They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor:[2] The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2.
[3][4] This enzyme belongs to oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor.
The copper ion is coordinated with three histidine residues and two water molecules in a distorted square pyramidal geometry, and has a dual function in catalysis and TPQ biogenesis.
The N2 and N3 N-terminal domains share a common structural fold, its core consisting of alpha-beta(4), where the helix is packed against the coiled anti-parallel beta-sheets.
An additional domain is found at the N-terminal of some copper amine oxidases, as well as in related proteins such as cell wall hydrolase and N-acetylmuramoyl-L-alanine amidase.