Tapernoux-Lüthi, E., Müller, T., Kräutler, B. and Hörtensteiner, S. In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown. Plant Cell 19 (2007) 369-387. [PMID: 17237353]
4. Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55-77. [PMID: 16669755]
5. Rodoni, S., Vicentini, F., Schellenberg, M., Matile, P. and Hörtensteiner, S. Partial purification and characterization of red chlorophyll catabolite reductase, a stroma protein involved in chlorophyll breakdown. Plant Physiol. 115 (1997) 677-682. [PMID: 12223836]
Note: For reference 1 an accent may not be seen. ž is z-hacek
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]
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]
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]
Accepted name: acrylyl-CoA reductase (NADPH)
Reaction: propanoyl-CoA + NADP+ = acryloyl-CoA + NADPH + H+
Glossary: acrylyl-CoA = acryloyl-CoA
propanoyl-CoA = propionyl-CoA
Systematic name: propanoyl-CoA:NADP+ oxidoreductase
Comments: Catalyses a step in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [1]. The reaction is catalysed in the opposite direction to that shown. 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]
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+
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, 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]
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, 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, 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-[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]
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]
Accepted name: acrylyl-CoA reductase (NADH)
Reaction: propanoyl-CoA + NAD+ = acrylyl-CoA + NADH + H+
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:
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]
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]