N-(1-Methyl)cyclopropylbenzylamine: A novel inactivator of mitochondrial monoamine oxidase

Richard B. Silverman*, Stephen J. Hoffman

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

43 Scopus citations

Abstract

N-(1-Methyl)cyclopropylbenzylamine was synthesized and shown to inactivate pig liver mitochondrial monoamine oxidase. Inactivation is time-dependent, concentration dependent, protected by the substrate and product of the enzyme, and is not reversed by exhaustive dialysis. Unlike N-cyclopropylbenzylamine, the adduct formed between N-(1-methyl)cyclopropylbenzylamine and monoamine oxidase is stable to treatment with benzylamine. A mechanism for the inactivation is proposed.

Original languageEnglish (US)
Pages (from-to)1396-1401
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume101
Issue number4
DOIs
StatePublished - Aug 31 1981

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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