AOC3 deaminates BZAM

Stable Identifier
R-HSA-5696183
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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
Participants
Participates
Catalyst Activity

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

Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
Cite Us!