ABSTRACT
Mitochondrial monoamine oxidase monoamine oxidase (MAO) is a tightly bound component of the outer membrane, which occurs in two forms: A and B. The two differ in substrate specificity, although there is some overlap and some substrates are processed by both forms. The most widely used reversible MAO inhibitors are amphetamines and tricyclic antidepressants. One of the most potent reversible inhibitors of MAOs is 3-[4-(3-cyanophenylme-thoxy)phenyl]-5-(methoxymethyl)-2-oxazolidinone. A particularly fascinating aspect of the reaction of reversible inhibitors with MAO-B concerns the different kinetics observed with benzylamine and phenylethylamine as substrates. Among irreversible inhibitors of MAO, those containing an acetylenic linkage in the ß position to the amine have been most widely investigated from the biochemical standpoint and have received the widest attention as potential or actual therapeutic agents. The reactivity of MAO-A and MAO-B, respectively, with suicide inhibitors and substrates may be a basis for predicting the structural basis of differences between the two forms.
