Monoamine oxidase contains a redox-active disulfide

Rona Ruth Ramsay, SO Sablin

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)

Abstract

Mitochondrial monoamine oxidases A and B (MAO A and MAO B) are ubiquitous homodimeric FAD-containing oxidases that catalyze the oxidation of biogenic amines. Both enzymes play a vital role in the regulation of neurotransmitter levels in brain and are of interest as drug targets. However, little is known about the amino acid residues involved in the catalysis. The experiments reported here show that both MAO A and MAO B contain a redox-active disulfide at the catalytic center. The results imply that MAO may be a novel type of disulfide oxidoreductase and open the way to characterizing the catalytic and chemical mechanism of the enzyme.

Original languageEnglish
Pages (from-to)14074-14076
Number of pages3
JournalJournal of Biological Chemistry
Volume273
Publication statusPublished - 5 Jun 1998

Keywords

  • SITE-DIRECTED MUTAGENESIS
  • KINETIC MECHANISM
  • HALF-REACTION
  • INACTIVATION

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