AOC3 deaminates BZAM

Stable Identifier
R-HSA-5696183
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
19588076 The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase

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

Cell. Mol. Life Sci. 2009
9653080 Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule

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

J. Exp. Med. 1998
17400359 Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes

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

Biochimie 2007
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
primary amine oxidase activity of AOC3 dimer:2xCu2+:4xCa2+ [plasma membrane]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created