Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)

Proposed Changes to the Enzyme List

The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC-IUBMB by Keith Tipton, Sinéad Boyce, Gerry Moss, Dick Cammack and Hal Dixon, with assistance from Alan Chester, and were put on the web by Gerry Moss. Comments and suggestions on these draft entries should be sent to Professor K.F. Tipton and Dr S. Boyce (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland). These entries were made public January 2002 and approved April 2002.

An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.


*EC 1.1.1.88

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.

[EC 1.1.1.88 created 1972, modified 2002]

*EC 1.1.1.170

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]

[EC 1.1.1.170 created 1978, modified 2002]

EC 1.1.1.270

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]

[EC 1.1.1.270 created 2002]

*EC 1.2.3.1

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]

[EC 1.2.3.1 created 1961, modified 2002]

*EC 1.2.3.9

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.

[EC 1.2.3.9 created 1986, modified 2002]

*EC 1.2.3.11

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]

[EC 1.2.3.11 created 1990, modified 2002]

EC 1.5.1.29

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]

[EC 1.5.1.29 created 1981 as EC 1.6.8.1, transferred 2002 to EC 1.5.1.29]

EC 1.5.1.30

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 1.5.1.30 created 1982 as EC 1.6.8.2, transferred 2002 to EC 1.5.1.30]

[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

EC 1.7.1.1

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]

[EC 1.7.1.1 created 1961 as EC 1.6.6.1, transferred 2002 to EC 1.7.1.1]

EC 1.7.1.2

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]

[EC 1.7.1.2 created 1961 as EC 1.6.6.2, transferred 2002 to EC 1.7.1.2]

EC 1.7.1.3

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]

[EC 1.7.1.3 created 1961 as EC 1.6.6.3, transferred 2002 to EC 1.7.1.3]

EC 1.7.1.4

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]

[EC 1.7.1.4 created 1961 as EC 1.6.6.4, transferred 2002 to EC 1.7.1.4]

EC 1.7.1.5

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.

[EC 1.7.1.5 created 1961 as EC 1.6.6.6, transferred 2002 to EC 1.7.1.5]

EC 1.7.1.6

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]

[EC 1.7.1.6 created 1961 as EC 1.6.6.7, transferred 2002 to EC 1.7.1.6]

EC 1.7.1.7

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 1.7.1.7 created 1965 as EC 1.6.6.8, transferred 2002 to EC 1.7.1.7]

[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)]

EC 1.7.1.9

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]

[EC 1.7.1.9 created 1972 as EC 1.6.6.10, transferred 2002 to EC 1.7.1.9]

EC 1.7.1.10

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.

[EC 1.7.1.10 created 1972 as EC 1.6.6.11, transferred 2002 to EC 1.7.1.10]

EC 1.7.1.11

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]

[EC 1.7.1.11 created 1989 as EC 1.6.6.12, transferred 2002 to EC 1.7.1.11]

EC 1.7.1.12

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]

[EC 1.7.1.12 created 1989 as EC 1.6.6.13, transferred 2002 to EC 1.7.1.12]

EC 1.8.1.6

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]

[EC 1.8.1.6 created 1961 as EC 1.6.4.1, transferred 2002 to EC 1.8.1.6]

EC 1.8.1.7

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]

[EC 1.8.1.7 created 1961 as EC 1.6.4.2, modified 1989, transferred 2002 to EC 1.8.1.7]

EC 1.8.1.8

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.

[EC 1.8.1.8 created 1965 as EC 1.6.4.4, transferred 2002 to EC 1.8.1.8]

EC 1.8.1.9

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]

[EC 1.8.1.9 created 1972 as EC 1.6.4.5, transferred 2002 to EC 1.8.1.9]

EC 1.8.1.10

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]

[EC 1.8.1.10 created 1972 as EC 1.6.4.6, transferred 2002 to EC 1.8.1.10]

EC 1.8.1.11

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]

[EC 1.8.1.11 created 1978 as EC 1.6.4.7, transferred 2002 to EC 1.8.1.11]

EC 1.8.1.12

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]

[EC 1.8.1.12 created 1989 as EC 1.6.4.8, transferred 2002 to EC 1.8.1.12]

EC 1.8.1.13

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]

[EC 1.8.1.13 created 1992 as EC 1.6.4.9, transferred 2002 to EC 1.8.1.13]

EC 1.8.1.14

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]

[EC 1.8.1.14 created 1992 as EC 1.6.4.10, transferred 2002 to EC 1.8.1.14]

EC 1.8.1.15

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]

[EC 1.8.1.15 created 2002]

EC 1.14.13.72

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 1.14.13.72 created 1972 as EC 1.14.99.16, transferred 2002 to EC 1.14.13.72]

[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)]

*EC 1.14.15.7

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 1.14.15.7 created 2001, modified 2002 (EC 1.14.14.4 created 2000, incorporated 2002)]

[EC 1.14.99.16 Transferred entry: now EC 1.14.13.72, methylsterol monooxygenase (EC 1.14.99.16 created 1972, deleted 2002)]

EC 1.16.1.3

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]

[EC 1.16.1.3 created 1972 as EC 1.6.99.8, transferred 2002 to EC 1.16.1.3]

EC 1.16.1.4

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]

[EC 1.16.1.4 created 1972 as EC 1.6.99.9, transferred 2002 to EC 1.16.1.4]

EC 1.16.1.5

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]

[EC 1.16.1.5 created 1989 as EC 1.6.99.11, transferred 2002 to EC 1.16.1.5]

EC 1.16.1.6

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]

[EC 1.16.1.6 created 1989 as EC 1.6.99.12, transferred 2002 to EC 1.16.1.6]

EC 1.16.1.7

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.

[EC 1.16.1.7 created 1992 as EC 1.6.99.13, transferred 2002 to EC 1.16.1.7]

EC 2.1.1.144

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]

[EC 2.1.1.144 created 2002]

EC 2.1.1.145

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]

[EC 2.1.1.145 created 2002]

*EC 2.4.1.68

Common name: glycoprotein 6-α-L-fucosyltransferase

Reaction: GDP-L-fucose + N4-{N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]3)-[N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]6)]-β-D-mannosyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl}asparagine = GDP + N4-{N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]3)-[N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]6)]-β-D-mannosyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl-(1[arrow right]4)-[α-L-fucosyl-(1[arrow right]6)]-N-acetyl-β-D-glucosaminyl}asparagine

For diagram click here.

Other name(s): GDPfucose-glycoprotein fucosyltransferase; GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1[arrow right]6fucosyltransferase; 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-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]3)-[N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]6)]-β-D-mannosyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl-(1[arrow right]4)-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 [arrow right] 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 α1[arrow right]6fucosyltransferase 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 α1[arrow right]6fucosyltransferase. J. Biol. Chem. 271 (1996) 27810-27817. [PMID: 8910378]

[EC 2.4.1.68 created 1972, modified 2002]

EC 2.4.1.214

Common name: glycoprotein 3-α-L-fucosyltransferase

Reaction: GDP-L-fucose + N4-{N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]3)-[N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]6)]-β-D-mannosyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl}asparagine = GDP + N4-{N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]3)-[N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]6)]-β-D-mannosyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl-(1[arrow right]4)-[α-L-fucosyl-(1[arrow right]3)]-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 (Fucα1[arrow right]6GlcNAc)-Asn-peptide) α1[arrow right]3-fucosyltransferase

Systematic name: GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]3)-[N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]6)]-β-D-mannosyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl-(1[arrow right]4)-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 α1[arrow right]3-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 (Fucα1[arrow right]6GlcNAc)-Asn-peptide) α1[arrow right]3-fucosyltransferase activity in honeybee (Apis mellifica) venom glands. The difucosylation of asparagine-bound N-acetylglucosamine. Eur. J. Biochem. 199 (1991) 745-751. [PMID: 1868856]

[EC 2.4.1.214 created 2001]

EC 2.4.2.38

Common name: glycoprotein 2-β-D-xylosyltransferase

Reaction: UDP-D-xylose + N4-{N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]3)-[N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]6)]-β-D-mannosyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl}asparagine = UDP + N4-{N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]3)-[N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]6)]-[β-D-xylosyl-(1[arrow right]2)]-β-D-mannosyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl-(1[arrow right]4)-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-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]3)-[N-acetyl-β-D-glucosaminyl-(1[arrow right]2)-α-D-mannosyl-(1[arrow right]6)]-β-D-mannosyl-(1[arrow right]4)-N-acetyl-β-D-glucosaminyl-(1[arrow right]4)-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]

[EC 2.4.2.38 created 2001]

*EC 3.1.1.61

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 3.1.1.61 created 1989, modified 2002]

[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)]

*EC 4.2.2.2

Common name: pectate lyase

Reaction: Eliminative cleavage of (1[arrow right]4)-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: (1[arrow right]4)-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]

[EC 4.2.2.2 created 1965 as EC 4.2.99.3, transferred 1972 to EC 4.2.2.2, modified 2002]

*EC 4.2.2.9

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: (1[arrow right]4)-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.

[EC 4.2.2.9 created 1972, modified 2002]

*EC 4.2.2.10

Common name: pectin lyase

Reaction: Eliminative cleavage of (1[arrow right]4)-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: (1[arrow right]4)-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]

[EC 4.2.2.10 created 1972, modified 2002]

*EC 5.3.3.2

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 δ32-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.

[EC 5.3.3.2 created 1961, modified 2002]


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