| Entry |
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| Name |
primary-amine oxidase;
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)
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| Class |
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With oxygen as acceptor
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| Sysname |
primary-amine:oxygen oxidoreductase (deaminating)
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| Reaction(IUBMB) |
RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN: R01853]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
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).
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| History |
EC 1.4.3.21 created 2007 (EC 1.4.3.6 created 1961, part-incorporated 2008)
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| Pathway |
| ec00260 | Glycine, serine and threonine metabolism |
| ec00950 | Isoquinoline alkaloid biosynthesis |
| ec00960 | Tropane, piperidine and pyridine alkaloid biosynthesis |
| ec01110 | Biosynthesis of secondary metabolites |
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| Orthology |
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| Genes |
» show all
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| Reference |
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| Authors |
Haywood GW, Large PJ. |
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| Title |
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. |
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| Journal |
Biochem J 199:187-201 (1981) |
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| Reference |
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| Authors |
Tipping AJ, McPherson MJ. |
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| Title |
Cloning and molecular analysis of the pea seedling copper amine oxidase. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Lyles GA. |
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| Title |
Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects. |
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| Journal |
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| Reference |
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| Authors |
Wilce MC, Dooley DM, Freeman HC, Guss JM, Matsunami H, McIntire WS, Ruggiero CE, Tanizawa K, Yamaguchi H. |
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| Title |
Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Lee Y, Sayre LM. |
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| Title |
Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini. |
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| Journal |
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| Reference |
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| Authors |
Houen G. |
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| Title |
Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions. |
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| Journal |
APMIS Suppl 96:1-46 (1999) |
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| Reference |
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| Authors |
Andres N, Lizcano JM, Rodriguez MJ, Romera M, Unzeta M, Mahy N. |
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| Title |
Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase. |
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| Journal |
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| Reference |
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| Authors |
Saysell CG, Tambyrajah WS, Murray JM, Wilmot CM, Phillips SE, McPherson MJ, Knowles PF. |
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| Title |
Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue. |
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| Journal |
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| Reference |
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| Authors |
O'Sullivan J, Unzeta M, Healy J, O'Sullivan MI, Davey G, Tipton KF. |
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| Title |
Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do. |
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| Journal |
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| Reference |
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| Authors |
Airenne TT, Nymalm Y, Kidron H, Smith DJ, Pihlavisto M, Salmi M, Jalkanen S, Johnson MS, Salminen TA. |
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| Title |
Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 1.4.3.21 |
| ExPASy - ENZYME nomenclature database: | 1.4.3.21 |
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