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)

Oxidoreductases;
Acting on the CH-NH2 group of donors;
With oxygen as acceptor

primary-amine:oxygen oxidoreductase (deaminating)

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853]

R01853 > R02382 R02529 R02613 R03139 R04027 R04300 R05334 R06154 R06740

RCH2NH2 [CPD:C00375];
H2O [CPD:C00001];
O2 [CPD:C00007]

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).

1  [PMID:7337701]

Haywood GW, Large PJ.

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.

Candida boidinii

2  [PMID:7622512]

Tipping AJ, McPherson MJ.

Cloning and molecular analysis of the pea seedling copper amine oxidase.

J. Biol. Chem. 270 (1995) 16939-46.

Pisum sativum

3  [PMID:8920635]

Lyles GA.

Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects.

Int. J. Biochem. Cell. Biol. 28 (1996) 259-74.

Homo sapiens [GN:hsa]

4  [PMID:9405045]

Wilce MC, Dooley DM, Freeman HC, Guss JM, Matsunami H, McIntire WS, Ruggiero CE, Tanizawa K, 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) 16116-33.

Arthrobacter globiformis

5  [PMID:9677370]

Lee Y, Sayre LM.

Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini.

J. Biol. Chem. 273 (1998) 19490-4.

Bos taurus [GN:bta]

6  [PMID:10668504]

Houen G.

Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions.

APMIS. Suppl. 96 (1999) 1-46.

Homo sapiens [GN:hsa]

7  [PMID:11156689]

Andres N, Lizcano JM, Rodriguez MJ, Romera M, Unzeta M, Mahy N.

Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase.

J. Histochem. Cytochem. 49 (2001) 209-17.

Homo sapiens [GN:hsa]

8  [PMID:11985492]

Saysell CG, Tambyrajah WS, Murray JM, Wilmot CM, Phillips SE, McPherson MJ, Knowles PF.

Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue.

Biochem. J. 365 (2002) 809-16.

Escherichia coli [GN:eco]

9  [PMID:14697905]

O'Sullivan J, Unzeta M, Healy J, O'Sullivan MI, Davey G, Tipton KF.

Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do.

Neurotoxicology. 25 (2004) 303-15.

Homo sapiens [GN:hsa]

10 [PMID:16046623]

Airenne TT, Nymalm Y, Kidron H, Smith DJ, Pihlavisto M, Salmi M, Jalkanen S, Johnson MS, Salminen TA.

Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications.

Protein. Sci. 14 (2005) 1964-74.

Homo sapiens [GN:hsa]