Inactivation of monoamine oxidase B by cis- and trans-5-aminomethyl-3-(4-methoxyphenyl)dihydrofuran-2(3H)-ones Original Research Article

Monoamine oxidase B was previously shown to be inactivated by cis- (3) and trans-5-(aminomethyl)-3-(4-methoxyphenyl)dihydrofuran-2(3H)-one hydrochloride (4) in a time-dependent manner (Ding, Z.; Silverman, R. B. J. Med. Chem. 1992, 35, 885) and to catalyze its oxidative decarboxylation (Silverman, R. B.; Zhou, J. J. P.; Ding, C. Z.; Lu, X. J. Am. Chem. Soc. 1995, 117, 12895). By [14C]-labeling of the aryl methoxyl groups of these two inactivators, it is shown that this is not a mechanism-based inactivation and that multiple enzyme residues are labeled.