AOC3 deaminates BZAM

Stable Identifier
Reaction [transition]
Homo sapiens
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Membrane primary amine oxidase (AOC3, aka vascular adhesion protein 1, VAP-1) is a membrane-bound, dimeric enzyme that can catalyse the oxidative deamination of primary amines such as benzylamine (BZAM) and methyalmine to their respective aldehydes (Kaitaniemi et al. 2009, Bour et al. 2007). It is widely expressed with highest expression in peripheral lymph nodes, hepatic endothelia, appendix, lung and small intestine (Smith et al. 1998).

Literature References
PubMed ID Title Journal Year
9653080 Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule

Bono, P, Jalkanen, S, Smith, DJ, Leu, T, Salmi, M, Hellman, J

J. Exp. Med. 1998
19588076 The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase

Jalkanen, S, Elovaara, H, Grön, K, Salmi, M, Kaitaniemi, S, Elima, K, Liukkonen, J, Salminen, T, Kidron, H

Cell. Mol. Life Sci. 2009
17400359 Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes

Saulnier-Blache, JS, Lefort, C, Wabitsch, M, Valet, P, Gres, S, Carpéné, C, Zorzano, A, Prévot, D, Daviaud, D, Bour, S

Biochimie 2007
Catalyst Activity

primary amine oxidase activity of AOC3 dimer:2xCu2+:4xCa2+ [plasma membrane]

Orthologous Events
Cross References
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