Monoamine oxidase (MAO) is an enzyme of the mitochondrial outer membrane and catalyzes the oxidative deamination of biogenic amines throughout the body. MAO is critical in the neuronal metabolism of catecholamine and indolamine transmitters. Cultured skin fibroblasts show both MAO-A and MAO-B and both MAOs differ in molecular structure. MAO-A, the primary type in fibroblasts, preferentially degrades serotonin and norepinephrine. Only MAO-B is present in platelets and only MAO-A is present in trophoblasts. MAO-B, the primary type found not only in platelets but also in the brain of man and other primates, preferentially degrades phenylethylamine and benzylamine. MAO has been of particular interest to psychiatry and genetics because of the suggestion that low activity is a 'genetic marker' for schizophrenia. The genes which encode MAO-A and MAO-B map to human chromosome Xp11.23.
