Amine oxidase copper-containing 2 (AOC2)

Amine oxidase copper-containing 2 (AOC2) is an enzyme that catalyzes the oxidative deamination of primary amines to corresponding aldehydes, generating hydrogen peroxide and ammonia as by-products[1][2][3]. AOC2 is characterized by a copper ion and topaquinone (TPQ) cofactor at its active site and shares high sequence similarity with other copper amine oxidases[1][2]. In humans, AOC2 is thought to play a critical role in the retina, modulating neurotransmitter levels such as dopamine, histamine, and putrescine, and may be implicated in hereditary ocular disease[2][3]. Structurally, the enzyme operates as a dimer with a buried catalytic site, typical of the copper amine oxidase family. While this protein family (including AOC1 and AOC3) is a focus for drug design (especially AOC3/VAP-1 in inflammation and cancer), AOC2-specific physiological functions and clinical inhibitors are less well-characterized. Potential therapeutic challenges include the risk of cross-inhibition with other copper amine oxidases[3].

Other names

Amine oxidase [copper-containing] 2Retina-specific copper amine oxidaseSemicarbazide-sensitive amine oxidaseRAOSSAODAO2

Mechanism-based inhibition via covalent interaction with the TPQ cofactor (main for family, for AOC3 and by homology AOC2) Non-covalent blocking of access to the active site (for imidazole derivatives)