Kinetics of monoamine oxidase (MAO) catalyzed dehydrogenation of neurotropic analogues of biogenic monoamines in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine series were studied. It is shown that methyl substitution in the phenyl ring increases significantly the enzyme-substrate affinity, but the substituent's effect on the catalytic stage largely depends upon its position in the ring. o- and m-Methyl derivatives were preferably oxidized by B type of MAO, whereas p-total derivative was oxidized by B type as well as by A type of the enzyme. In the course of the oxidation reactions MAO is irreversibly inhibited by the dihydropyridinium product of the reaction, particularly in case of methyl derivatives. The significant and structure-dependent inhibition of the enzyme might be responsible for the differences in neurotropic properties of the above substrate homologues.