Enzyme Nomenclature

Continued from EC 1.3.2 to EC 1.3.99

EC 1.4

ACTING ON THE CH-NH2 GROUP OF DONORS

Sections

EC 1.4.1 With NAD+ or NADP+ as acceptor
EC 1.4.2 With a cytochrome as acceptor
EC 1.4.3 With oxygen as acceptor
EC 1.4.4 With a disulfide as acceptor
EC 1.4.5 With a quinone or similar compound as acceptor
EC 1.4.7 With an iron-sulfur protein as acceptor
EC 1.4.9 With a copper protein as acceptor
EC 1.4.98 With other, known, physiological acceptors
EC 1.4.99 With unknown physiological acceptors


EC 1.4.1 With NAD+ or NADP+ as acceptor

Contents

EC 1.4.1.1 alanine dehydrogenase
EC 1.4.1.2 glutamate dehydrogenase
EC 1.4.1.3 glutamate dehydrogenase [NAD(P)+]
EC 1.4.1.4 glutamate dehydrogenase (NADP+)
EC 1.4.1.5 L-amino-acid dehydrogenase
EC 1.4.1.6 deleted, included in EC 1.4.4.1
EC 1.4.1.7 serine 2-dehydrogenase
EC 1.4.1.8 valine dehydrogenase (NADP+)
EC 1.4.1.9 leucine dehydrogenase
EC 1.4.1.10 glycine dehydrogenase
EC 1.4.1.11 L-erythro-3,5-diaminohexanoate dehydrogenase
EC 1.4.1.12 2,4-diaminopentanoate dehydrogenase
EC 1.4.1.13 glutamate synthase (NADPH)
EC 1.4.1.14 glutamate synthase (NADH)
EC 1.4.1.15 lysine dehydrogenase
EC 1.4.1.16 diaminopimelate dehydrogenase
EC 1.4.1.17 N-methylalanine dehydrogenase
EC 1.4.1.18 lysine 6-dehydrogenase
EC 1.4.1.19 tryptophan dehydrogenase
EC 1.4.1.20 phenylalanine dehydrogenase
EC 1.4.1.21 aspartate dehydrogenase
EC 1.4.1.22 deleted
EC 1.4.1.23 valine dehydrogenase (NAD+)
EC 1.4.1.24 3-dehydroquinate synthase II


EC 1.4.1.1

Accepted name: alanine dehydrogenase

Reaction: L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+

Other name(s): AlaDH; L-alanine dehydrogenase; NAD-linked alanine dehydrogenase; α-alanine dehydrogenase; NAD-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase

Systematic name: L-alanine:NAD+ oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-06-5

References:

1. O'Connor, R.J. and Halvorson, H. The substrate specificity of L-alanine dehydrogenase. Biochim. Biophys. Acta 48 (1961) 47-55.

2. Piérard, A. and Wiame, J.M. Propriétés de la L(+)-alanine-déshydrogénase. Biochim. Biophys. Acta 37 (1960) 490-502.

3. Yoshida, A. and Freese, E. Enzymic properties of alanine dehydrogenase of Bacillus subtilis. Biochim. Biophys. Acta 96 (1965) 248-262.

[EC 1.4.1.1 created 1961]

EC 1.4.1.2

Accepted name: glutamate dehydrogenase

Reaction: L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+

Other name(s): glutamic dehydrogenase; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase; NAD-linked glutamic dehydrogenase; NAD-specific glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; NAD:glutamate oxidoreductase; NADH-linked glutamate dehydrogenase

Systematic name: L-glutamate:NAD+ oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-46-1

References:

1. Frieden, C. L-Glutamate dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed. vol. 7, Academic Press, New York, 1963, p. 3-24.

2. Nisman, B. The Stickland reaction. Bacteriol. Rev. 18 (1954) 16-42.

3. Pahlich, E. and Joy, K.W. Glutamate dehydrogenase from pea roots: purification and properties of the enzyme. Can. J. Biochem. 49 (1971) 127-138. [PMID: 4324282]

4. Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F. Glutamate dehydrogenases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic Press, New York, 1975, p. 293-367.

[EC 1.4.1.2 created 1961]

EC 1.4.1.3

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

Reaction: L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+

Other name(s): glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]

Systematic name: L-glutamate:NAD(P)+ oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-12-3

References:

1. Olson, J.A. and Anfinsen, C.B. The crystallization and characterization of L-glutamic acid dehydrogenase. J. Biol. Chem. 197 (1952) 67-79.

2. Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F. Glutamate dehydrogenases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 11, Academic Press, New York, 1975, p. 293-367.

3. Strecker, H.J. Glutamic dehydrogenase. Arch. Biochem. Biophys. 46 (1953) 128-140.

[EC 1.4.1.3 created 1961]

EC 1.4.1.4

Accepted name: glutamate dehydrogenase (NADP+)

Reaction: L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+

Other name(s): glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP)

Systematic name: L-glutamate:NADP+ oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-11-2

References:

1. Coulton, J.W. and Kapoor, M. Purification and some properties of the glutamate dehydrogenase of Salmonella typhimurium. Can. J. Microbiol. 19 (1973) 427-438. [PMID: 4144743]

2. Grisolia, S., Quijada, C.L. and Fernandez, M. Glutamate dehydrogenase from yeast and from animal tissues. Biochim. Biophys. Acta 81 (1964) 61-70.

3. Shiio, I. and Ozaki, H. Regulation of nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase from Brevibacterium flavum, a glutamate-producing bacterium. J. Biochem. (Tokyo) 68 (1970) 633-647. [PMID: 4394939]

4. Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F. Glutamate dehydrogenases. In: Boyer, P.D. (Ed.) T he Enzymes, 3rd ed., vol. 11, Academic Press, New York, 1975, p. 293-367.

[EC 1.4.1.4 created 1961]

EC 1.4.1.5

Accepted name: L-amino-acid dehydrogenase

Reaction: an L-amino acid + H2O + NAD+ = a 2-oxo carboxylate + NH3 + NADH + H+

Systematic name: L-amino-acid:NAD+ oxidoreductase (deaminating)

Comments: Acts on aliphatic amino acids.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-13-4

References:

1. Nisman, B. and Mager, J. Diphosphopyridine nucleotide and phosphate requirement for oxidation of amino-acids by cell-free extracts of obligate anaerobes. Nature (Lond.) 169 (1952) 243-244.

[EC 1.4.1.5 created 1961]

[EC 1.4.1.6 Deleted entry: now included with EC 1.4.4.1 D-proline reductase (dithiol) (EC 1.4.1.6 created 1961, deleted 1982)]

EC 1.4.1.7

Accepted name: serine 2-dehydrogenase

Reaction: L-serine + H2O + NAD+ = 3-hydroxypyruvate + NH3 + NADH + H+

Other name(s): L-serine:NAD oxidoreductase (deaminating); serine dehydrogenase

Systematic name: L-serine:NAD+ 2-oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9038-55-5

References:

1. Kretovich, V.L. and Stepanovich, K.M. [The enzyme catalyzing the reductive amination of oxypyruvate.] (in Russian) Izv. Akad. Nauk SSSR Ser. Biol. No. 2 (1966) 295-300. [PMID: 5972761]

[EC 1.4.1.7 created 1972, modified 2003]

EC 1.4.1.8

Accepted name: valine dehydrogenase (NADP+)

Reaction: L-valine + H2O + NADP+ = 3-methyl-2-oxobutanoate + NH3 + NADPH + H+

Other name(s): valine dehydrogenase (nicotinanide adenine dinucleotide phosphate); valine dehydrogenase (NADP)

Systematic name: L-valine:NADP+ oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-39-3

References:

1. Kagan, Z.S., Kretovich, V.L. and Polyakov, V.A. Biosynthesis of valine by reductive amination of its keto analogue in plants. Enzymologia 30 (1966) 343-366. [PMID: 6005410]

2. Kagan, Z.S., Polyakov, V.A. and Kretovich, V.L. Soluble valine dehydrogenase from roots of plant seedings. Biochemistry (Moscow) 33 (1968) 74-84. [PMID: 4385962]

3. Kagan, Z.S., Polyakov, V.A. and Kretovich, V.L. Purification and properties of valine dehydrogenase. Biochemistry (Moscow) 34 (1969) 47-51. [PMID: 4389825]

[EC 1.4.1.8 created 1972]

EC 1.4.1.9

Accepted name: leucine dehydrogenase

Reaction: L-leucine + H2O + NAD+ = 4-methyl-2-oxopentanoate + NH3 + NADH + H+

Other name(s): L-leucine dehydrogenase; L-leucine:NAD+ oxidoreductase, deaminating; LeuDH

Systematic name: L-leucine:NAD+ oxidoreductase (deaminating)

Comments: Also acts on isoleucine, valine, norvaline and norleucine.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9082-71-7

References:

1. Sanwal, B.D. and Zink, M.W. L-Leucine dehydrogenase of Bacillus cereus. Arch. Biochem. Biophys. 94 (1961) 430-435.

2. Zink, M.W. and Sanwal, B.D. The distribution and substrate specificity of L-leucine dehydrogenase. Arch. Biochem. Biophys. 99 (1962) 72-77.

[EC 1.4.1.9 created 1972]

EC 1.4.1.10

Accepted name: glycine dehydrogenase

Reaction: glycine + H2O + NAD+ = glyoxylate + NH3 + NADH + H+

Systematic name: glycine:NAD+ oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37255-40-6

References:

1. Goldman, D.S. and Wagner, M.J. Enzyme systems in the mycobacteria. XIII. Glycine dehydrogenase and the glyoxylic acid cycle. Biochim. Biophys. Acta 65 (1962) 297-306.

[EC 1.4.1.10 created 1972]

EC 1.4.1.11

Accepted name: L-erythro-3,5-diaminohexanoate dehydrogenase

Reaction: L-erythro-3,5-diaminohexanoate + H2O + NAD+ = (S)-5-amino-3-oxohexanoate + NH3 + NADH + H+

For diagram of reaction click here.

Other name(s): L-3,5-diaminohexanoate dehydrogenase

Systematic name: L-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37377-90-5

References:

1. Baker, J.J., Jeng, I. and Barker, H.A. Purification and properties of L-erythro-3,5-diaminohexanoate dehydrogenase from a lysine-fermenting Clostridium. J. Biol. Chem. 247 (1972) 7724-7734. [PMID: 4344229]

[EC 1.4.1.11 created 1976]

EC 1.4.1.12

Accepted name: 2,4-diaminopentanoate dehydrogenase

Reaction: 2,4-diaminopentanoate + H2O + NAD(P)+ = 2-amino-4-oxopentanoate + NH3 + NAD(P)H + H+

Other name(s): 2,4-diaminopentanoic acid C4 dehydrogenase

Systematic name: 2,4-diaminopentanoate:NAD(P)+ oxidoreductase (deaminating)

Comments: Also acts, more slowly, on 2,5-diaminohexanoate forming 2-amino-5-oxohexanoate, which then cyclizes non-enzymically to 1-pyrroline-2-methyl-5-carboxylate.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 39346-26-4

References:

1. Somack, R. and Costilow, R.N. 2,4-Diaminopentanoic acid C4 dehydrogenase. Purification and properties of the protein. J. Biol. Chem. 248 (1973) 385-388. [PMID: 4684685]

2. Stadtman, T.C. Lysine metabolism by clostridia. XIIB 2,4-Diaminohexanoate dehydrogenase (2,4-diaminopentanoate dehydrogenase). Adv. Enzymol. Relat. Areas Mol. Biol. 38 (1973) 441-445.

3. Tsuda, Y. and Friedmann, H.C. Ornithine metabolism by Clostridium sticklandii. Oxidation of ornithine to 2-amino-4-ketopentanoic acid via 2,4-diaminopentanoic acid; participation of B12 coenzyme, pyridoxal phosphate, and pyridine nucleotide. J. Biol. Chem. 245 (1970) 5914-5926. [PMID: 4394942]

[EC 1.4.1.12 created 1976]

EC 1.4.1.13

Accepted name: glutamate synthase (NADPH)

Reaction: 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+ (overall reaction)
(1a) L-glutamate + NH3 = L-glutamine + H2O
(1b) L-glutamate + NADP+ + H2O = NH3 + 2-oxoglutarate + NADPH + H+

Other name(s): glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase; L-glutamate synthase; L-glutamate synthetase; glutamate synthetase (NADP); NADPH-dependent glutamate synthase; glutamine-ketoglutaric aminotransferase; NADPH-glutamate synthase; NADPH-linked glutamate synthase; glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP); L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing; GOGAT

Systematic name: L-glutamate:NADP+ oxidoreductase (transaminating)

Comments: Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the opposite direction. The protein is composed of two subunits, α and β. The α subunit is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The β subunit transfers electrons to the cosubstrate. The NH3 is channeled through a 31 Å channel in the active protein. In the absence of the β subunit, coupling between the two domains of the α subunit is compromised and some ammonium can be produced. In the intact αβ complex, ammonia production only takes place as part of the overall reaction.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37213-53-9

References:

1. Miller, R.E. and Stadtman, E.R. Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein. J. Biol. Chem. 247 (1972) 7407-7419. [PMID: 4565085]

2. Tempest, D.W., Meers, J.L. and Brown, C.M. Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route. Biochem. J. 117 (1970) 405-407. [PMID: 5420057]

3. Vanoni, M.A. and Curti, B. Glutamate synthase: a complex iron-sulfur flavoprotein. Cell. Mol. Life Sci. 55 (1999) 617-638. [PMID: 10357231]

4. Ravasio, S., Curti, B. and Vanoni, M.A. Determination of the midpoint potential of the FAD and FMN flavin cofactors and of the 3Fe-4S cluster of glutamate synthase. Biochemistry 40 (2001) 5533-5541. [PMID: 11331018]

[EC 1.4.1.13 created 1972 as EC 2.6.1.53, transferred 1976 to EC 1.4.1.13, modified 2001, modified 2012]

EC 1.4.1.14

Accepted name: glutamate synthase (NADH)

Reaction: 2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+

Other name(s): glutamate (reduced nicotinamide adenine dinucleotide) synthase; NADH: GOGAT; L-glutamate synthase (NADH); L-glutamate synthetase; NADH-glutamate synthase; NADH-dependent glutamate synthase; glutamate synthase (NADH2)

Systematic name: L-glutamate:NAD+ oxidoreductase (transaminating)

Comments: A flavoprotein (FMN).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 65589-88-0

References:

1. Boland, M.J. and Benny, A.G. Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules. Eur. J. Biochem. 79 (1977) 355-362. [PMID: 21790]

[EC 1.4.1.14 created 1978]

EC 1.4.1.15

Accepted name: lysine dehydrogenase

Reaction: L-lysine + NAD+ = 1,2-didehydropiperidine-2-carboxylate + NH3 + NADH + H+

Systematic name: L-lysine:NAD+ oxidoreductase (deaminating, cyclizing)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 68073-29-0

References:

1. Burgi, W., Richterich, R. and Colombo, J.P. L-Lysine dehydrogenase deficiency in a patient with congenital lysine intolerance. Nature (Lond.) 211 (1966) 854-855. [PMID: 4291003]

[EC 1.4.1.15 created 1978]

EC 1.4.1.16

Accepted name: diaminopimelate dehydrogenase

Reaction: meso-2,6-diaminoheptanedioate + H2O + NADP+ = L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+

Other name(s): meso-α,ε-diaminopimelate dehydrogenase; meso-diaminopimelate dehydrogenase

Systematic name: meso-2,6-diaminoheptanedioate:NADP+ oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 60894-21-5

References:

1. Misono, H., Togawa, H., Yamamoto, T. and Soda, K. Occurrence of meso-α,ε-diaminopimelate dehydrogenase in Bacillus sphaericus. Biochem. Biophys. Res. Commun. 72 (1976) 89-93. [PMID: 10904]

2. Misono, H., Togawa, H., Yamamoto, T. and Soda, K. meso-α,ε-Diaminopimelate D-dehydrogenase: distribution and the reaction product. J. Bacteriol. 137 (1979) 22-27. [PMID: 762012]

[EC 1.4.1.16 created 1981]

EC 1.4.1.17

Accepted name: N-methylalanine dehydrogenase

Reaction: N-methyl-L-alanine + H2O + NADP+ = pyruvate + methylamine + NADPH + H+

Systematic name: N-methyl-L-alanine:NADP+ oxidoreductase (demethylating, deaminating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 56379-51-2

References:

1. Lin, M.C.M. and Wagner, C. Purification and characterization of N-methylalanine dehydrogenase. J. Biol. Chem. 250 (1975) 3746-3751. [PMID: 236301]

[EC 1.4.1.17 created 1984]

EC 1.4.1.18

Accepted name: lysine 6-dehydrogenase

Reaction: L-lysine + NAD+ = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NADH + H+ + NH3 (overall reaction)
(1a) L-lysine + NAD+ + H2O = (S)-2-aminoadipate 6-semialdehyde + NADH + H+ + NH3
(1b) (S)-2-aminoadipate 6-semialdehyde = (S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + H2O (spontaneous)

For diagram click here, another example.

Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate

Other name(s): L-lysine ε-dehydrogenase; L-lysine 6-dehydrogenase; LysDH

Systematic name: L-lysine:NAD+ 6-oxidoreductase (deaminating)

Comments: The enzyme is highly specific for L-lysine as substrate, although (S)-(β-aminoethyl)-L-cysteine can act as a substrate, but more slowly. While the enzyme from Agrobacterium tumefaciens can use only NAD+, that from the thermophilic bacterium Geobacillus stearothermophilus can also use NADP+, but more slowly [1,4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 89400-30-6

References:

1. Misono, H. and Nagasaki, S. Occurrence of L-lysine ε-dehydrogenase in Agrobacterium tumefaciens. J. Bacteriol. 150 (1982) 398-401. [PMID: 6801024]

2. Misono, H., Uehigashi, H., Morimoto, E. and Nagasaki, S. Purification and properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens. Agric. Biol. Chem. 49 (1985) 2253-2255.

3. Misono, H., Hashimoto, H., Uehigashi, H., Nagata, S. and Nagasaki, S. Properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens. J. Biochem. (Tokyo) 105 (1989) 1002-1008. [PMID: 2768207]

4. Heydari, M., Ohshima, T., Nunoura-Kominato, N. and Sakuraba, H. Highly stable L-lysine 6-dehydrogenase from the thermophile Geobacillus stearothermophilus isolated from a Japanese hot spring: characterization, gene cloning and sequencing, and expression. Appl. Environ. Microbiol. 70 (2004) 937-942. [PMID: 14766574]

[EC 1.4.1.18 created 1989, modified 2006]

EC 1.4.1.19

Accepted name: tryptophan dehydrogenase

Reaction: L-tryptophan + NAD(P)+ + H2O = (indol-3-yl)pyruvate + NH3 + NAD(P)H + H+

Other name(s): NAD(P)+-L-tryptophan dehydrogenase; L-tryptophan dehydrogenase; L-Trp-dehydrogenase; TDH

Systematic name: L-tryptophan:NAD(P)+ oxidoreductase (deaminating)

Comments: Activated by Ca2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 94047-13-9

References:

1. Vackova, K., Mehta, A. and Kutacek, M. Tryptophan aminotransferase and tryptophan dehydrogenase - activities in some cell compartments of spinach leaves - the effect of calcium-ions on tryptophan dehydrogenase. Biol. Plant. 27 (1985) 154-158.

[EC 1.4.1.19 created 1989]

EC 1.4.1.20

Accepted name: phenylalanine dehydrogenase

Reaction: L-phenylalanine + H2O + NAD+ = phenylpyruvate + NH3 + NADH + H+

Other name(s): L-phenylalanine dehydrogenase; PHD

Systematic name: L-phenylalanine:NAD+ oxidoreductase (deaminating)

Comments: The enzymes from Bacillus badius and Sporosarcina ureae are highly specific for L-phenylalanine; that from Bacillus sphaericus also acts on L-tyrosine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 69403-12-9

References:

1. Asano, Y., Nakazawa, A. and Endo, K. Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization. J. Biol. Chem. 262 (1987) 10346-10354. [PMID: 3112142]

2. Asano, Y., Nakazawa, A., Endo, K., Hibino, Y., Ohmori, M., Numao, N. and Kondo, K. Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning. Eur. J. Biochem. 168 (1987) 153-159. [PMID: 3311741]

[EC 1.4.1.20 created 1989]

EC 1.4.1.21

Accepted name: aspartate dehydrogenase

Reaction: L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+

Other name(s): NAD-dependent aspartate dehydrogenase; NADH2-dependent aspartate dehydrogenase; NADP+-dependent aspartate dehydrogenase

Systematic name: L-aspartate:NAD(P)+ oxidoreductase (deaminating)

Comments: The enzyme is strictly specific for L-aspartate as substrate. Catalyses the first step in NAD biosynthesis from aspartate. The enzyme has a higher affinity for NAD+ than NADP+ [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37278-97-0

References:

1. Yang, Z., Savchenko, A., Yakunin, A., Zhang, R., Edwards, A., Arrowsmith, C. and Tong, L. Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643. J. Biol. Chem. 278 (2003) 8804-8808. [PMID: 12496312]

2. Okamura, T., Noda, H., Fukuda, S. and Ohsugi, M. Aspartate dehydrogenase in vitamin B12-producing Klebsiella pneumoniae IFO 13541. J. Nutr. Sci. Vitaminol. (Tokyo) 44 (1998) 483-490. [PMID: 9819709]

3. Kretovich, W.L., Kariakina, T.I., Weinova, M.K., Sidelnikova, L.I. and Kazakova, O.W. The synthesis of aspartic acid in Rhizobium lupini bacteroids. Plant Soil 61 (1981) 145-156.

[EC 1.4.1.21 created 2005]

[EC 1.4.1.22 Deleted entry: ornithine cyclodeaminase. It was pointed out during the public-review process that there is no overall consumption of NAD+ during the reaction. As a result, transfer of the enzyme from EC 4.3.1.12 was not necessary and EC 1.4.1.22 was withdrawn before being made official. (EC 1.4.1.22 created 2006, deleted 2006)] EC 1.4.1.23

Accepted name: valine dehydrogenase (NAD+)

Reaction: L-valine + H2O + NAD+ = 3-methyl-2-oxobutanoate + NH3 + NADH + H+

Systematic name: L-valine:NAD+ oxidoreductase (deaminating)

Comments: The enzyme from Streptomyces spp. has no activity with NADP+ [cf. EC 1.4.1.8, valine dehydrogenase (NADP+)].

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

References:

1. Vancurová, I., Vancura, A., Volc, J., Neuzil, J., Flieger, M., Basarová, G. and Behal, V. Isolation and characterization of valine dehydrogenase from Streptomyces aureofaciens. J. Bacteriol. 170 (1988) 5192-5196. [PMID: 3182727]

2. Navarrete, R.M., Vara, J.A. and Hutchinson, C.R. Purification of an inducible L-valine dehydrogenase of Streptomyces coelicolor A3(2). J. Gen. Microbiol. 136 (1990) 273-281. [PMID: 2324704]

[EC 1.4.1.23 created 2012]

EC 1.4.1.24

Accepted name: 3-dehydroquinate synthase II

Reaction: 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+ = 3-dehydroquinate + NH3 + NADP+ + H+

For diagram of reaction click here.

Glossary: 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate = 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate

Other name(s): DHQ synthase II; MJ1249 (gene name); aroB' (gene name)

Systematic name: 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate:NAD+ oxidoreductase (deaminating)

Comments: The enzyme, which was isolated from the archaeon Methanocaldococcus jannaschii, plays a key role in an alternative pathway for the biosynthesis of 3-dehydroquinate (DHQ), an intermediate of the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme catalyses a two-step reaction - an oxidative deamination, followed by cyclization.

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

References:

1. White, R.H. L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii. Biochemistry 43 (2004) 7618-7627. [PMID: 15182204]

[EC 1.4.1.24 created 2012]


EC 1.4.2 With a cytochrome as acceptor

EC 1.4.2.1

Accepted name: glycine dehydrogenase (cytochrome)

Reaction: glycine + H2O + 2 ferricytochrome c = glyoxylate + NH3 + 2 ferrocytochrome c + 2 H+

Other name(s): glycine—cytochrome c reductase

Systematic name: glycine:ferricytochrome-c oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9075-55-2

References:

1. Sanders, H.K., Becker, G.E. and Nason, A. Glycine-cytochrome c reductase from Nitrobacter agilis. J. Biol. Chem. 247 (1972) 2015-2025. [PMID: 5016640]

[EC 1.4.2.1 created 1976]


EC 1.4.3 With a oxygen as acceptor

Contents

EC 1.4.3.1 D-aspartate oxidase
EC 1.4.3.2 L-amino-acid oxidase
EC 1.4.3.3 D-amino-acid oxidase
EC 1.4.3.4 amine oxidase
EC 1.4.3.5 pyridoxal 5'-phosphate synthase
EC 1.4.3.6 deleted now EC 1.4.3.21 and EC 1.4.3.22
EC 1.4.3.7 D-glutamate oxidase
EC 1.4.3.8 ethanolamine oxidase
EC 1.4.3.9 deleted, included in EC 1.4.3.4
EC 1.4.3.10 putrescine oxidase
EC 1.4.3.11 L-glutamate oxidase
EC 1.4.3.12 cyclohexylamine oxidase
EC 1.4.3.13 protein-lysine 6-oxidase
EC 1.4.3.14 L-lysine oxidase
EC 1.4.3.15 D-glutamate(D-aspartate) oxidase
EC 1.4.3.16 L-aspartate oxidase
EC 1.4.3.17 now EC 1.3.3.10
EC 1.4.3.18 deleted, not approved
EC 1.4.3.19 glycine oxidase
EC 1.4.3.20 L-lysine 6-oxidase
EC 1.4.3.21 primary-amine oxidase
EC 1.4.3.22 diamine oxidase
EC 1.4.3.23 7-chloro-L-tryptophan oxidase
EC 1.4.3.24 pseudooxynicotine oxidase


EC 1.4.3.1

Accepted name: D-aspartate oxidase

Reaction: D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2

Other name(s): aspartic oxidase; D-aspartic oxidase

Systematic name: D-aspartate:oxygen oxidoreductase (deaminating)

Comments: A flavoprotein (FAD).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-20-3

References:

1. Dixon, M. and Kenworthy, P. D-Aspartate oxidase of kidney. Biochim. Biophys. Acta 146 (1967) 54-76. [PMID: 6060479]

2. Still, J.L., Buell, M.V., Knox, W.E. and Green, D.E. Studies on the cyclophorase system. VII. D-Aspartic oxidase. J. Biol. Chem. 179 (1949) 831-837.

3. Still, J.L. and Sperling, E.On the prosthetic group of the D-aspartic oxidase. J. Biol. Chem. 182 (1950) 585-589.

[EC 1.4.3.1 created 1961]

EC 1.4.3.2

Accepted name: L-amino-acid oxidase

Reaction: an L-amino acid + H2O + O2 = a 2-oxo carboxylate + NH3 + H2O2

Other name(s): ophio-amino-acid oxidase

Systematic name: L-amino-acid:oxygen oxidoreductase (deaminating)

Comments: A flavoprotein (FAD).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9000-89-9

References:

1. Meister, A. and Wellner, D. Flavoprotein amino acid oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 609-648.

2. Wellner, D. and Meister, A. Crystalline L-amino acid oxidase of Crotalus adamanteus. J. Biol. Chem. 235 (1960) 2013-2018.

[EC 1.4.3.2 created 1961]

EC 1.4.3.3

Accepted name: D-amino-acid oxidase

Reaction: a D-amino acid + H2O + O2 = a 2-oxo carboxylate + NH3 + H2O2

Other name(s): ophio-amino-acid oxidase; L-amino acid:O2 oxidoreductase; new yellow enzyme

Systematic name: D-amino-acid:oxygen oxidoreductase (deaminating)

Comments: A flavoprotein (FAD). Wide specificity for D-amino acids. Also acts on glycine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9000-88-8

References:

1. Dixon, M. and Kleppe, K. D-Amino acid oxidase. I. Dissociation and recombination of the haloenzyme. Biochim. Biophys. Acta 96 (1965) 357-367.

2. Dixon, M. and Kleppe, K. D-Amino acid oxidase. II. Specificity, competitive inhibition and reaction sequence. Biochim. Biophys. Acta 96 (1965) 368-382.

3. Dixon, M. and Kleppe, K. D-Amino acid oxidase. III. Effect of pH. Biochim. Biophys. Acta 96 (1965) 383-389.

4. Massey, V., Palmer, G. and Bennett, R. The purification and some properties of D-amino acid oxidase. Biochim. Biophys. Acta 48 (1961) 1-9.

5. Meister, A. and Wellner, D. Flavoprotein amino acid oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 609-648.

[EC 1.4.3.3 created 1961]

EC 1.4.3.4

Accepted name: monoamine oxidase

Reaction: RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2

Other name(s): adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine:oxygen oxidoreductase (deaminating) (flavin-containing); epinephrine oxidase; MAO; MAO A; MAO B; MAO-A; MAO-B; monoamine oxidase A; monoamine oxidase B; monoamine:O2 oxidoreductase (deaminating); polyamine oxidase (ambiguous); serotonin deaminase; spermidine oxidase (ambiguous); spermine oxidase (ambiguous); tyraminase; tyramine oxidase

Systematic name: amine:oxygen oxidoreductase (deaminating)

Comments: A mitochondrial outer-membrane flavoprotein (FAD) that catalyses the oxidative deamination of neurotransmitters and biogenic amines [3]. Acts on primary amines, and also on some secondary and tertiary amines. It differs from EC 1.4.3.21, primary-amine oxidase as it can oxidize secondary and tertiary amines but not methylamine. This enzyme is inhibited by acetylenic compounds such as chlorgyline, 1-deprenyl and pargyline but, unlike EC 1.4.3.21 and EC 1.4.3.22 (diamine oxidase), it is not inhibited by semicarbazide.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD , CAS registry number: 9001-66-5

References:

1. Blaschko, H. Amine oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 337-351.

2. Dostert, P.L., Strolin Benedetti, M. and Tipton, K.F. Interactions of monoamine oxidase with substrates and inhibitors. Med. Res. Rev. 9 (1989) 45-89. [PMID: 2644497]

3. Edmondson, D.E., Mattevi, A., Binda, C., Li, M. and Hubálek, F. Structure and mechanism of monoamine oxidase. Curr. Med. Chem. 11 (2004) 1983-1993. [PMID: 15279562]

4. Shih, J.C. and Chen, K. Regulation of MAO-A and MAO-B gene expression. Curr. Med. Chem. 11 (2004) 1995-2005. [PMID: 15279563]

5. Tipton, K.F., Boyce, S., O'Sullivan, J., Davey, G.P. and Healy, J. Monoamine oxidases: certainties and uncertainties. Curr. Med. Chem. 11 (2004) 1965-1982. [PMID: 15279561]

6. De Colibus, L., Li, M., Binda, C., Lustig, A., Edmondson, D.E. and Mattevi, A. Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc. Natl. Acad. Sci. USA 102 (2005) 12684-12689. [PMID: 16129825]

7. Youdim, M.B., Edmondson, D. and Tipton, K.F. The therapeutic potential of monoamine oxidase inhibitors. Nat. Rev. Neurosci. 7 (2006) 295-309. [PMID: 16552415]

8. Youdim, M.B. and Bakhle, Y.S. Monoamine oxidase: isoforms and inhibitors in Parkinson's disease and depressive illness. Br. J. Pharmacol. 147 Suppl. 1 (2006) S287-S296. [PMID: 16402116]

[EC 1.4.3.4 created 1961, modified 1983 (EC 1.4.3.9 created 1972, incorporated 1984), modified 2008]

EC 1.4.3.5

Accepted name: pyridoxal 5'-phosphate synthase

Reaction: (1) pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2
(2) pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2

For diagram, click here

Other name(s): pyridoxamine 5'-phosphate oxidase; pyridoxamine phosphate oxidase; pyridoxine (pyridoxamine)phosphate oxidase; pyridoxine (pyridoxamine) 5'-phosphate oxidase; pyridoxaminephosphate oxidase (EC 1.4.3.5: deaminating); PMP oxidase; pyridoxol-5'-phosphate:oxygen oxidoreductase (deaminating) (incorrect); pyridoxamine-phosphate oxidase; PdxH

Systematic name: pyridoxamine-5'-phosphate:oxygen oxidoreductase (deaminating)

Comments: A flavoprotein (FMN). In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). N4'-Substituted pyridoxamine derivatives are also oxidized in reaction (1) to form pyridoxal 5'-phosphate and the corresponding primary amine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-21-4

References:

1. Choi, J.-D., Bowers-Komro, D.M., Davis, M.D., Edmondson, D.E. and McCormick, D.B. Kinetic properties of pyridoxamine (pyridoxine)-5'-phosphate oxidase from rabbit liver. J. Biol. Chem. 258 (1983) 840-845. [PMID: 6822512]

2. Wada, H. and Snell, E.E. The enzymatic oxidation of pyridoxine and pyridoxamine phosphates. J. Biol. Chem. 236 (1961) 2089-2095. [PMID: 13782387]

3. Notheis, C., Drewke, C. and Leistner, E. Purification and characterization of the pyridoxol-5'-phosphate:oxygen oxidoreductase (deaminating) from Escherichia coli. Biochim. Biophys. Acta 1247 (1995) 265-271. [PMID: 7696318]

4. Laber, B., Maurer, W., Scharf, S., Stepusin, K. and Schmidt, F.S. Vitamin B6 biosynthesis: formation of pyridoxine 5'-phosphate from 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by PdxA and PdxJ protein. FEBS Lett. 449 (1999) 45-48. [PMID: 10225425]

5. Musayev, F.N., Di Salvo, M.L., Ko, T.P., Schirch, V. and Safo, M.K. Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase. Protein Sci. 12 (2003) 1455-1463. [PMID: 12824491]

6. Safo, M.K., Musayev, F.N. and Schirch, V. Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in a tetragonal crystal form: insights into the mechanistic pathway of the enzyme. Acta Crystallogr. D Biol. Crystallogr. 61 (2005) 599-604. [PMID: 15858270]

7. Zhang, Z. and McCormick, D.B. Uptake and metabolism of N-(4'-pyridoxyl)amines by isolated rat liver cells. Arch. Biochem. Biophys. 294 (1992) 394-397. [PMID: 1567194]

[EC 1.4.3.5 created 1961, modified 2006]

[EC 1.4.3.6 Deleted entry: amine oxidase (copper-containing). This was classified on the basis of cofactor content rather than reaction catalysed and is now known to contain two distinct enzyme activities. It has been replaced by two enzymes, EC 1.4.3.21 (primary-amine oxidase) and EC 1.4.3.22 (diamine oxidase) (EC 1.4.3.6 created 1961, modified 1983, modified 1989, deleted 2008)]

EC 1.4.3.7

Accepted name: D-glutamate oxidase

Reaction: D-glutamate + H2O + O2 = 2-oxoglutarate + NH3 + H2O2

Other name(s): D-glutamic oxidase; D-glutamic acid oxidase

Systematic name: D-glutamate:oxygen oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-41-7

References:

1. Rocca, E. and Ghiretti, F. Purification and properties of D-glutamic acid oxidase from Octopus vulgaris Lam. Arch. Biochem. Biophys. 77 (1958) 336-349.

2. Urich, K. [D-Glutamate oxidase from the antennal gland of the crayfish Oronectes limosus: purification and characterization]. Z. Naturforsch. B 23 (1968) 1508-1511. [PMID: 4387700]

[EC 1.4.3.7 created 1972]

EC 1.4.3.8

Accepted name: ethanolamine oxidase

Reaction: ethanolamine + H2O + O2 = glycolaldehyde + NH3 + H2O2

Systematic name: ethanolamine:oxygen oxidoreductase (deaminating)

Comments: A cobamide-protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9013-00-7

References:

1. Narrod, S.A. and Jakoby, W.B. Metabolism of ethanolamine. An ethanolamine oxidase. J. Biol. Chem. 239 (1964) 2189-2193.

[EC 1.4.3.8 created 1972]

[EC 1.4.3.9 Deleted entry: tyramine oxidase. Now included with EC 1.4.3.4 amine oxidase (flavin-containing) (EC 1.4.3.9 created 1972, deleted 1984)]

EC 1.4.3.10

Accepted name: putrescine oxidase

Reaction: putrescine + O2 + H2O = 4-aminobutanal + NH3 + H2O2

Systematic name: putrescine:oxygen oxidoreductase (deaminating)

Comments: A flavoprotein (FAD). 4-Aminobutanal condenses non-enzymically to 1-pyrroline.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9076-87-3

References:

1. DeSa, R.J. Putrescine oxidase from Micrococcus rubens. Purification and properties of the enzyme. J. Biol. Chem. 247 (1972) 5527-5534. [PMID: 4341347]

2. Yamada, H. Putrescine oxidase (Micrococcus rubens). Methods Enzymol. 17B (1971) 726-730.

[EC 1.4.3.10 created 1976]

EC 1.4.3.11

Accepted name: L-glutamate oxidase

Reaction: L-glutamate + O2 + H2O = 2-oxoglutarate + NH3 + H2O2

Other name(s): glutamate (acceptor) dehydrogenase; glutamate oxidase; glutamic acid oxidase; glutamic dehydrogenase (acceptor); L-glutamic acid oxidase

Systematic name: L-glutamate:oxygen oxidoreductase (deaminating)

Comments: A flavoprotein (FAD). The enzyme from Azotobacter previously listed under this number, which did not produce H2O2, was a crude cell-free extract that probably contained catalase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 39346-34-4

References:

1. Kusakabe, H., Midorikawa, Y., Fujishima, T., Kuninaka, A. and Yoshino, H. Purification and properties of a new enzyme, L-glutamate oxidase, from Streptomyces sp X-119-6 grown on wheat bran. Agric. Biol. Chem. 47 (1983) 1323-1328.

[EC 1.4.3.11 created 1976, modified 1989]

EC 1.4.3.12

Accepted name: cyclohexylamine oxidase

Reaction: cyclohexylamine + O2 + H2O = cyclohexanone + NH3 + H2O2

Systematic name: cyclohexylamine:oxygen oxidoreductase (deaminating)

Comments: A flavoprotein (FAD). Some other cyclic amines can act instead of cyclohexylamine, but not simple aliphatic and aromatic amides.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD , CAS registry number: 63116-97-2

References:

1. Tokieda, T., Niimura, T., Takamura, F. and Yamaha, T. Purification and some properties of cyclohexylamine oxidase from a Pseudomonas sp. J. Biochem. (Tokyo) 81 (1977) 851-858. [PMID: 18451]

[EC 1.4.3.12 created 1978]

EC 1.4.3.13

Accepted name: protein-lysine 6-oxidase

Reaction: peptidyl-L-lysyl-peptide + O2 + H2O = peptidyl-allysyl-peptide + NH3 + H2O2

Other name(s): lysyl oxidase

Systematic name: protein-L-lysine:oxygen 6-oxidoreductase (deaminating)

Comments: Also acts on protein 5-hydroxylysine. This enzyme catalyses the final known enzymic step required for collagen and elastin cross-linking in the biosynthesis of normal mature extracellular matrices [4]. These reactions play an important role for the development, elasticity and extensibility of connective tissue. The enzyme is also active on free amines, such as cadaverine or benzylamine [4,5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 99676-44-5

References:

1. Harris, E.D., Gonnerman, W.A., Savage, J.E. and O'Dell, B.L. Connective tissue amine oxidase. II. Purification and partial characterization of lysyl oxidase from chick aorta. Biochim. Biophys. Acta 341 (1974) 332-344. [PMID: 4838158]

2. Rayton, J.K. and Harris, E.D. Induction of lysyl oxidase with copper. Properties of an in vitro system. J. Biol. Chem. 254 (1979) 621-626. [PMID: 33171]

3. Stassen, F.L.H. Properties of highly purified lysyl oxidase from embryonic chick cartilage. Biochim. Biophys. Acta 438 (1976) 49-60. [PMID: 7318]

4. Palamakumbura, A.H. and Trackman, P.C. A fluorometric assay for detection of lysyl oxidase enzyme activity in biological samples. Anal. Biochem. 300 (2002) 245-251. [PMID: 11779117]

5. Kagan, H.M., Williams, M.A., Williamson, P.R. and Anderson, J.M. Influence of sequence and charge on the specificity of lysyl oxidase toward protein and synthetic peptide substrates. J. Biol. Chem. 259 (1984) 11203-11207. [PMID: 6147351]

[EC 1.4.3.13 created 1980, modified 1983]

EC 1.4.3.14

Accepted name: L-lysine oxidase

Reaction: L-lysine + O2 + H2O = 6-amino-2-oxohexanoate + NH3 + H2O2

Other name(s): L-lysine α-oxidase; L-lysyl-α-oxidase

Systematic name: L-lysine:oxygen 2-oxidoreductase (deaminating)

Comments: Also acts, more slowly, on L-ornithine, L-phenylalanine, L-arginine and L-histidine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 70132-14-8

References:

1. Kusakabe, H., Kodama, K., Kuninaka, A., Yoshino, H., Misono, H. and Soda, K. A new antitumor enzyme, L-lysine α-oxidase from Trichoderma viride. Purification and enzymological properties. J. Biol. Chem. 255 (1980) 976-981. [PMID: 6101334]

[EC 1.4.3.14 created 1981]

EC 1.4.3.15

Accepted name: D-glutamate(D-aspartate) oxidase

Reaction: (1) D-glutamate + H2O + O2 = 2-oxoglutarate + NH3 + H2O2
(2) D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2

Other name(s): D-glutamic-aspartic oxidase; D-monoaminodicarboxylic acid oxidase

Systematic name: D-glutamate(D-aspartate):oxygen oxidoreductase (deaminating)

Comments: A flavoprotein (FAD). D-Glutamate and D-aspartate are oxidized at the same rate. Other D-monoaminodicarboxylates, and other D- and L-amino acids, are not oxidized. cf. EC 1.4.3.7, D-glutamate oxidase and EC 1.4.3.1, D-aspartate oxidase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-20-3

References:

1. Mizushima, S. Purified D-glutamic-aspartic oxidase of Aspergillus ustus. J. Gen. Appl. Microbiol. 3 (1957) 233-239.

[EC 1.4.3.15 created 1983, modified 2012]

EC 1.4.3.16

Accepted name: L-aspartate oxidase

Reaction: L-aspartate + O2 = iminosuccinate + H2O2

For diagram of reaction click here.

Other name(s): NadB; Laspo; AO

Systematic name: L-aspartate:oxygen oxidoreductase (deaminating)

Comments: A flavoprotein (FAD). L-Aspartate oxidase catalyses the first step in the de novo biosynthesis of NAD+ in some bacteria. O2 can be replaced by fumarate as electron acceptor, yielding succinate [5]. The ability of the enzyme to use both O2 and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions [5]. Iminosuccinate can either be hydrolysed to form oxaloacetate and NH3 or can be used by EC 2.5.1.72, quinolinate synthase, in the production of quinolinate. The enzyme is a member of the succinate dehydrogenase/fumarate-reductase family of enzymes [5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 69106-47-4

References:

1. Nasu, S., Wicks, F.D. and Gholson, R.K. L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase. J. Biol. Chem. 257 (1982) 626-632. [PMID: 7033218]

2. Mortarino, M., Negri, A., Tedeschi, G., Simonic, T., Duga, S., Gassen, H.G. and Ronchi, S. L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition. Eur. J. Biochem. 239 (1996) 418-426. [PMID: 8706749]

3. Tedeschi, G., Negri, A., Mortarino, M., Ceciliani, F., Simonic, T., Faotto, L. and Ronchi, S. L-Aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate: fumarate oxidoreductase activity. Eur. J. Biochem. 239 (1996) 427-433. [PMID: 8706750]

4. Mattevi, A., Tedeschi, G., Bacchella, L., Coda, A., Negri, A. and Ronchi, S. Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. Structure 7 (1999) 745-756. [PMID: 10425677]

5. Bossi, R.T., Negri, A., Tedeschi, G. and Mattevi, A. Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis. Biochemistry 41 (2002) 3018-3024. [PMID: 11863440]

6. Katoh, A., Uenohara, K., Akita, M. and Hashimoto, T. Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid. Plant Physiol. 141 (2006) 851-857. [PMID: 16698895]

[EC 1.4.3.16 created 1984, modified 2008]

[EC 1.4.3.17 Transferred entry: now EC 1.3.3.10 tryptophan α,β-oxidase. Enzyme was incorrectly classified as acting on a CH-NH bond rather than a CH-CH bond. (EC 1.4.3.17 created 2000, deleted 2003)]

[EC 1.4.3.18 Deleted entry: Not approved as the enzyme was shown to be a dehydrogenase and not an oxidase (see EC 1.5.99.12 cytokinin dehydrogenase). (EC 1.4.3.18 proposed 2000)]

EC 1.4.3.19

Accepted name: glycine oxidase

Reaction: glycine + H2O + O2 = glyoxylate + NH3 + H2O2 (overall reaction)
(1a) glycine + O2 = 2-iminoacetate + H2O2
(1b) 2-iminoglycine + H2O = glyoxylate + NH3

For diagram of reaction click here

Systematic name: glycine:oxygen oxidoreductase (deaminating)

Comments: A flavoenzyme containing non-covalently bound FAD. The enzyme from Bacillus subtilis is active with glycine, sarcosine, N-ethylglycine, D-alanine, D-α-aminobutyrate, D-proline, D-pipecolate and N-methyl-D-alanine. It differs from EC 1.4.3.3, D-amino-acid oxidase, due to its activity on sarcosine and D-pipecolate. The intermediate 2-iminoacetate is used directly by EC 2.8.1.10, thiazole synthase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 39307-16-9

References:

1. Job, V., Marcone, G.L., Pilone, M.S. and Pollegioni, L. Glycine oxidase from Bacillus subtilis. Characterization of a new flavoprotein. J. Biol. Chem. 277 (2002) 6985-6993. [PMID: 11744710]

2. Nishiya, Y. and Imanaka, T. Purification and characterization of a novel glycine oxidase from Bacillus subtilis. FEBS Lett. 438 (1998) 263-266. [PMID: 9827558]

[EC 1.4.3.19 created 2002, modified 2012]

EC 1.4.3.20

Accepted name: L-lysine 6-oxidase

Reaction: L-lysine + O2 + H2O = (S)-2-amino-6-oxohexanoate + H2O2 + NH3

Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine

Other name(s): L-lysine-ε-oxidase; Lod; LodA; marinocine

Systematic name: L-lysine:oxygen 6-oxidoreductase (deaminating)

Comments: Differs from EC 1.4.3.13, protein-lysine 6-oxidase, by using free L-lysine rather than the protein-bound form. 2-N-Acetyl-L-lysine is also a substrate, but 6-N-acetyl-L-lysine, which has an acetyl group at position 6, is not a substrate. Also acts on L-ornithine, D-lysine and 4-hydroxy-L-lysine, but more slowly. The amines cadaverine and putrescine are not substrates [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 1116448-48-6

References:

1. Lucas-Elío, P., Gómez, D., Solano, F. and Sanchez-Amat, A. The antimicrobial activity of marinocine, synthesized by Marinomonas mediterranea, is due to hydrogen peroxide generated by its lysine oxidase activity. J. Bacteriol. 188 (2006) 2493-2501. [PMID: 16547036]

2. Gómez, D., Lucas-Elío, P., Sanchez-Amat, A. and Solano, F. A novel type of lysine oxidase: L-lysine-ε-oxidase. Biochim. Biophys. Acta 1764 (2006) 1577-1585. [PMID: 17030025]

[EC 1.4.3.20 created 2006]

EC 1.4.3.21

Accepted name: primary-amine oxidase

Reaction: RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

Other name(s): amine oxidase (ambiguous); amine oxidase (copper-containing); amine oxidase (pyridoxal containing) (incorrect); benzylamine oxidase (incorrect); CAO (ambiguous); copper amine oxidase (ambiguous); Cu-amine oxidase (ambiguous); Cu-containing amine oxidase (ambiguous); diamine oxidase (incorrect); diamino oxhydrase (incorrect); histamine deaminase (ambiguous); histamine oxidase (ambiguous); monoamine oxidase (ambiguous); plasma monoamine oxidase (ambiguous); polyamine oxidase (ambiguous); semicarbazide-sensitive amine oxidase (ambiguous); SSAO (ambiguous)

Systematic name: primary-amine:oxygen oxidoreductase (deaminating)

Comments: A group of enzymes that oxidize primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, monoamine oxidase, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).

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

References:

1. Haywood, G.W. and Large, P.J. Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source. Biochem. J. 199 (1981) 187-201. [PMID: 7337701]

2. Tipping, A.J. and McPherson, M.J. Cloning and molecular analysis of the pea seedling copper amine oxidase. J. Biol. Chem. 270 (1995) 16939-16946. [PMID: 7622512]

3. Lyles, G.A. Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects. Int. J. Biochem. Cell Biol. 28 (1996) 259-274. [PMID: 8920635]

4. Wilce, M.C., Dooley, D.M., Freeman, H.C., Guss, J.M., Matsunami, H., McIntire, W.S., Ruggiero, C.E., Tanizawa, K. and Yamaguchi, H. Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone. Biochemistry 36 (1997) 16116-16133. [PMID: 9405045]

5. Lee, Y. and Sayre, L.M. Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini. J. Biol. Chem. 273 (1998) 19490-19494. [PMID: 9677370]

6. Houen, G. Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions. APMIS Suppl. 96 (1999) 1-46. [PMID: 10668504]

7. Andrés, N., Lizcano, J.M., Rodríguez, M.J., Romera, M., Unzeta, M. and Mahy, N. Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase. J. Histochem. Cytochem. 49 (2001) 209-217. [PMID: 11156689]

8. Saysell, C.G., Tambyrajah, W.S., Murray, J.M., Wilmot, C.M., Phillips, S.E., McPherson, M.J. and Knowles, P.F. Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue. Biochem. J. 365 (2002) 809-816. [PMID: 11985492]

9. O'Sullivan, J., Unzeta, M., Healy, J., O'Sullivan, M.I., Davey, G. and Tipton, K.F. Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do. Neurotoxicology 25 (2004) 303-315. [PMID: 14697905]

10. Airenne, T.T., Nymalm, Y., Kidron, H., Smith, D.J., Pihlavisto, M., Salmi, M., Jalkanen, S., Johnson, M.S. and Salminen, T.A. Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications. Protein Sci. 14 (2005) 1964-1974. [PMID: 16046623]

[EC 1.4.3.21 created 2007 (EC 1.4.3.6 created 1961, part-incorporated 2008)]

EC 1.4.3.22

Accepted name: diamine oxidase

Reaction: histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2

Other name(s): amine oxidase (ambiguous); amine oxidase (copper-containing) (ambiguous); CAO (ambiguous); Cu-containing amine oxidase (ambiguous); copper amine oxidase (ambiguous); diamine oxidase (ambiguous); diamino oxhydrase (ambiguous); histaminase; histamine deaminase (incorrect); semicarbazide-sensitive amine oxidase (incorrect); SSAO (incorrect)

Systematic name: histamine:oxygen oxidoreductase (deaminating)

Comments: A group of enzymes that oxidize diamines, such as histamine, and also some primary monoamines but have little or no activity towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, like EC 1.4.3.21 (primary-amine oxidase) but unlike EC 1.4.3.4 (monoamine oxidase), they are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide.

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

References:

1. Zeller, E.A. Diamine oxidases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 313-335.

2. Crabbe, M.J., Waight, R.D., Bardsley, W.G., Barker, R.W., Kelly, I.D. and Knowles, P.F. Human placental diamine oxidase. Improved purification and characterization of a copper- and manganese-containing amine oxidase with novel substrate specificity. Biochem. J. 155 (1976) 679-687. [PMID: 182134]

3. Chassande, O., Renard, S., Barbry, P. and Lazdunski, M. The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter. J. Biol. Chem. 269 (1994) 14484-14489. [PMID: 8182053]

4. Houen, G. Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions. APMIS Suppl. 96 (1999) 1-46. [PMID: 10668504]

5. Elmore, B.O., Bollinger, J.A. and Dooley, D.M. Human kidney diamine oxidase: heterologous expression, purification, and characterization. J. Biol. Inorg. Chem. 7 (2002) 565-579. [PMID: 12072962]

[EC 1.4.3.22 created 2007 (EC 1.4.3.6 created 1961, part-incorporated 2008)]

EC 1.4.3.23

Accepted name: 7-chloro-L-tryptophan oxidase

Reaction: 7-chloro-L-tryptophan + O2 = 2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2

For diagram of reaction click here

Other name(s): RebO

Systematic name: 7-chloro-L-tryptophan:oxygen oxidoreductase

Comments: Contains a noncovalently bound FAD [1,2]. This enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. During catalysis, the bound FAD is reoxidized at the expense of molecular oxygen, producing one molecule of hydrogen peroxide. The enzyme shows significant preference for 7-chloro-L-tryptophan over L-tryptophan [1].

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

References:

1. Nishizawa, T., Aldrich, C.C. and Sherman, D.H. Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243. J. Bacteriol. 187 (2005) 2084-2092. [PMID: 15743957]

2. Howard-Jones, A.R. and Walsh, C.T. Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD. Biochemistry 44 (2005) 15652-15663. [PMID: 16313168]

[EC 1.4.3.23 created 2010]

EC 1.4.3.24

Accepted name: pseudooxynicotine oxidase

Reaction: 4-(methylamino)-1-(pyridin-3-yl)butan-1-one + H2O + O2 = 4-oxo-4-(pyridin-3-yl)butanal + methylamine + H2O2

Glossary: 4-(methylamino)-1-(pyridin-3-yl)butan-1-one = pseudooxynicotine
4-oxo-4-(pyridin-3-yl)butanal = 3-succinoylsemialdehyde-pyridine

Systematic name: 4-(methylamino)-1-(pyridin-3-yl)butan-1-one:oxygen oxidoreductase (methylamine releasing)

Comments: Contains one non-covalently bound FAD molecule per dimer. This enzyme, characterized from the soil bacterium Pseudomonas sp. HZN6, is involved the nicotine degradation.

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

References:

1. Qiu, J., Ma, Y., Wen, Y., Chen, L., Wu, L. and Liu, W. Functional identification of two novel genes from Pseudomonas sp. strain HZN6 involved in the catabolism of nicotine. Appl. Environ. Microbiol. 78 (2012) 2154-2160. [PMID: 22267672]

[EC 1.4.3.24 created 2012]


EC 1.4.4 With a disulfide as acceptor

Contents

EC 1.4.4.1 now EC 1.21.4.1
EC 1.4.4.2 glycine dehydrogenase (aminomethyl-transferring)

[EC 1.4.4.1 Transferred entry: now EC 1.21.4.1, D-proline reductase (dithiol) (EC 1.4.4.1 created 1972, modified 1982 (EC 1.4.1.6 created 1961, incorporated 1982), deleted 2003)]

EC 1.4.4.2

Accepted name: glycine dehydrogenase (aminomethyl-transferring)

Reaction: glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2

For diagram of reaction click here.

Glossary: dihydrolipoyl group

Other name(s): P-protein; glycine decarboxylase; glycine-cleavage complex; glycine:lipoylprotein oxidoreductase (decarboxylating and acceptor-aminomethylating); protein P1; glycine dehydrogenase (decarboxylating); glycine cleavage system P-protein; glycine-cleavage complex P-protein

Systematic name: glycine:H-protein-lipoyllysine oxidoreductase (decarboxylating, acceptor-amino-methylating)

Comments: A pyridoxal-phosphate protein. A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10, aminomethyltransferase), the L protein (EC 1.8.1.4, dihydrolipoyl dehydrogenase) and the lipoyl-bearing H protein [3]. Previously known as glycine synthase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37259-67-9

References:

1. Hiraga, K. and Kikuchi, G. The mitochondrial glycine cleavage system. Functional association of glycine decarboxylase and aminomethyl carrier protein. J. Biol. Chem. 255 (1980) 11671-11676. [PMID: 7440563]

2. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]

3. Nesbitt, N.M., Baleanu-Gogonea, C., Cicchillo, R.M., Goodson, K., Iwig, D.F., Broadwater, J.A., Haas, J.A., Fox, B.G. and Booker, S.J. Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. Protein Expr. Purif. 39 (2005) 269-282. [PMID: 15642479]

[EC 1.4.4.2 created 1984, modified 2003, modified 2006, modified 2013]


EC 1.4.5 with a quinone or similar compound as acceptor

EC 1.4.5.1

Accepted name: D-amino acid dehydrogenase (quinone)

Reaction: a D-amino acid + H2O + a quinone = a 2-oxo carboxylate + NH3 + a quinol

Other name(s): DadA

Systematic name: D-amino acid:quinone oxidoreductase (deaminating)

Comments: An iron-sulfur flavoprotein (FAD). The enzyme from the bacterium Helicobacter pylori is highly specific for D-proline, while the enzyme from the bacterium Escherichia coli B is most active with D-alanine, D-phenylalanine and D-methionine. This enzyme may be the same as EC 1.4.99.6.

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

References:

1. Olsiewski, P.J., Kaczorowski, G.J. and Walsh, C. Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B. J. Biol. Chem. 255 (1980) 4487-4494. [PMID: 6102989]

2. Tanigawa, M., Shinohara, T., Saito, M., Nishimura, K., Hasegawa, Y., Wakabayashi, S., Ishizuka, M. and Nagata, Y. D. Amino acid dehydrogenase from Helicobacter pylori NCTC 11637. Amino Acids 38 (2010) 247-255. [PMID: 19212808]

[EC 1.4.5.1 created 2010]


EC 1.4.7 With an iron-sulfur protein as acceptor

EC 1.4.7.1

Accepted name: glutamate synthase (ferredoxin)

Reaction: 2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+ (overall reaction)
(1a) L-glutamate + NH3 = L-glutamine + H2O
(1b) L-glutamate + 2 oxidized ferredoxin + H2O = NH3 + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+

Other name(s): ferredoxin-dependent glutamate synthase; ferredoxin-glutamate synthase; glutamate synthase (ferredoxin-dependent)

Systematic name: L-glutamate:ferredoxin oxidoreductase (transaminating)

Comments: Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH3 is channeled through a 24 Å channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein [5,6].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 62213-56-3

References:

1. Galván, F., Márquez, A.J. and Vega, J.M. Purification and molecular properties of ferredoxin-glutamate synthase from Chlamydomonas reinhardii. Planta 162 (1984) 180-187.

2. Lea, P.J. and Miflin, B.J. Alternative route for nitrogen assimilation in higher plants. Nature (Lond.) 251 (1974) 614-616. [PMID: 4423889]

3. Ravasio, S., Dossena, L., Martin-Figueroa, E., Florencio, F.J., Mattevi, A., Morandi, P., Curti, B. and Vanoni, M.A. Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis PCC6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated α subunit. Biochemistry 41 (2002) 8120-8133. [PMID: 12069605]

4. Navarro, F., Martin-Figueroa, E., Candau, P. and Florencio, F.J. Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the cyanobacterium Synechocystis sp. PCC 6803: expression and assembly in Escherichia coli. Arch. Biochem. Biophys. 379 (2000) 267-276. [PMID: 10898944]

5. van den Heuvel, R.H., Ferrari, D., Bossi, R.T., Ravasio, S., Curti, B., Vanoni, M.A., Florencio, F.J. and Mattevi, A. Structural studies on the synchronization of catalytic centers in glutamate synthase. J. Biol. Chem. 277 (2002) 24579-24583. [PMID: 11967268]

6. van den Heuvel, R.H., Svergun, D.I., Petoukhov, M.V., Coda, A., Curti, B., Ravasio, S., Vanoni, M.A. and Mattevi, A. The active conformation of glutamate synthase and its binding to ferredoxin. J. Mol. Biol. 330 (2003) 113-128. [PMID: 12818206]

[EC 1.4.7.1 created 1976, modified 2012]


EC 1.4.9 With a copper protein as acceptor

Contents

EC 1.4.9.1 methylamine dehydrogenase (amicyanin)
EC 1.4.9.2 aralkylamine dehydrogenase (azurin)

EC 1.4.9.1

Accepted name: methylamine dehydrogenase (amicyanin)

Reaction: methylamine + H2O + 2 amicyanin = formaldehyde + NH3 + 2 reduced amicyanin

Glossary: TTQ = tryptophan tryptophylquinone
amicyanin = an electron-transfer protein containing a type-1 copper site.

Other name(s): amine dehydrogenase; primary-amine dehydrogenase; amine: (acceptor) oxidoreductase (deaminating); primary-amine:(acceptor) oxidoreductase (deaminating)

Systematic name: methylamine:amicyanin oxidoreductase (deaminating)

Comments: Contains tryptophan tryptophylquinone (TTQ) cofactor. The enzyme oxidizes aliphatic monoamines and diamines, histamine and ethanolamine, but not secondary and tertiary amines, quaternary ammonium salts or aromatic amines.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD , CAS registry number: 60496-14-2

References:

1. De Beer, R., Duine, J.A., Frank, J., Jr. and Large, P.J. The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure. Biochim. Biophys. Acta 622 (1980) 370-374. [PMID: 6246962]

2. Eady, R.R. and Large, P.J. Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine. Biochem. J. 106 (1968) 245-255. [PMID: 4388687]

3. Eady, R.R. and Large, P.J. Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1. Biochem. J. 123 (1971) 757-771. [PMID: 5124384]

4. Cavalieri, C., Biermann, N., Vlasie, M.D., Einsle, O., Merli, A., Ferrari, D., Rossi, G.L. and Ubbink, M. Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus. Biochemistry 47 (2008) 6560-6570. [PMID: 18512962]

5. Meschi, F., Wiertz, F., Klauss, L., Cavalieri, C., Blok, A., Ludwig, B., Heering, H.A., Merli, A., Rossi, G.L. and Ubbink, M. Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex. J. Am. Chem. Soc. 132 (2010) 14537-14545. [PMID: 20873742]

[EC 1.4.9.1 created 1978 as EC 1.4.99.3, modified 1986, transferred 2011 to EC 1.4.98.1, transferred 2011 to EC 1.4.9.1]

EC 1.4.9.2

Accepted name: aralkylamine dehydrogenase (azurin)

Reaction: ArCH2NH2 + H2O + 2 azurin = ArCHO + NH3 + 2 reduced azurin

Glossary: azurin = an electron-transfer protein containing a type-1 copper site

Other name(s): aromatic amine dehydrogenase; arylamine dehydrogenase; tyramine dehydrogenase; aralkylamine:(acceptor) oxidoreductase (deaminating)

Systematic name: aralkylamine:azurin oxidoreductase (deaminating)

Comments: Phenazine methosulfate can act as acceptor. Acts on aromatic amines and, more slowly, on some long-chain aliphatic amines, but not on methylamine or ethylamine

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

References:

1. Iwaki, M., Yagi, T., Horiike, K., Saeki, Y., Ushijima, T. and Nozaki, M. Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp. Arch. Biochem. Biophys. 220 (1983) 253-262. [PMID: 6830237]

2. Hyun, Y.L. and Davidson, V.L. Electron transfer reactions between aromatic amine dehydrogenase and azurin. Biochemistry 34 (1995) 12249-12254. [PMID: 7547967]

3. Hyun, Y.L., Zhu, Z. and Davidson, V.L. Gated and ungated electron transfer reactions from aromatic amine dehydrogenase to azurin. J. Biol. Chem. 274 (1999) 29081-29086. [PMID: 10506161]

4. Davidson, V.L. Electron transfer in quinoproteins. Arch. Biochem. Biophys. 428 (2004) 32-40. [PMID: 15234267]

5. Sukumar, N., Chen, Z.W., Ferrari, D., Merli, A., Rossi, G.L., Bellamy, H.D., Chistoserdov, A., Davidson, V.L. and Mathews, F.S. Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis. Biochemistry 45 (2006) 13500-13510. [PMID: 17087503]

[EC 1.4.9.2 created 1986 as EC 1.4.99.4, transferred 2011 to 1.4.9.2]


EC 1.4.98 With other, known, physiological acceptors
[EC 1.4.98.1 Transferred entry: amine dehydrogenase. Now EC 1.4.9.1, methylamine dehydrogenase (amicyanin) (EC 1.4.98.1 created 1978 as EC 1.4.99.3, modified 1986, transferred 2011 to EC 1.4.98.1, deleted 2011)]


EC 1.4.99 With unknown physiological acceptors

Contents

EC 1.4.99.1 transferred now EC 1.4.99.6
EC 1.4.99.2 taurine dehydrogenase
EC 1.4.99.3 transferred now EC 1.4.98.1
EC 1.4.99.4 transferred now EC 1.4.9.2
EC 1.4.99.5 glycine dehydrogenase (cyanide-forming)
EC 1.4.99.6 D-arginine dehydrogenase

[EC 1.4.99.1 Transferred entry: D-amino-acid dehydrogenase. Now listed as EC 1.4.99.6, D-arginine dehydrogenase (EC 1.4.99.1 created 1972, deleted 2015)]

EC 1.4.99.2

Accepted name: taurine dehydrogenase

Reaction: taurine + H2O + acceptor = 2-sulfoacetaldehyde + NH3 + reduced acceptor

Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
taurine = 2-aminoethanesulfonate

Other name(s): taurine:(acceptor) oxidoreductase (deaminating); N-methyltaurine dehydrogenase; TauXY; TDH

Systematic name: taurine:acceptor oxidoreductase (deaminating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 50812-14-1

References:

1. Kondo, H., Kagotani, K., Oshima, M. and Ishimoto, M. Purification and some properties of taurine dehydrogenase from a bacterium. J. Biochem. (Tokyo) 73 (1973) 1269-1278. [PMID: 4724302]

[EC 1.4.99.2 created 1976]

[EC 1.4.99.3 Transferred entry: amine dehydrogenase. Now EC 1.4.98.1, methylamine dehydrogenase (amicyanin) (EC 1.4.99.3 created 1978, modified 1986, deleted 2011)]

[EC 1.4.99.4 Transferred entry: aralkylamine dehydrogenase. Now EC 1.4.9.2, aralkylamine dehydrogenase (azurin) (EC 1.4.99.4 created 1986, deleted 2011)]

EC 1.4.99.5

Accepted name: glycine dehydrogenase (cyanide-forming)

Reaction: glycine + 2 A = hydrogen cyanide + CO2 + 2 AH2

For diagram click here.

Other name(s): hydrogen cyanide synthase; HCN synthase

Systematic name: glycine:acceptor oxidoreductase (hydrogen-cyanide-forming)

Comments: The enzyme from Pseudomonas sp. contains FAD. The enzyme is membrane-bound, and the 2-electron acceptor is a component of the respiratory chain. The enzyme can act with various artificial electron acceptors, including phenazine methosulfate.

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

References:

1. Wissing, F. Cyanide production from glycine by a homogenate from a Pseudomonas species. J. Bacteriol. 121 (1975) 695-699. [PMID: 234422]

2. Castric, P.A. Glycine metabolism by Pseudomonas aeruginosa: Hydrogen cyanide biosynthesis. J. Bacteriol. 130 (1977) 826-831. [PMID: 233722]

3. Laville, J., Blumer, C., Von Schroetter, C., Gaia, V., Defago, G., Keel, C. and Haas, D. Characterization of the hcnABC gene cluster encoding hydrogen cyanide synthase and anaerobic regulation by ANR in the strictly aerobic biocontrol agent Pseudomonas fluorescens CHA0. J. Bacteriol. 180 (1998) 3187-3196. [PMID: 9620970]

4. Blumer, C. and Haas, D. Mechanism, regulation, and ecological role of bacterial cyanide biosynthesis. Arch. Microbiol. 173 (2000) 170-177. [PMID: 10763748]

[EC 1.4.99.5 created 2002]

EC 1.4.99.6

Accepted name: D-arginine dehydrogenase

Reaction: D-arginine + acceptor + H2O = 5-guanidino-2-oxopentanoate + NH3 + reduced acceptor (overall reaction)
(1a) D-arginine + acceptor = iminoarginine + reduced acceptor
(1b) iminoarginine + H2O = 5-guanidino-2-oxopentanoate + NH3 (spontaneous)

Glossary: 5-guanidino-2-oxopentanoate = 2-ketoarginine
iminoarginine = 5-carbamimidamido-2-iminopentanoate

Other name(s): D-amino-acid:(acceptor) oxidoreductase (deaminating); D-amino-acid dehydrogenase; D-amino-acid:acceptor oxidoreductase (deaminating)

Systematic name: D-arginine:acceptor oxidoreductase (deaminating)

Comments: Contains a non-covalent FAD cofactor. The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, is a catabolic enzyme that is part of a two-enzyme complex involved in the racemization of D and L-arginine. The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate. However, activity is maximal with D-arginine and D-lysine. Not active on glycine.

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

References:

1. Tsukada, K. D-Amino acid dehydrogenases of Pseudomonas fluorescens. J. Biol. Chem. 241 (1966) 4522-4528. [PMID: 5925166]

2. Li, C. and Lu, C.D. Arginine racemization by coupled catabolic and anabolic dehydrogenases. Proc. Natl. Acad. Sci. USA 106 (2009) 906-911. [PMID: 19139398]

3. Fu, G., Yuan, H., Li, C., Lu, C.D., Gadda, G. and Weber, I.T. Conformational changes and substrate recognition in Pseudomonas aeruginosa D-arginine dehydrogenase. Biochemistry 49 (2010) 8535-8545. [PMID: 20809650]

4. Yuan, H., Fu, G., Brooks, P.T., Weber, I. and Gadda, G. Steady-state kinetic mechanism and reductive half-reaction of D-arginine dehydrogenase from Pseudomonas aeruginosa. Biochemistry 49 (2010) 9542-9550. [PMID: 20932054]

5. Fu, G., Yuan, H., Wang, S., Gadda, G. and Weber, I.T. Atomic-resolution structure of an N5 flavin adduct in D-arginine dehydrogenase. Biochemistry 50 (2011) 6292-6294. [PMID: 21707047]

6. Yuan, H., Xin, Y., Hamelberg, D. and Gadda, G. Insights on the mechanism of amine oxidation catalyzed by D-arginine dehydrogenase through pH and kinetic isotope effects. J. Am. Chem. Soc. 133 (2011) 18957-18965. [PMID: 21999550]

[EC 1.4.99.6 created 1972 as EC 1.4.99.1, transferred 2015 to EC 1.4.99.6]


Continued with EC 1.5
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