Mechanism of inactivation of monoamine oxidase by trans-2-phenylcyclopropylamine and the structure of the enzyme-inactivator adduct

Research output: Contribution to journalArticlepeer-review

96 Scopus citations

Abstract

Mitochondrial monoamine oxidase was inactivated with 2-[2-14C]phenylcyclopropylamine, dialyzed, and treated with acidic 2,4-dinitrophenylhydrazine. Contrary to the report of Paech et al. (Paech, C., Salach, J.I., and Singer, T.P. (1980) J. Biol. Chem. 255, 2700-2704), the 2,4-dinitrophenylhydrazone obtained was not that of 2-phenylcyclopropanone, but rather of cinnamaldehyde. Furthermore, denaturation of the labeled enzyme in the presence of sodium borohydride resulted in retention of 5.6 times more radioactivity than in its absence. Based on these results, a mechanism of inactivation of monoamine oxidase by 2-phenylcyclopropylamine and the structure of the enzyme-inactivator adduct are proposed.

Original languageEnglish (US)
Pages (from-to)14766-14769
Number of pages4
JournalJournal of Biological Chemistry
Volume258
Issue number24
StatePublished - 1983

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Mechanism of inactivation of monoamine oxidase by trans-2-phenylcyclopropylamine and the structure of the enzyme-inactivator adduct'. Together they form a unique fingerprint.

Cite this