Inactivation of monoamine oxidase B by cis- and trans-5-aminomethyl-3-(4-methoxyphenyl)dihydrofuran-2(3H)-ones.
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.
Lu
X
X
Department of Chemistry, Northwestern University, Evanston, IL 60208-3113, USA.
Silverman
R B
RB
D015107:4-Butyrolactone / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism / Q000494:pharmacology; D002250:Carbon Radioisotopes; D004789:Enzyme Activation; D008995:Monoamine Oxidase / Q000187:drug effects* / Q000378:metabolism; D008996:Monoamine Oxidase Inhibitors / Q000138:chemical synthesis* / Q000378:metabolism / Q000494:pharmacology*
C116522:5-(aminomethyl)-3-(4-methoxyphenyl)dihydrofuran-2(3H)-one; D002250:Carbon Radioisotopes; D008996:Monoamine Oxidase Inhibitors; D008995:Monoamine Oxidase; D015107:4-Butyrolactone