Monoamine oxidase: to B or not to B?
That the enzyme, monoamine oxidase (E.C. 1.4.3.4. amine: O2 oxidoreductase, MAO) exists in multiple forms was first suggested by Johnston (1) who studied the effects of the irreversible inhibitor clorgyline on MAO. It has been proposed that MAO can be classified into two types, A and B, according to their inhibitor sensitivity and substrate specificity. Type A MAO was found to be solely responsible for the deamination of 5-hydroxytryptamine (5-HT) and shows high sensitivity to clorgyline, while type B MAO metabolizes 2-phenethylamine (PEA) and benzylamine (BA) and is less sensitive to clorgyline. Subsequently, it was shown that type B MAO is highly sensitive to the irreversible inhibitor deprenyl (2). Recently, the "multiple forms" concept has been questioned (3-5) mainly because of increasing evidence which is contradictory to some earlier findings. As an alternative, another hypothesis was put forward insinuating that MAO is an enzyme with multiple binding sites but only one molecular entity (3,4,6,7). This account will focus on some experimental findings accumulated mainly since 1978 and which, although equivocal, strongly support the "one molecular entity" hypothesis of MAO.
D000818:Animals; D006801:Humans; D008928:Mitochondria / Q000201:enzymology; D008995:Monoamine Oxidase / Q000032:analysis* / Q000302:isolation & purification; D010743:Phospholipids / Q000494:pharmacology; D013379:Substrate Specificity
D010743:Phospholipids; D008995:Monoamine Oxidase