Copper Amine Oxidase
Copper amine oxidase refers to a ubiquitous family of enzymes that catalyze the oxidative deamination of primary amines, concomitant with the two-electron reduction of molecular oxygen to hydrogen peroxide. To accomplish this reaction, these enzymes utilize the redox-active cofactor 2,4,5-trihydroxyphenylalanine quinone (TOPA quinone or TPQ).
Up until recently, copper amine oxidases (CAOs) were classified within the Enzyme Commission classification EC 220.127.116.11, distinct from the flavin-containing amine oxidases (monoamine oxidase, EC 18.104.22.168) (Boyce et al. 2009). This distinction was based on cofactor content rather than reaction catalyzed, however, leading to some confusion in the literature. For clarification, EC 22.214.171.124 has now been deleted and replaced with two distinct entries: EC 126.96.36.199 and EC 188.8.131.52 (Boyce et al. 2009). EC 184.108.40.206...
- Boyce S, Tipton KF, O’Sullivan MI, Davey GP, Gildea MM, McDonald AG, Olivieri A, O’Sullivan J (2009) Nomenclature and potential functions of copper amine oxidases. In: Floris G, Mondovì B (eds) Copper amine oxidases: structures, catalytic mechanisms, and role in pathophysiology. CRC Press, Boca RatonGoogle Scholar
- Guss JM, Zanotti G, Salminen TA (2009) Copper amine oxidase crystal structures. In: Floris G, Mondovì B (eds) Copper amine oxidases: structures, catalytic mechanisms, and role in pathophysiology. CRC Press, Boca RatonGoogle Scholar