EC 1 - Oxidoreductases
EC 1.4 - Acting on the CH-NH2 group of donors
EC 1.4.3 - With oxygen as acceptor
EC 1.4.3.21 - Primary-amine oxidase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.4.3.21
Names
Accepted name:
primary-amine oxidase
Other
names:
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]
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)
Reaction
- RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
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
References
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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 : 187-201 (1981). [PMID: 7337701]
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Cloning and molecular analysis of the pea seedling copper amine oxidase.J. Biol. Chem. 270 : 16939-16946 (1995). [PMID: 7622512]
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Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects.Int. J. Biochem. Cell Biol. 28 : 259-274 (1996). [PMID: 8920635]
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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 : 16116-16133 (1997). [PMID: 9405045]
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Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini.J. Biol. Chem. 273 : 19490-19494 (1998). [PMID: 9677370]
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Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions.APMIS Suppl. 96 : 1-46 (1999). [PMID: 10668504]
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Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase.J. Histochem. Cytochem. 49 : 209-217 (2001). [PMID: 11156689]
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Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue.Biochem. J. 365 : 809-816 (2002). [PMID: 11985492]
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Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do.Neurotoxicology 25 : 303-315 (2004). [PMID: 14697905]
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Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications.Protein Sci. 14 : 1964-1974 (2005). [PMID: 16046623]
[EC 1.4.3.21 created 2008]