The Enzyme Database

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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 edn, vol. 7, Academic Press, New York, 1963, pp. 609–648.
2.  Wellner, D. and Meister, A. Crystalline L-amino acid oxidase of Crotalus adamanteus. J. Biol. Chem. 235 (1960) 2013–2018. [PMID: 13843884]
[EC 1.4.3.2 created 1961]
 
 
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. N2-Acetyl-L-lysine is also a substrate, but N6-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. [DOI] [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. [DOI] [PMID: 17030025]
[EC 1.4.3.20 created 2006, modified 2011]
 
 
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
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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
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. [DOI] [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 rebeccamycin biosynthesis, 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
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. [DOI] [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. [DOI] [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
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. [DOI] [PMID: 22267672]
[EC 1.4.3.24 created 2012]
 
 
EC 1.4.3.25     
Accepted name: L-arginine oxidase
Reaction: L-arginine + H2O + O2 = 5-guanidino-2-oxopentanoate + NH3 + H2O2
Systematic name: L-arginine:oxygen oxidoreductase (deaminating)
Comments: Contains FAD. The enzyme from cyanobacteria can also act on other basic amino acids with lower activity. The enzyme from the bacterium Pseudomonas sp. TPU 7192 is highly specific.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Miller, D.L. and Rodwell, V.W. Metabolism of basic amino acids in Pseudomonas putida. Intermediates in L-arginine catabolism. J. Biol. Chem. 246 (1971) 5053–5058. [PMID: 5570437]
2.  Pistorius, E.K. and Voss, H. Some properties of a basic L-amino-acid oxidase from Anacystis nidulans. Biochim. Biophys. Acta 611 (1980) 227–240. [DOI] [PMID: 6766743]
3.  Gau, A.E., Heindl, A., Nodop, A., Kahmann, U. and Pistorius, E.K. L-amino acid oxidases with specificity for basic L-amino acids in cyanobacteria. Z. Naturforsch. C 62 (2007) 273–284. [PMID: 17542496]
4.  Matsui, D., Terai, A. and Asano, Y. L-Arginine oxidase from Pseudomonas sp. TPU 7192: Characterization, gene cloning, heterologous expression, and application to L-arginine determination. Enzyme Microb. Technol. 82 (2016) 151–157. [DOI] [PMID: 26672462]
[EC 1.4.3.25 created 2017]
 
 


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