Inhibition of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine metabolic activity of porcine FAD-containing monooxygenase by selective monoamine oxidase-B inhibitors

Ru Feng Wu, Yoshiyuki Ichikawa

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

The MPTP metabolic activity of porcine FAD-containing monooxygenase (FMO) (EC 1.14.13.8) was inhibited considerably by deprenyl and pargyline, selective MAO-B inhibitors, and they showed typical competitive inhibition. Deprenyl and pargyline, amine derivatives were also examined as to whether they are substrates for the FMO. It was found that deprenyl and pargyline are excellent substrates for the FMO. The Ki and Km values of deprenyl and pargyline for the FMO are 14 μM and 9 μM, and 14.3 μM and 11.6 μM, at pH 8.0 and 25°C, respectively.

Original languageEnglish (US)
Pages (from-to)145-148
Number of pages4
JournalFEBS Letters
Volume358
Issue number2
DOIs
StatePublished - Jan 23 1995

Keywords

  • Deprenyl
  • FAD-containing monooxygenase
  • Monoamine oxidase-B inhibitor
  • Pargyline

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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