Primary amine oxidase

Primary amine oxidase, also referred to as phenylethylamine oxidase or copper amine oxidase in certain bacterial species, is an enzyme that catalyzes the oxidative deamination of primary aromatic amines like phenylethylamine, producing the corresponding aldehyde, ammonia, and hydrogen peroxide. In humans, analogous activity is performed by monoamine oxidase A and monoamine oxidase B, which play crucial roles in neurotransmitter catabolism and are therapeutic targets in neurological and psychiatric disorders. In microorganisms such as Arthrobacter globiformis, this enzyme is copper-dependent and uses topaquinone as a cofactor.

Other names

2-phenylethylamine oxidasecopper amine oxidasetyramine oxidasetynA (bacterial)monoamine oxidase (if referring broadly in mammals)MAO-AMAO-Bsemicarbazide-sensitive amine oxidase (SSAOs, but these have broader substrate scopes)

Inhibition of amine oxidase enzymatic activity, resulting in decreased breakdown of amines (such as phenylethylamine) and increased synaptic concentrations