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

Xingliang Lu, Richard B. Silverman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


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. Copyright (C) 1998 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)1851-1856
Number of pages6
JournalBioorganic and Medicinal Chemistry
Issue number10
StatePublished - Oct 1998


  • 2-Mercaptoethanol
  • Dihydrofuranone
  • Inactivation
  • Mechanism-based inactivation
  • Monoamine oxidase

ASJC Scopus subject areas

  • Drug Discovery
  • Molecular Medicine
  • Molecular Biology
  • Biochemistry
  • Clinical Biochemistry
  • Pharmaceutical Science
  • Organic Chemistry


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