An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
Common name: hydroxymethylglutaryl-CoA reductase
Reaction: (R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
For diagram click here.
Other name(s): β-hydroxy-β-methylglutaryl coenzyme A reductase; β-hydroxy-β-methylglutaryl CoA-reductase; 3-hydroxy-3-methylglutaryl coenzyme A reductase; hydroxymethylglutaryl coenzyme A reductase
Systematic name: (R)-mevalonate:NAD+ oxidoreductase (CoA-acylating)
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37250-24-1
References:
1. Fimognari, G.M. and Rodwell, V.W. Substrate-competitive inhibition of bacterial mevalonate:nicotinamide-adenine dinucleotide oxidoreductase (acylating CoA). Biochemistry 4 (1965) 2086-2090.
Common name: sterol-4α-carboxylate 3-dehydrogenase (decarboxylating)
Reaction: 3β-hydroxy-4β-methyl-5α-cholest-7-ene-4α-carboxylate + NAD(P)+ = 4α-methyl-5α-cholest-7-en-3-one + CO2 + NAD(P)H + H+
For diagram click here.
Other name(s): 3β-hydroxy-4β-methylcholestenecarboxylate 3-dehydrogenase (decarboxylating); 3β-hydroxy-4β-methylcholestenoate dehydrogenase; 3β-hydroxy-4β-methylcholestenoate dehydrogenase; sterol 4α-carboxylic decarboxylase
Systematic name: 3β-hydroxy-4β-methyl-5α-cholest-7-ene-4α-carboxylate:NAD(P)+ 3-oxidoreductase (decarboxylating)
Comments: Also acts on 3β-hydroxy-5α-cholest-7-ene-4α-carboxylate.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 71822-23-6
References:
1. Brady, D.R., Crowder, R.D. and Hayes, W.J. Mixed function oxidases in sterol metabolism. Source of reducing equivalents. J. Biol. Chem. 255 (1980) 10624-10629. [PMID: 7430141]
2. Rahimtula, A.D. and Gaylor, J.L. Partial purification of a microsomal sterol 4α-carboxylic acid decarboxylase. J. Biol. Chem. 247 (1972) 9-15. [PMID: 4401584]
Common name: 3-keto-steroid reductase
Reaction: 4α-methyl-5α-cholest-7-en-3β-ol + NADP+ = 4α-methyl-5α-cholest-7-en-3-one + NADPH + H+
For diagram click here.
Other name(s): 3-KSR
Systematic name: 3β-hydroxy-steroid:NADP+ 3-oxidoreductase
Comments: Also acts on 5α-cholest-7-en-3-one.
References:
1. Billheimer, J.T., Alcorn, M. and Gaylor, J.L. Solubilization and partial purification of a microsomal 3-ketosteroid reductase of cholesterol biosynthesis. Purification and properties of 3-β-hydroxysteroid dehydrogenase and δ5-3-ketosteroid isomerase from bovine corpora lutea. Arch. Biochem. Biophys. 211 (1981) 430-438. [PMID: 6946726]
2. Swindell, A.C. and Gaylor, J.L. Investigation of the component reactions of oxidative sterol demethylation. Formation and metabolism of 3-ketosteroid intermediates. J. Biol. Chem. 243 (1968) 5546-5555. [PMID: 4387005]
Common name: aldehyde oxidase
Reaction: an aldehyde + H2O + O2 = a carboxylic acid + H2O2
Other name(s): quinoline oxidase
Systematic name: aldehyde:oxygen oxidoreductase
Comments: A molybdenum flavohemoprotein. Also oxidizes quinoline and pyridine derivatives. May be identical with EC 1.2.3.11, retinal oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9029-07-06
References:
1. Gordon, A.H., Green, D.E. and Subrahmanyan, V. Liver aldehyde oxidase. Biochem. J. 34 (1940) 764-774.
2. Knox, W.E. The quinine-oxidizing enzyme and liver aldehyde oxidase. J. Biol. Chem. 163 (1946) 699-711.
3. Mahler, H.R., Mackler, B., Green, D.E. and Bock, R.M. Studies on metalloflavoproteins. III. Aldehyde oxidase: a molybdoflavoprotein. J. Biol. Chem. 210 (1954) 465-480.
4. Huang D.-Y., Furukawa, A. and Ichikawa, Y. Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli. Arch. Biochem. Biophys. 364 (1999) 264-272. [PMID: 10190983]
Common name: aryl-aldehyde oxidase
Reaction: an aromatic aldehyde + O2 + H2O = an aromatic carboxylic acid + H2O2
Systematic name: aryl-aldehyde:oxygen oxidoreductase
Comments: Acts on benzaldehyde, vanillin and a number of other aromatic aldehydes, but not on aliphatic aldehydes or sugars.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, WIT, CAS registry number: 82657-93-0
References:
1. Crawford, D.L., Sutherland, J.B., Pometto, A.L., III and Miller, J.M. Production of an aromatic aldehyde oxidase by Streptomyces viridosporus. Arch. Microbiol. 131 (1982) 351-355.
Common name: retinal oxidase
Reaction: retinal + O2 + H2O = retinoate + H2O2
Other name(s): retinene oxidase
Systematic name: retinal:oxygen oxidoreductase
Comments: May be the same as EC 1.2.3.1, aldehyde oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9033-52-7
References:
1. Mandal, S.K. and Chaudhuri, B.D. Enzymic oxidation of vitamin A aldehyde to vitamin A acid by rat livers of experimental thyroid disorders. Indian J. Exp. Biol. 25 (1987) 796-797. [PMID: 3452601]
2. Huang D.-Y., Furukawa, A. and Ichikawa, Y. Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli. Arch. Biochem. Biophys. 364 (1999) 264-272. [PMID: 10190983]
Common name: FMN reductase
Reaction: FMNH2 + NAD(P)+ = FMN + NAD(P)H + H+
Other name(s): NAD(P)H:flavin oxidoreductase; riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide (phosphate)) reductase; flavin mononucleotide reductase; flavine mononucleotide reductase; NAD(P)H-FMN reductase; NAD(P)H:FMN oxidoreductase; riboflavin mononucleotide reductase; riboflavine mononucleotide reductase; NAD(P)H2 dehydrogenase (FMN); NAD(P)H2:FMN oxidoreductase
Systematic name: FMNH2:NAD(P)+ oxidoreductase
Comments: The enzyme from luminescent bacteria also reduces riboflavin and FAD, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 64295-83-6
References:
1. Duane, W. and Hastings, J.W. Flavin mononucleotide reductase of luminous bacteria. Mol. Cell. Biochem. 6 (1975) 53-64. [PMID: 47604]
2. Fisher, J., Spencer, R. and Walsh, C. Enzyme-catalyzed redox reactions with the flavin analogues 5-deazariboflavin, 5-deazariboflavin 5'-phosphate, and 5-deazariboflavin 5'-diphosphate, 5' leads to 5'-adenosine ester. Biochemistry 15 (1976) 1054-1064. [PMID: 3207]
3. Tu, S.-C., Becvar, J.E. and Hastings, J.W. Kinetic studies on the mechanism of bacterial NAD(P)H:flavin oxidoreductase. Arch. Biochem. Biophys. 193 (1979) 110-116. [PMID: 222213]
4. Liu, M., Lei, B., Ding, Q., Lee, J.C. and Tu, S.C. Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium. Arch. Biochem. Biophys. 337 (1997) 89-95. [PMID: 8990272]
5. Lei, B. and Tu, S.C. Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase. Biochemistry 37 (1998) 14623-14629. [PMID: 9772191]
6. Tang, C.K., Jeffers, C.E., Nichols, J.C. and Tu, S.C. Flavin specificity and subunit interaction of Vibrio fischeri general NAD(P)H-flavin oxidoreductase FRG/FRase I. Arch. Biochem. Biophys. 392 (2001) 110-116. [PMID: 11469801]
7. Ingelman, M., Ramaswamy, S., Nivière, V., Fontecave, M. and Eklund, H. Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli. Biochemistry 38 (1999) 7040-7049. [PMID: 10353815]
Common name: flavin reductase
Reaction: reduced riboflavin + NADP+ = riboflavin + NADPH + H+
Other name(s): NADPH:flavin oxidoreductase; riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide phosphate) reductase; flavin mononucleotide reductase; flavine mononucleotide reductase; FMN reductase (NADPH); NADPH-dependent FMN reductase; NADPH-flavin reductase; NADPH-FMN reductase; NADPH-specific FMN reductase; riboflavin mononucleotide reductase; riboflavine mononucleotide reductase; NADPH2 dehydrogenase (flavin); NADPH2:riboflavin oxidoreductase
Systematic name: reduced-riboflavin:NADP+ oxidoreductase
Comments: The enzyme from Entamoeba histolytica reduces riboflavin and galactoflavin, and, more slowly, FMN and FAD. NADH is oxidized more slowly than NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 56626-29-0
References:
1. Lo, H.-S. and Reeves, R.E. Purification and properties of NADPH:flavin oxidoreductase from Entamoeba histolytica. Mol. Biochem. Parasitol. 2 (1980) 23-30. [PMID: 6258069]
1. Yubisui, T., Tamura, M. and Takeshita, M. Characterization of a second form of NADPH-flavin reductase purified from human erythrocytes. Biochem. Int. 15 (1987) 1-8. [PMID: 3453680]
[EC 1.6.4.1 Transferred entry: now EC 1.8.1.6, cystine reductase (EC 1.6.4.1 created 1961, deleted 2002)]
[EC 1.6.4.2 Transferred entry: now EC 1.8.1.7, glutathione-disulfide reductase (EC 1.6.4.2 created 1961, modified 1989, deleted 2002)]
[EC 1.6.4.4 Transferred entry: now EC 1.8.1.8, protein-disulfide reductase (EC 1.6.4.4 created 1965, deleted 2002)]
[EC 1.6.4.5 Transferred entry: now EC 1.8.1.9, thioredoxin-disulfide reductase (EC 1.6.4.5 created 1972, deleted 2002)]
[EC 1.6.4.6 Transferred entry: now EC 1.8.1.10, CoA-glutathione reductase (EC 1.6.4.6 created 1972, deleted 2002)]
[EC 1.6.4.7 Transferred entry: now EC 1.8.1.11, asparagusate reductase (EC 1.6.4.7 created 1978, deleted 2002)]
[EC 1.6.4.8 Transferred entry: now EC 1.8.1.12, trypanothione-disulfide reductase (EC 1.6.4.8 created 1989, deleted 2002)]
[EC 1.6.4.9 Transferred entry: now EC 1.8.1.13, bis-γ-glutamylcystine reductase (EC 1.6.4.9 created 1992, deleted 2002)]
[EC 1.6.4.10 Transferred entry: now EC 1.8.1.14, CoA-disulfide reductase (EC 1.6.4.10 created 1992, deleted 2002)]
[EC 1.6.6.1 Transferred entry: now EC 1.7.1.1, nitrate reductase (NADH) (EC 1.6.6.1 created 1961, deleted 2002)]
[EC 1.6.6.2 Transferred entry: now EC 1.7.1.2, nitrate reductase [NAD(P)H] (EC 1.6.6.2 created 1961, deleted 2002)]
[EC 1.6.6.3 Transferred entry: now EC 1.7.1.3, nitrate reductase (NADPH) (EC 1.6.6.3 created 1961, deleted 2002)]
[EC 1.6.6.4 Transferred entry: now EC 1.7.1.4, nitrite reductase [NAD(P)H] (EC 1.6.6.4 created 1961, deleted 2002)]
[EC 1.6.6.6 Transferred entry: now EC 1.7.1.5, hyponitrite reductase (EC 1.6.6.6 created 1961, deleted 2002)]
[EC 1.6.6.7 Transferred entry: now EC 1.7.1.6, azobenzene reductase (EC 1.6.6.7 created 1961, deleted 2002)]
[EC 1.6.6.8 Transferred entry: now EC 1.7.1.7, GMP reductase (EC 1.6.6.8 created 1965, deleted 2002)]
[EC 1.6.6.10 Transferred entry: now EC 1.7.1.9, nitroquinoline-N-oxide reductase (EC 1.6.6.10 created 1972, deleted 2002)]
[EC 1.6.6.11 Transferred entry: now EC 1.7.1.10, hydroxylamine reductase (NADH) (EC 1.6.6.11 created 1972, deleted 2002)]
[EC 1.6.6.12 Transferred entry: now EC 1.7.1.11, 4-(dimethylamino)phenylazoxybenzene reductase (EC 1.6.6.12 created 1989, deleted 2002)]
[EC 1.6.6.13 Transferred entry: now EC 1.7.1.12, N-hydroxy-2-acetamidofluorene reductase (EC 1.6.6.13 created 1989, deleted 2002)]
[EC 1.6.8.1 Transferred entry: now EC 1.5.1.29, FMN reductase (EC 1.6.8.1 created 1981, deleted 2002)]
[EC 1.6.8.2 Transferred entry: now EC 1.5.1.30, flavin reductase (EC 1.6.8.2 created 1982, deleted 2002)]
[EC 1.6.99.8 Transferred entry: now EC 1.16.1.3, aquacobalamin reductase (EC 1.6.99.8 created 1972, deleted 2002)]
[EC 1.6.99.9 Transferred entry: now EC 1.16.1.4, cob(II)alamin reductase (EC 1.6.99.9 created 1972, deleted 2002)]
[EC 1.6.99.11 Transferred entry: now EC 1.16.1.5, aquacobalamin reductase (NADPH) (EC 1.6.99.11 created 1989, deleted 2002)]
[EC 1.6.99.12 Transferred entry: now EC 1.16.1.6, cyanocobalamin reductase (cyanide-eliminating) (EC 1.6.99.12 created 1989, deleted 2002)]
[EC 1.6.99.13 Transferred entry: now EC 1.16.1.7, ferric-chelate reductase (EC 1.6.99.13 created 1992, deleted 2002)]
EC 1.7.1 With a NAD or NADP as acceptor
Common name: nitrate reductase (NADH)
Reaction: nitrite + NAD+ + H2O = nitrate + NADH + H+
Other name(s): assimilatory nitrate reductase; NADH-nitrate reductase; NADH-dependent nitrate reductase; assimilatory NADH: nitrate reductase; nitrate reductase (NADH2); NADH2:nitrate oxidoreductase
Systematic name: nitrite:NAD+ oxidoreductase
Comments: An iron-sulfur molybdenum flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9013-03-0
References:
1. Fewson, C.A. and Nicholas, D.J.D. Nitrate reductase from Pseudomonas aeruginosa. Biochim. Biophys. Acta 49 (1961) 335-349.
2. Nason, A. Nitrate reductases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, pp. 587-607.
3. Nicholas, D.J.D. and Nason, A. Diphosphopyridine nucleotide-nitrate reductase from Escherichia coli. J. Bacteriol. 69 (1955) 580-583.
4. Spencer, D. A reduced diphosphopyridine-specific nitrate reductase from germinating wheat. Aust. J. Biol. Sci. 12 (1959) 181-189.
5. Berks, B.C., Ferguson, S.J., Moir, J.W. and Richardson, D.J. Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions. Biochim. Biophys. Acta 1232 (1995) 97-173. [PMID: 8534676]
Common name: nitrate reductase [NAD(P)H]
Reaction: nitrite + NAD(P)+ + H2O = nitrate + NAD(P)H + H+
Other name(s): assimilatory nitrate reductase; assimilatory NAD(P)H-nitrate reductase; NAD(P)H bispecific nitrate reductase; nitrate reductase (reduced nicotinamide adenine dinucleotide (phosphate)); nitrate reductase NAD(P)H; NAD(P)H-nitrate reductase; nitrate reductase [NAD(P)H2]; NAD(P)H2:nitrate oxidoreductase
Systematic name: nitrite:NAD(P)+ oxidoreductase
Comments: An iron-sulfur molybdenum flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9029-27-0
References:
1. Nason, A. Nitrate reductases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, pp. 587-607.
2. Paneque, A., Del Campo, F.F., Ramirez, J.M. and Losada, M. Flavin nucleotide nitrate reductase from spinach. Biochim. Biophys. Acta 109 (1965) 79-85. [PMID: 5864033]
3. Campbell, W.H. Structure and function of eukaryotic NAD(P)H:nitrate reductase. Cell. Mol. Life Sci. 58 (2001) 194-204. [PMID: 11289301]
4. Berks, B.C., Ferguson, S.J., Moir, J.W. and Richardson, D.J. Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions. Biochim. Biophys. Acta 1232 (1995) 97-173. [PMID: 8534676]
Common name: nitrate reductase (NADPH)
Reaction: nitrite + NADP+ + H2O = nitrate + NADPH + H+
Other name(s): assimilatory nitrate reductase; assimilatory reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase; NADPH-nitrate reductase; assimilatory NADPH-nitrate reductase; triphosphopyridine nucleotide-nitrate reductase; NADPH:nitrate reductase; nitrate reductase (NADPH2); NADPH2:nitrate oxidoreductase
Systematic name: nitrite:NADP+ oxidoreductase
Comments: An iron-sulfur molybdenum flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9029-28-1
References:
1. Nason, A. Nitrate reductases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, pp. 587-607.
2. Nason, A. and Evans, H.J. Triphosphopyridine nucleotide-nitrate reductase in Neurospora. J. Biol. Chem. 202 (1953) 655-673.
3. Nicholas, D.J.D. and Nason, A. Molybdenum and nitrate reductase. II. Molybdenum as a constituent of nitrate reductase. J. Biol. Chem. 207 (1954) 353-360.
4. Taniguchi, H., Mitsui, H., Nakamura, K. and Egami, F. Ann. Acad. Sci. Fenn. Ser. A II 60 (1955) 200.
5. Berks, B.C., Ferguson, S.J., Moir, J.W. and Richardson, D.J. Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions. Biochim. Biophys. Acta 1232 (1995) 97-173. [PMID: 8534676]
Common name: nitrite reductase [NAD(P)H]
Reaction: ammonium hydroxide + 3 NAD(P)+ + H2O = nitrite + 3 NAD(P)H + 3 H+
Other name(s): nitrite reductase (reduced nicotinamide adenine dinucleotide (phosphate)); NADH-nitrite oxidoreductase; NADPH-nitrite reductase; assimilatory nitrite reductase; nitrite reductase [NAD(P)H2]; NAD(P)H2:nitrite oxidoreductase
Systematic name: ammonium-hydroxide:NAD(P)+ oxidoreductase
Comments: An iron-sulfur heme flavoprotein containing siroheme.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9029-29-2
References:
1. Cammack, R., Jackson, R.H., Cornish-Bowden, A. and Cole, J.A. Electron-spin-resonance studies of the NADH-dependent nitrite reductase from Escherichia coli K12. Biochem. J. 207 (1982) 333-339. [PMID: 6297458]
2. Lazzarini, R.A. and Atkinson, D.E. A triphosphopyridine nucleotide-specific nitrite reductase from Escherichia coli. J. Biol. Chem. 236 (1961) 3330-3335.
3. Nicholas, D.J.D., Medina, A. and Jones, O.T.G. A nitrite reductase from Neurospora crassa. Biochim. Biophys. Acta 37 (1960) 468.
4. Taniguchi, H., Mitsui, H., Nakamura, K. and Egami, F. Ann. Acad. Sci. Fenn. Ser. A II 60 (1955) 200.
5. Colandene, J.D. and Garrett, R.H. Functional dissection and site-directed mutagenesis of the structural gene for NAD(P)H-nitrite reductase in Neurospora crassa. J. Biol. Chem. 271 (1996) 24096-24104. [PMID: 8798648]
Common name: hyponitrite reductase
Reaction: 2 hydroxylamine + 2 NAD+ = hyponitrous acid + 2 NADH + 2 H+
Glossary: hypnitrous acid = HO-N=N-OH
Other name(s): NADH2:hyponitrite oxidoreductase
Systematic name: hydroxylamine:NAD+ oxidoreductase
Comments: A metalloprotein.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9029-30-5
References:
1. Medina, A. and Nicholas, D.J.D. Hyponitrite reductase in Neurospora. Nature (Lond.) 179 (1957) 533-534.
Common name: azobenzene reductase
Reaction: N,N-dimethyl-1,4-phenylenediamine + aniline + NADP+ = 4-(dimethylamino)azobenzene + NADPH + H+
Other name(s): new coccine (NC)-reductase; NC-reductase; azo-dye reductase; orange II azoreductase; NAD(P)H:1-(4'-sulfophenylazo)-2-naphthol oxidoreductase; orange I azoreductase; azo reductase; azoreductase; nicotinamide adenine dinucleotide (phosphate) azoreductase; NADPH2-dependent azoreductase; dimethylaminobenzene reductase; p-dimethylaminoazobenzene azoreductase; dibromopropylaminophenylazobenzoic azoreductase; N,N-dimethyl-4-phenylazoaniline azoreductase; p-aminoazobenzene reductase; methyl red azoreductase; NADPH2:4-(dimethylamino)azobenzene oxidoreductase
Systematic name: N,N-dimethyl-1,4-phenylenediamine, aniline:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9029-31-6
References:
1. Mueller, G.C. and Miller, J.A. The reductive cleavage of 4-dimethylaminoazobenzene by rat liver: the intracellular distribution of the enzyme system and its requirements for triphosphopyridine nucleotide. J. Biol. Chem. 180 (1949) 1125-1136.
2. Suzuki, Y., Yoda, T., Ruhul, A. and Sugiura, W. Molecular cloning and characterization of the gene coding for azoreductase from Bacillus sp. OY1-2 isolated from soil. J. Biol. Chem. 276 (2001) 9059-9065. [PMID: 11134015]
Common name: GMP reductase
Reaction: inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH + H+
Other name(s): guanosine 5'-monophosphate reductase; NADPH:GMP oxidoreductase (deaminating); guanosine monophosphate reductase; guanylate reductase; NADPH2:guanosine-5'-phosphate oxidoreductase (deaminating); guanosine 5'-phosphate reductase
Systematic name: inosine-5'-phosphate:NADP+ oxidoreductase (aminating)
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9029-32-7
References:
1. MacKenzie, J.J. and Sorensen, L.B. Guanosine 5'-phosphate reductase of human erythrocytes. Biochim. Biophys. Acta 327 (1973) 282-294. [PMID: 4149840]
2. Mager, J. and Magasanik, B. Guanosine 5'-phosphate reductase and its role in the interconversion of purine nucleotides. J. Biol. Chem. 235 (1960) 1474-1478.
[EC 1.7.1.8 Deleted entry: withdrawn in the light of further information on the acceptor (EC 1.7.1.8 created 2002, deleted 2002)]
Common name: nitroquinoline-N-oxide reductase
Reaction: 4-(hydroxyamino)quinoline N-oxide + 2 NAD(P)+ + H2O = 4-nitroquinoline N-oxide + 2 NAD(P)H + 2 H+
Other name(s): 4-nitroquinoline 1-oxide reductase; 4NQO reductase; NAD(P)H2:4-nitroquinoline-N-oxide oxidoreductase
Systematic name: 4-(hydroxyamino)quinoline N-oxide:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37256-35-2
References:
1. Toriyama, N. [Metabolism of quinoline derivatives. On the reducing enzyme of 4-nitroquinoline-N-oxide] Nichidai Igaku Zasshi 24 (1965) 423-432. (in Japanese)
2. Stanley, J.S., York, J.L. and Benson AM. Nitroreductases and glutathione transferases that act on 4-nitroquinoline 1-oxide and their differential induction by butylated hydroxyanisole in mice. Cancer Res. 52 (1992) 58-63. [PMID: 1370076]
Common name: hydroxylamine reductase (NADH)
Reaction: NH3 + NAD+ + H2O = hydroxylamine + NADH + H+
Other name(s): hydroxylamine reductase; ammonium dehydrogenase; NADH-hydroxylamine reductase; N-hydroxy amine reductase; hydroxylamine reductase (NADH2); NADH2:hydroxylamine oxidoreductase
Systematic name: ammonium:NAD+ oxidoreductase
Comments: Also acts on some hydroxamates.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9032-06-8
References:
1. Bernheim, M.L.C. The hydroxylamine reductase of mitochondria. Arch. Biochem. Biophys. 134 (1969) 408-413. [PMID: 4311180]
2. Bernheim, M.L.C. and Hochstein, P. Reduction of hydroxylamine by rat liver mitochondria. Arch. Biochem. Biophys. 124 (1968) 436-442. [PMID: 4298499]
3. Wang, R. and Nicholas, D.J.D. Some properties of nitrite and hydroxylamine reductases from Derxia gummosa. Phytochemistry 25 (1986) 2463-2469.
Common name: 4-(dimethylamino)phenylazoxybenzene reductase
Reaction: 4-(dimethylamino)phenylazobenzene + NADP+ = 4-(dimethylamino)phenylazoxybenzene + NADPH + H+
Other name(s): N,N-dimethyl-p-aminoazobenzene oxide reductase; dimethylaminoazobenzene N-oxide reductase; NADPH-dependent DMAB N-oxide reductase; NADPH2:4-(dimethylamino)phenylazoxybenzene oxidoreductase
Systematic name: 4-(dimethylamino)phenylazobenzene:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 103843-39-6
References:
1. Lashmet Johnson, P.R. and Ziegler, D.M. Properties of an N,N-dimethyl-p-aminoazobenzene oxide reductase purified from rat liver cytosol. J. Biochem. Toxicol. 1 (1986) 15-27. [PMID: 3152268]
Common name: N-hydroxy-2-acetamidofluorene reductase
Reaction: 2-acetamidofluorene + NAD(P)+ + H2O = N-hydroxy-2-acetamidofluorene + NAD(P)H + H+
Other name(s): N-hydroxy-2-acetylaminofluorene reductase; NAD(P)H2:N-hydroxy-2-acetamidofluorene N-oxidoreductase
Systematic name: 2-acetamidofluorene:NAD(P)+ oxidoreductase
Comments: Also acts, more slowly, on N-hydroxy-4-acetamidobiphenyl.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 99890-08-1
References:
1. Gutmann, H.R. and Erickson, R.R. The conversion of the carcinogen N-hydroxy-2-fluorenylacetamide to o-amidophenols by rat liver in vitro. An inducible enzymatic reaction. J. Biol. Chem. 244 (1969) 1729-1740. [PMID: 5780838]
2. Kitamura, S. and Tatsumi, K. Purification of N-hydroxy-2-acetylaminofluorene reductase from rabbit liver cytosol. Biochem. Biophys. Res. Commun. 133 (1985) 67-74. [PMID: 4074379]
Common name: cystine reductase
Reaction: 2 L-cysteine + NAD+ = L-cystine + NADH + H+
Other name(s): cystine reductase (NADH); NADH-dependent cystine reductase; cystine reductase (NADH2); NADH2:L-cystine oxidoreductase
Systematic name: L-cysteine:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9029-18-9
References:
1. Romano, A.H. and Nickerson, W.J. Cystine reductase of pea seeds and yeast. J. Biol. Chem. 208 (1954) 409-416.
2. Carroll, J.E., Kosicki, G.W. and Thibert, R.J. α-Substituted cystines as possible substrates for cystine reductase and L-amino acid oxidase. Biochim. Biophys. Acta 198 (1970) 601-603. [PMID: 5436160]
3. Maresca, B., Jacobson, E., Medoff, G. and Kobayashi, G. Cystine reductase in the dimorphic fungus Histoplasma capsulatum. J. Bacteriol. 135 (1978) 987-992. [PMID: 211119]
Common name: glutathione-disulfide reductase
Reaction: 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
Glossary:
The term 'oxidized glutathione' has been replaced by the term 'glutathione disulfide' as the former is ambiguous. S,S'-Biglutathione may also be used to refer to this compound.
Other name(s): glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase
Systematic name: glutathione:NADP+ oxidoreductase
Comments: A dimeric flavoprotein (FAD); activity is dependent on a redox-active disulfide in each of the active centres.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, WIT, CAS registry number: 9001-48-3
References:
1. Pai, E.F., Schirmer, R.H. and Schulz, G.E. Structural studies on crystalline glutathione reductase from human erythrocytes. In: Singer, T.P. and Ondarza, R.N. (Eds.), Mechanisms of Oxidizing Enzymes, Elsevier North Holland, New York, 1978, p. 17-22.
2. Pigiet, V.P. and Conley, R.R. Purification of thioredoxin, thioredoxin reductase, and glutathione reductase by affinity chromatography. J. Biol. Chem. 252 (1977) 6367-6372. [PMID: 330529]
3. Racker, E. Glutathione reductase from bakers' yeast and beef liver. J. Biol. Chem. 217 (1955) 855-865.
4. van Heyningen, R. and Pirie, A. Reduction of glutathione coupled with oxidative decarboxylation of malate in cattle lens. Biochem. J. 53 (1953) 436-444.
5. Worthington, D.J. and Rosemeyer, M.A. Glutathione reductase from human erythrocytes. Catalytic properties and aggregation. Eur. J. Biochem. 67 (1976) 231-238. [PMID: 9277]
6. Böhmé, C.C., Arscott, L.D., Becker, K., Schirmer, R.H. and Williams, C.H., Jr. Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme. J. Biol. Chem. 275 (2000) 37317-37323. [PMID: 10969088]
7. Libreros-Minotta, C.A., Pardo, J.P., Mendoza-Hernandez, G. and Rendon, J.L. Purification and characterization of glutathione reductase from Rhodospirillum rubrum. Arch Biochem Biophys 298 (1992) 247-253. [PMID: 1524433]
Common name: protein-disulfide reductase
Reaction: protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H + H+
Other name(s): protein disulphide reductase; insulin-glutathione transhydrogenase; disulfide reductase; NAD(P)H2:protein-disulfide oxidoreductase
Systematic name: protein-dithiol:NAD(P)+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9029-19-0
References:
1. Hatch, M.D. and Turner, J.F. A protein disulphide reductase from pea seeds. Biochem. J. 76 (1960) 556-562.
Common name: thioredoxin-disulfide reductase
Reaction: thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
Glossary: The term 'oxidized thioredoxin' has been replaced by 'thioredoxin disulfide' as the former is ambiguous.
Other name(s): NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase
Systematic name: thioredoxin:NADP+ oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, WIT, CAS registry number: 9074-14-0
References:
1. Moore, E.C., Reichard, P. and Thelander, L. Enzymatic synthesis of deoxyribonucleotides. V. Purification and properties of thioredoxin reductase from Escherichia coli B. J. Biol. Chem. 239 (1964) 3445-3452.
2. Speranza, M.L., Ronchi, S. and Minchiotti, L. Purification and characterization of yeast thioredoxin reductase. Biochim. Biophys. Acta 327 (1973) 274-281. [PMID: 4149839]
3. Arner, E.S. and Holmgren, A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267 (2000) 6102-6109. [PMID: 11012661]
Common name: CoA-glutathione reductase
Reaction: CoA + glutathione + NADP+ = CoA-glutathione + NADPH + H+
Other name(s): coenzyme A glutathione disulfide reductase; NADPH-dependent coenzyme A-SS-glutathione reductase; coenzyme A disulfide-glutathione reductase; NADPH2:CoA-glutathione oxidoreductase
Systematic name: glutathione:NADP+ oxidoreductase (CoA-acylating)
Comments: A flavoprotein. The substrate is a mixed disulfide. May be identical to EC 1.8.1.9, thioredoxin-disulfide reductase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37256-33-0
References:
1. Ondarza, R.N., Abney, R. and López-Colomé, A.M. Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from yeast. Biochim. Biophys. Acta 191 (1969) 239-248. [PMID: 4390951]
2. Ondarza, R.N., Escamilla, E., Gutierrez, J. and De la Chica, G. CoAS-Sglutathione and GSSG reductases from rat liver. Two disulfide oxidoreductase activities in one protein entity. Biochim. Biophys. Acta 341 (1974) 162-171. [PMID: 4151341]
3. Carlberg, I. and Mannervik, B. Purification by affinity chromatography of yeast glutathione reductase, the enzyme responsible for the NADPH-dependent reduction of the mixed disulfide of coenzyme A and glutathione. Biochim. Biophys. Acta 484 (1977) 268-274. [PMID: 334266]
Common name: asparagusate reductase
Reaction: 3-mercapto-2-mercaptomethylpropanoate + NAD+ = asparagusate + NADH + H+
For diagram click here.
Other name(s): asparagusate dehydrogenase; asparagusic dehydrogenase; asparagusate reductase (NADH2); NADH2:asparagusate oxidoreductase
Systematic name: 3-mercapto-2-mercaptomethylpropanoate:NAD+ oxidoreductase
Comments: Also acts on lipoate.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 56126-52-4
References:
1. Yanagawa, H. and Egami, F. Asparagusate dehydrogenases and lipoyl dehydrogenase from asparagus mitochondria. Biochim. Biophys. Acta 384 (1975) 342-352. [PMID: 1125255]
2. Yanagawa, H. and Egami, F. Asparagusate dehydrogenases and lipoyl dehydrogenase from asparagus mitochondria. Physical, chemical, and enzymatic properties. J. Biol. Chem. 251 (1976) 3637-3644. [PMID: 180003]
Common name: trypanothione-disulfide reductase
Reaction: trypanothione + NADP+ = trypanothione disulfide + NADPH + H+
Other name(s): trypanothione reductase; NADPH2:trypanothione oxidoreductase
Systematic name: trypanothione:NADP+ oxidoreductase
Comments: Trypanothione disulfide is the oxidized form of N1,N6-bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata. The enzyme from Crithidia fasciculata is a flavoprotein (FAD), whose activity is dependent on a redox-active cystine at the active centre. (cf. EC 1.8.1.7, glutathione-disulfide reductase)
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 102210-35-5
References:
1. Shames, S.L., Fairlamb, A.H., Cerami, A. and Walsh, C.T. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. Biochemistry 25 (1986) 3519-3526.
2. Marsh, I.R. and Bradley, M. Substrate specificity of trypanothione reductase. Eur. J. Biochem. 243 (1977) 690-694. [PMID: 9057833]
3. Cunningham, M.L. and Fairlamb, A.H. Trypanothione reductase from Leishmania donovani. Purification, characterisation and inhibition by trivalent antimonials. Eur. J. Biochem. 230 (1995) 460-468. [PMID: 7607216]
Common name: bis-γ-glutamylcystine reductase
Reaction: 2 γ-glutamylcysteine + NADP+ = bis-γ-glutamylcystine + NADPH + H+
Other name(s): NADPH2:bis-γ-glutamylcysteine oxidoreductase
Systematic name: γ-glutamylcysteine:NADP+ oxidoreductase
Comments: Highly specific. Not identical with EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.14 (CoA-disulfide reductase).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 117056-54-9
References:
1. Sundquist, A.R. and Fahey, R.C. The novel disulfide reductase bis-γ-glutamylcystine reductase and dihydrolipoamide dehydrogenase from Halobacterium halobium: purification by immobilized-metal-ion affinity chromatography and properties of the enzymes. J. Bacteriol. 170 (1988) 3459-3467. [PMID: 3136140]
2. Sundquist, A.R. and Fahey, R.C. The function of γ-glutamylcysteine and bis-γ-glutamylcystine reductase in Halobacterium halobium. J. Biol. Chem. 264 (1989) 719-725. [PMID: 2910862]
Common name: CoA-disulfide reductase
Reaction: 2 CoA + NAD+ = CoA-disulfide + NADH + H+
Other name(s): CoA-disulfide reductase (NADH2); NADH2:CoA-disulfide oxidoreductase
Systematic name: CoA:NAD+ oxidoreductase
Comments: Not identical with EC 1.8.1.6 (cystine reductase), EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.13 (bis-γ-glutamylcystine reductase).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 206770-55-0
References:
1. Setlow, B. and Setlow, P. Levels of acetyl coenzyme A, reduced and oxidized coenzyme A, and coenzyme A in disulfide linkage to protein in dormant and germinated spores and growing and sporulating cells of Bacillus megaterium. J. Bacteriol. 132 (1977) 444-452. [PMID: 410791]
2. delCardayre, S.B., Stock, K.P., Newton, G.L., Fahey, R.C. and Davies, J.E. Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme. J. Biol. Chem. 273 (1998) 5744-5751. [PMID: 9488707]
Common name: mycothione reductase
Reaction: 2 mycothiol + NAD(P)+ = mycothione + NAD(P)H + H+
Glossary:
mycothiol = 1-O-(2-[N-acetyl-L-cysteinyl]amido-2-deoxy-α-D-glucopyranosyl)-D-myo-inositol
mycothione = oxidized (disulfide) form of mycothiol
Other name(s): mycothiol-disulfide reductase
Systematic name: mycothiol:NAD(P)+ oxidoreductase
Comments: Contains FAD. No activity with glutathione, trypanothione or coenzyme A as substrate.
References:
1. Patel, M.P. and Blanchard, J.S. Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase. Biochemistry 38 (1999) 11827-11833. [PMID: 10512639]
2. Patel, M.P. and Blanchard, J.S. Mycobacterium tuberculosis mycothione reductase: pH dependence of the kinetic parameters and kinetic isotope effects. Biochemistry 40 (2001) 5119-5126. [PMID: 11318633]
Common name: methylsterol monooxygenase
Reaction: 4,4-dimethyl-5α-cholest-7-en-3β-ol + NAD(P)H + H+ + O2 = 4β-hydroxymethyl-4α-methyl-5α-cholest-7-en-3β-ol + NAD(P)+ + H2O
4β-hydroxymethyl-4α-methyl-5α-cholest-7-en-3β-ol + NAD(P)H + H+ + O2 = 3β-hydroxy-4β-methyl-5α-cholest-7-ene-4α-carbaldehyde + NAD(P)+ + 2 H2O
3β-hydroxy-4β-methyl-5α-cholest-7-ene-4α-carbaldehyde + NAD(P)H + H+ + O2 = 3β-hydroxy-4β-methyl-5α-cholest-7-ene-4α-carboxylate + NAD(P)+ + H2O
For diagram click here.
Other name(s): methylsterol hydroxylase; 4-methylsterol oxidase
Systematic name: 4,4-dimethyl-5α-cholest-7-en-3β-ol,hydrogen-donor:oxygen oxidoreductase (hydroxylating)
Comments: Requires cytochrome b5. Also acts on 4α-methyl-5α-cholest-7-en-3β-ol. The sterol can be based on cycloartenol as well as lanosterol. Formerly EC 1.14.99.16.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37256-80-7
References:
1. Rahier, A., Smith, M. and Taton, M. The role of cytochrome b5 in 4α-methyl-oxidation and C5(6) desaturation of plant sterol precursors. Biochem. Biophys. Res. Commun. 236 (1997) 434-437. [PMID: 9240456]
2. Pascal, S., Taton, M. and Rahier, A. Plant sterol biosynthesis. Identification and characterization of two distinct microsomal oxidative enzymatic systems involved in sterol C4-demethylation. J. Biol. Chem. 268 (1993) 11639-11654. [PMID: 8505296 ]
3. Kawata, S., Trzaskos, J.M. and Gaylor, J.L. Affinity chromatography of microsomal enzymes on immobilized detergent-solubilized cytochrome b5. J. Biol. Chem. 261 (1986) 3790-3799. [PMID: 3949790 ]
4. Fukushima, H., Grinstead, G.F. and Gaylor, J.L. Total enzymic synthesis of cholesterol from lanosterol. Cytochrome b5-dependence of 4-methyl sterol oxidase. J. Biol. Chem. 256 (1981) 4822-4826. [PMID: 7228857 ]
5. Brady, D.R., Crowder, R.D. and Hayes, W.J. Mixed function oxidases in sterol metabolism. Source of reducing equivalents. J. Biol. Chem. 255 (1980) 10624-10629. [PMID: 7430141 ]
6. Gaylor, J.L. and Mason, H.S. Investigation of the component reactions of oxidative sterol demethylation. Evidence against participation of cytochrome P-450. J. Biol. Chem. 243 (1968) 4966-4972. [PMID: 4234469]
7. Miller, W.L., Kalafer, M.E., Gaylor, J.L. and Delwicke, C.V. Investigation of the component reactions of oxidative sterol demethylation. Study of the aerobic and anaerobic processes. Biochemistry 6 (1967) 2673-2678. [PMID: 4383278]
[EC 1.14.14.4 Deleted entry: choline monooxygenase. Identical to EC 1.14.15.7 (EC 1.14.14.4 created 2000, deleted 2002)]
Common name: choline monooxygenase
Reaction: choline + O2 + 2 reduced ferredoxin + 2 H+ = betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin
Glossary
betaine: N,N,N-trimethylammonioacetate
betaine aldehyde: N,N,N-trimethyl-2-oxoethylammonium
choline: (2-hydroxyethyl)trimethylammonium
Systematic name: choline,reduced-ferredoxin:oxygen oxidoreductase
Comments: The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Brouquisse, R., Weigel, P., Rhodes, D., Yocum, C.F. and Hanson, A.D. Evidence for a ferredoxin-dependent choline monooxygenase from spinach chloroplast stroma. Plant Physiol. 90 (1989) 322-329.
2. Burnet, M., Lafontaine, P.J. and Hanson, A.D. Assay, purification, and partial characterization of choline monooxygenase from spinach. Plant Physiol. 108 (1995) 581-588.
3. Rathinasabapathi, B., Burnet, M., Russell, B.L., Gage, D.A., Liao, P., Nye, G.J., Scott, P., Golbeck, J.H. and Hanson, A.D. Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning. Proc. Natl. Acad. Sci. USA 94 (1997) 3454-3458. [PMID: 9096415]
4. Russell, B.L., Rathinasabapathi, B. and Hanson, A.D. Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth. Plant Physiol. 116 (1998) 859-865. [PMID: 9489025]
5. Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. Glycine betaine synthesis in transgenic tobacco expressing choline monooxygenase is limited by the endogenous choline supply. Plant J. 16 (1998) 101-110.
6. Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. The endogenous choline supply limits glycine betaine synthesis in transgenic tobacco expressing choline. Plant J. 16 (1998) 487-496. [PMID: 9881168]
[EC 1.14.99.16 Transferred entry: now EC 1.14.13.72, methylsterol monooxygenase (EC 1.14.99.16 created 1972, deleted 2002)]
Common name: aquacobalamin reductase
Reaction: 2 cob(II)alamin + NAD+ = 2 aquacob(III)alamin + NADH + H+
Other name(s): aquocobalamin reductase; vitamin B12a reductase; NADH-linked aquacobalamin reductase; B12a reductase; NADH2:cob(III)alamin oxidoreductase
Systematic name: cob(II)alamin:NAD+ oxidoreductase
Comments: A flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37256-39-6
References:
1. Walker, G.A., Murphy, S. and Huennekens, F.M. Enzymatic conversion of vitamin B12a to adenosyl-B12: evidence for the existence of two separate reducing systems. Arch. Biochem. Biophys. 134 (1969) 95-102. [PMID: 4390543]
Common name: cob(II)alamin reductase
Reaction: 2 cob(I)alamin + NAD+ = 2 cob(II)alamin + NADH + H+
Other name(s): vitamin B12r reductase; B12r reductase; NADH2:cob(II)alamin oxidoreductase
Systematic name: cob(I)alamin:NAD+ oxidoreductase
Comments: A flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37256-40-9
References:
1. Walker, G.A., Murphy, S. and Huennekens, F.M. Enzymatic conversion of vitamin B12a to adenosyl-B12: evidence for the existence of two separate reducing systems. Arch. Biochem. Biophys. 134 (1969) 95-102. [PMID: 4390543]
Common name: aquacobalamin reductase (NADPH)
Reaction: 2 cob(II)alamin + NADP+ = 2 aquacob(III)alamin + NADPH + H+
Other name(s): aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH-linked aquacobalamin reductase; NADPH2:aquacob(III)alamin oxidoreductase
Systematic name: cob(II)alamin:NADP+ oxidoreductase
Comments: A flavoprotein. Acts on aquacob(III)alamin and hydroxycobalamin, but not on cyanocobalamin.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 110777-32-7
References:
1. Watanabe, F., Oki, Y., Nakano, Y. and Kitaoka, S. Purification and characterization of aquacobalamin reductase (NADPH) from Euglena gracilis. J. Biol. Chem. 262 (1987) 11514-11518. [PMID: 3114247]
2. Watanabe, F., Yamaji, R., Isegawa, Y., Yamamoto, T., Tamura, Y. and Nakano, Y. Characterization of aquacobalamin reductase (NADPH) from Euglena gracilis. Arch. Biochem. Biophys. 305 (1993) 421-427. [PMID: 8373179]
Common name: cyanocobalamin reductase (cyanide-eliminating)
Reaction: cob(I)alamin + cyanide + NADP+ = cyanocob(III)alamin + NADPH + H+
Other name(s): cyanocobalamin reductase; cyanocobalamin reductase (NADPH, cyanide-eliminating); cyanocobalamin reductase (NADPH; CN-eliminating); NADPH2:cyanocob(III)alamin oxidoreductase (cyanide-eliminating)
Systematic name: cob(I)alamin, cyanide:NADP+ oxidoreductase
Comments: A flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 131145-00-1
References:
1. Watanabe, F., Oki, Y., Nakano, Y. and Kitaoka, S. Occurrence and characterization of cyanocobalamin reductase (NADPH; CN-eliminating) involved in decyanation of cyanocobalamin in Euglena gracilis. J. Nutr. Sci. Vitaminol. 34 (1988) 1-10. [PMID: 3134526]
Common name: ferric-chelate reductase
Reaction: 2 Fe(II) + NAD+ = 2 Fe(III) + NADH + H+
Other name(s): ferric chelate reductase; iron chelate reductase; NADH:Fe3+-EDTA reductase; NADH2:Fe3+ oxidoreductase
Systematic name: Fe(II):NAD+ oxidoreductase
Comments: Involved in the transport of iron across plant plasma membranes.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 122097-10-3
References:
1. Askerlund, P., Larrson, C. and Widell, S. Localization of donor and acceptor sites of NADH dehydrogenase activities using inside-out and right-side-out plasma membrane vesicles from plants. FEBS Lett. 239 (1988) 23-28.
2. Brüggemann, W. and Moog, P.R. NADH-dependent Fe3+ EDTA and oxygen reduction by plasma membrane vesicles from barley roots. Physiol. Plant. 75 (1989) 245-254.
3. Brüggemann, W., Moog, P.R., Nakagawa, H., Janiesch, P. and Kuiper, P.J.C. Plasma membrane-bound NADH:Fe3+-EDTA reductase and iron deficiency in tomato (Lycopersicon esculentum). Is there a Turbo reductase ? Physiol. Plant. 79 (1990) 339-346.
4. Buckhout, T.J. and Hrubec, T.C. Pyridine nucleotide-dependent ferricyanide reduction associated with isolated plasma membranes of maize (Zea mays L.) roots. Protoplasma 135 (1986) 144-154.
5. Sandelius, A.S., Barr, R., Crane, F.L. and Morré, D.J. Redox reactions of plasma membranes isolated from soybean hypocotyls by phase partition. Plant Sci. 48 (1986) 1-10.
Common name: trans-aconitate 2-methyltransferase
Reaction: S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-3-(methoxycarbonyl)pent-2-enedioate
For diagram click here.
Glossary:
trans-aconitate = (E)-prop-1-ene-1,2,3-tricarboxylate
Systematic name: S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate 2'-O-methyltransferase
Comments: Also catalyses the formation of the methyl monoester of cis-aconitate, isocitrate and citrate, but more slowly. While the enzyme from Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate as the product, that from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.145, trans-aconitate 3-methyltransferase).
References:
1. Cai, H. and Clarke, S. A novel methyltransferase catalyzes the esterification of trans-aconitate in Escherichia coli. J. Biol. Chem. 274 (1999) 13470-13479. [PMID: 10224113]
2. Cai, H., Strouse, J., Dumlao, D., Jung, M.E. and Clarke, S. Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferase. Biochemistry 40 (2001) 2210-2219. [PMID: 11329290]
Common name: trans-aconitate 3-methyltransferase
Reaction: S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate
For diagram click here.
Glossary:
trans-aconitate = (E)-prop-1-ene-1,2,3-tricarboxylate
Systematic name: S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate 3'-O-methyltransferase
Comments: Also catalyses the formation of the methyl monoester of cis-aconitate, isocitrate and citrate, but more slowly. While the enzyme from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate as the product, that from Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.144, trans-aconitate 2-methyltransferase)
References:
1. Cai, H. and Clarke, S. A novel methyltransferase catalyzes the esterification of trans-aconitate in Escherichia coli. J. Biol. Chem. 274 (1999) 13470-13479. [PMID: 10224113]
2. Cai, H., Strouse, J., Dumlao, D., Jung, M.E. and Clarke, S. Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferase. Biochemistry 40 (2001) 2210-2219. [PMID: 11329290]
Common name: glycoprotein 6-α-L-fucosyltransferase
Reaction: GDP-L-fucose + N4-{N-acetyl-β-D-glucosaminyl-(1![[arrow right]](../../../greek/ARROWR.GIF)
2)-α-D-mannosyl-(13)-[N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(16)]-β-D-mannosyl-(14)-N-acetyl-β-D-glucosaminyl-(14)-N-acetyl-β-D-glucosaminyl}asparagine = GDP + N4-{N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(13)-[N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(16)]-β-D-mannosyl-(14)-N-acetyl-β-D-glucosaminyl-(14)-[α-L-fucosyl-(16)]-N-acetyl-β-D-glucosaminyl}asparagine
For diagram click here.
Other name(s): GDPfucose-glycoprotein fucosyltransferase; GDP-L-Fuc:N-acetyl-β-D-glucosaminide α16fucosyltransferase; GDP-L-fucose-glycoprotein fucosyltransferase; glycoprotein fucosyltransferase; guanosine diphosphofucose-glycoprotein fucosyltransferase
Systematic name: GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(13)-[N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(16)]-β-D-mannosyl-(14)-N-acetyl-β-D-glucosaminyl-(14)-N-acetyl-β-D-glucosaminyl}asparagine) 6-α-L-fucosyl-transferase
Comments: This enzyme catalyses a reaction similar to that of EC 2.4.1.214, glycoprotein 3-α-L-fucosyltransferase, but transfers the L-fucosyl group from GDP-β-L-fucose to form an α1,6-linkage rather than an α1,3-linkage.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9033-08-3
References:
1. Longmore, G.D. and Schachter, H. Product-identification and substrate-specificity studies of the GDP-L-fucose:2-acetamido-2-deoxy-β-D-glucoside (FUC Asn-linked GlcNAc) 6-α-L-fucosyltransferase in a Golgi-rich fraction from porcine liver. Carbohydr. Res. 100 (1982) 365-392. [PMID: 7083256]
2. Voynow, J.A., Scanlin, T.F. and Glick, M.C. A quantitative method for GDP-L-Fuc:N-acetyl-β-D-glucosaminide α16fucosyltransferase activity with lectin affinity chromatography. Anal. Biochem. 168 (1988) 367-373. [PMID: 3364733]
3. Uozumi, N., Yanagidani, S., Miyoshi, E., Ihara, Y., Sakuma, T., Gao, C.-X., Teshima, T., Fujii, S., Shiba, T. and Taniguchi, N. Purification and cDNA cloning of porcine brain GDP-L-Fuc:N-acetyl-β-D-glucosaminide α16fucosyltransferase. J. Biol. Chem. 271 (1996) 27810-27817. [PMID: 8910378]
Common name: glycoprotein 3-α-L-fucosyltransferase
Reaction: GDP-L-fucose + N4-{N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(13)-[N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(16)]-β-D-mannosyl-(14)-N-acetyl-β-D-glucosaminyl-(14)-N-acetyl-β-D-glucosaminyl}asparagine = GDP + N4-{N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(13)-[N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(16)]-β-D-mannosyl-(14)-N-acetyl-β-D-glucosaminyl-(14)-[α-L-fucosyl-(13)]-N-acetyl-β-D-glucosaminyl}asparagine
For diagram click here.
Other name(s): GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1,3-fucosyltransferase; GDP-L-Fuc:Asn-linked GlcNAc α1,3-fucosyltransferase; GDP-fucose:β-N-acetylglucosamine (Fuc to (Fucα16GlcNAc)-Asn-peptide) α13-fucosyltransferase
Systematic name: GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(13)-[N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(16)]-β-D-mannosyl-(14)-N-acetyl-β-D-glucosaminyl-(14)-N-acetyl-β-D-glucosaminyl}asparagine) 3-α-L-fucosyl-transferase
Comments: Requires Mn2+. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. This enzyme catalyses a reaction similar to that of EC 2.4.1.68, glycoprotein 6-α-L-fucosyltransferase, but transferring the L-fucosyl group from GDP-β-L-fucose to form an α1,3-linkage rather than an α1,6-linkage. The N-glycan products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea).
References:
1. Wilson, I.B.H., Rendic, D., Freilinger, A., Dumic, J., Altmann, F., Mucha, J., Müller, S. and Hauser, M.-T. Cloning and expression of α1,3-fucosyltransferase homologues from Arabidopsis thaliana. Biochim. Biophys. Acta 1527 (2001) 88-96. [PMID: 11420147]
2. Fabini, G., Freilinger, A., Altmann, F. and Wilson, I.B.H. Identification of core α1,3-fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the neural anti-horseradish peroxidase epitope. J. Biol. Chem. 276 (2001) 28058-28067. [PMID: 11382750]
3. Leiter, H., Mucha, J., Staudacher, E., Grimm, R., Glössl, J. and Altmann, F. Purification, cDNA cloning, and expression of GDP-L-Fuc:Asn-linked GlcNAc α1,3-fucosyltransferase from mung beans. J. Biol. Chem. 274 (1999) 21830-21839. [PMID: 10419500]
4. van Tetering, A., Schiphorst, W.E.C.M., van den Eijnden, D.H. and van Die, I. Characterization of core α13-fucosyltransferase from the snail Lymnaea stagnalis that is involved in the synthesis of complex type N-glycans. FEBS Lett. 461 (1999) 311-314. [PMID: 10567717]
5. Staudacher, E., Altmann, F., Glössl, J., März, L., Schachter, H., Kamerling, J.P., Hård, K. and Vliegenthart, J.F.G. GDP-fucose:β-N-acetylglucosamine (Fuc to (Fucα16GlcNAc)-Asn-peptide) α13-fucosyltransferase activity in honeybee (Apis mellifica) venom glands. The difucosylation of asparagine-bound N-acetylglucosamine. Eur. J. Biochem. 199 (1991) 745-751. [PMID: 1868856]
Common name: glycoprotein 2-β-D-xylosyltransferase
Reaction: UDP-D-xylose + N4-{N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(13)-[N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(16)]-β-D-mannosyl-(14)-N-acetyl-β-D-glucosaminyl-(14)-N-acetyl-β-D-glucosaminyl}asparagine = UDP + N4-{N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(13)-[N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(16)]-[β-D-xylosyl-(12)]-β-D-mannosyl-(14)-N-acetyl-β-D-glucosaminyl-(14)-N-acetyl-β-D-glucosaminyl}asparagine
For diagram click here.
Other name(s): β1,2-xylosyltransferase
Systematic name: UDP-D-xylose:glycoprotein (D-xylose to the 3,6-disubstituted mannose of N4-{N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(13)-[N-acetyl-β-D-glucosaminyl-(12)-α-D-mannosyl-(16)]-β-D-mannosyl-(14)-N-acetyl-β-D-glucosaminyl-(14)-N-acetyl-β-D-glucosaminyl}asparagine) 2-β-D-xylosyltransferase
Comments: Specific for N-linked oligosaccharides (N-glycans).
References:
1. Zeng, Y., Bannon, G., Thomas, V.H., Rice, K., Drake, R. and Elbein, A. Purification and specificity of β1,2-xylosyltransferase, an enzyme that contributes to the allergenicity of some plant proteins. J. Biol. Chem. 272 (1997) 31340-31347. [PMID: 9395463]
2. Strasser, R., Mucha, J., Mach, L., Altmann, F., Wilson, I.B., Glössl, J. and Steinkellner, H. Molecular cloning and functional expression of β1,2-xylosyltransferase cDNA from Arabidopsis thaliana. FEBS Lett. 472 (2000) 105-108. [PMID: 10781814]
Common name: protein-glutamate methylesterase
Reaction: protein L-glutamate O5-methyl ester + H2O = protein L-glutamate + methanol
Other name(s): chemotaxis-specific methylesterase; methyl-accepting chemotaxis protein methyl-esterase; CheB methylesterase; methylesterase CheB; protein methyl-esterase; protein carboxyl methylesterase; PME; protein methylesterase
Systematic name: protein-L-glutamate-O5-methyl-ester acylhydrolase
Comments: Hydrolyses the products of EC 2.1.1.77 (protein-L-isoaspartate(D-aspartate) O-methyltransferase), EC 2.1.1.78 (isoorientin 3'-O-methyltransferase), EC 2.1.1.80 (protein-glutamate O-methyltransferase) and EC 2.1.1.100 (protein-S-isoprenylcysteine O-methyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Gagnon, C., Harbour, G. and Camato, R. Purification and characterization of protein methylesterase from rat kidney. J. Biol. Chem. 259 (1984) 10212-10215. [PMID: 6469959]
2. Kehry, M.R., Doak, T.G. and Dahlquist, F.W. Stimulus-induced changes in methylesterase activity during chemotaxis in Escherichia coli. J. Biol. Chem. 259 (1984) 11828-11835. [PMID: 6384215]
[EC 3.5.1.80 Deleted entry: identical to EC 3.5.1.25, N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.80 created 1999, deleted 2002)]
Common name: pectate lyase
Reaction: Eliminative cleavage of (14)-α-D-galacturonan to give oligosaccharides with 4-deoxy-α-D-galact-4-enuronosyl groups at their non-reducing ends
For diagram click here.
Other name(s): pectate transeliminase; polygalacturonic transeliminase; pectic acid transeliminase; polygalacturonate lyase; endopectin methyltranseliminase; pectate transeliminase; endogalacturonate transeliminase; pectic acid lyase; pectic lyase; α-1,4-D-endopolygalacturonic acid lyase; PGA lyase; PPase-N; endo-α-1,4-polygalacturonic acid lyase; polygalacturonic acid lyase; pectin trans-eliminase; Polygalacturonic acid trans-eliminase
Systematic name: (14)-α-D-galacturonan lyase
Comments: Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase). Formerly EC 4.2.99.3.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9015-75-2
References:
1. Albersheim, P. and Killias, U. Studies relating to the purification and properties of pectin transeliminase. Arch. Biochem. Biophys. 97 (1962) 107-115.
2. Edstrom, R.D. and Phaff, H.J. Purification and certain properties of pectin trans-eliminase from Aspergillus fonsecaeus. J. Biol. Chem. 239 (1964) 2403-2408.
3. Edstrom, R.D. and Phaff, H.J. Eliminative cleavage of pectin and of oligogalacturonide methyl esters by pectin trans-eliminase. J. Biol. Chem. 239 (1964) 2409-2415.
4. Nagel, C.W. and Vaughn, R.H. The degradation of oligogalacturonides by the polygalacturonase of Bacillus polymyxa. Arch. Biochem. Biophys. 94 (1961) 328.
5. Nasuno, S. and Starr, M.P. Polygalacturonic acid trans-eliminase of Xanthomonas campestris. Biochem. J. 104 (1967) 178-185. [PMID: 6035509]
6. Mayans, O., Scott, M., Connerton, I., Gravesen, T., Benen, J., Visser, J., Pickersgill, R. and Jenkins, J. Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases. Structure 5 (1997) 677-689. [PMID: 9195887]
Common name: pectate disaccharide-lyase
Reaction: Eliminative cleavage of 4-(4-deoxy-α-D-galact-4-enuronosyl)-D-galacturonate from the reducing end of pectate, i.e. de-esterified pectin
For diagram click here.
Other name(s): pectate exo-lyase; exopectic acid transeliminase; exopectate lyase; exopolygalacturonic acid-trans-eliminase; PATE; exo-PATE; exo-PGL
Systematic name: (14)-α-D-galacturonan reducing-end-disaccharide-lyase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37290-87-2
References:
1. Macmillan, J.D. and Vaughn, R.H. Purification and properties of a polygalacturonic acid-trans-eliminase produced by Clostridium multifermentans. Biochemistry 3 (1964) 564-572.
Common name: pectin lyase
Reaction: Eliminative cleavage of (14)-α-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-α-D-galact-4-enuronosyl groups at their non-reducing ends
For diagram click here.
Other name(s): pectin trans-eliminase; endo-pectin lyase; polymethylgalacturonic transeliminase; pectin methyltranseliminase; pectolyase; PL; PNL; PMGL
Systematic name: (14)-6-O-methyl-α-D-galacturonan lyase
Comments: Favours pectin, the methyl ester, over pectate, the anion (which is the preferred substrate of EC 4.2.2.2, pectate lyase). Demethylation progressively slows its action; it can nevertheless cleave on either side of a demethylated residue if the residue at the other end of the scissile bond is methylated.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9033-35-6
References:
1. Albersheim, P., Neukom, H. and Deuel, H. Über die Bildung von ungesättigten Abbauprodukten durch ein pekinabbauendes Enzym. Helv. Chim. Acta 43 (1960) 1422-1426.
2. Mayans, O., Scott, M., Connerton, I., Gravesen, T., Benen, J., Visser, J., Pickersgill, R. and Jenkins, J. Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases. Structure 5 (1997) 677-689. [PMID: 9195887]
3. Kester, H.C.M and Visser, J. Purification and characterization of pectin lyase B, a novel pectinolytic enzyme from Aspergillus niger. FEMS Microbiol. Lett. 120 (1994) 63-68.
4. Mutenda, K.E., Körner, R., Christensen, T.M.I.E., Mikkelsen, J. and Roepstorff, P. Application of mass spectrometry to determine the activity and specificity of pectin lyase A. Carbohydr.Res. 337 (2002) 1213-1223. [PMID: 12110197]
Common name: isopentenyl-diphosphate δ-isomerase
Reaction: isopentenyl diphosphate = dimethylallyl diphosphate
For reaction pathway click here.
Other name(s): isopentenylpyrophosphate δ-isomerase; methylbutenylpyrophosphate isomerase; isopentenylpyrophosphate isomerase
Systematic name: isopentenyl-diphosphate δ3-δ2-isomerase
Comments: The enzyme from Streptomyces sp. strain CL190 requires FMN and NAD(P)H as cofactors. Activity is reduced if FMN is replaced by FAD, but the enzyme becomes inactive when NAD(P)H is replaced by NAD or NADP. That enzyme also requires Mg2+, Mn2+ or Ca2+ for activity.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, WIT, CAS registry number: 9033-27-6
References:
1. Kaneda, K., Kuzuyama, T., Takagi, M., Hayakawa, Y. and Seto, H. An unusual isopentenyl diphosphate isomerase found in the mevalonate pathway gene cluster from Streptomyces sp. strain CL190. Proc. Natl. Acad. Sci. USA 98 (2001) 932-937. [PMID: 11158573]
2. Bishop, J.M. Cellular oncogenes and retroviruses. Annu. Rev. Biochem. 52 (1983) 301-354. [PMID: 6351725]
3. Agranoff, B.W., Eggerer, H., Henning, U. and Lynen, F. Biosynthesis of terpenes. VII. Isopentenyl pyrophosphate isomerase. J. Biol. Chem. 235 (1960) 326-332.