Localization, purification and substrate specificity of monoamine oxidase.

Bovine kidney monoamine oxidase (amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4) has been purified to one band on disc electrophoresis, and is shown to be localized in the intra- and extramitochondrial membrane. Kinetic models have been used to determine the effect of different substances on the enzyme activity. This enzyme shows a very high substrate specificity. It is suggested that phenol ring and one hydrogen atom each on the methylene and amine groups are responsible for the enzyme activity. N-methylbenzylamine exhibits a homotropic negative cooperative effect which is also supported by the n and Rs values. Benzylhydrazine is apparently a good substrate unlike phenylhydrazine, semicarbazide, harmaline and alpha- and beta-naphthol which show an inhibitory effect on the enzyme activity. Methylamine has no effect. It is suggested that the enzyme may have different sites or different conformations for different substrates. The results of this communication demonstrate bovine kidney monoamine oxidase to be different from monoamine oxidase from other sources.