Structures and mechanism of the monoamine oxidase family

Helena Gaweska, Paul F. Fitzpatrick

Research output: Contribution to journalReview articlepeer-review

77 Scopus citations

Abstract

Members of the monoamine oxidase family of flavoproteins catalyze the oxidation of primary and secondary amines, polyamines, amino acids, and methylated lysine side chains in proteins. The enzymes have similar overall structures, with conserved flavin adenine dinucleotide (FAD)-binding domains and varied substrate-binding sites. Multiple mechanisms have been proposed for the catalytic reactions of these enzymes. The present review compares the structures of different members of the family and the various mechanistic proposals.

Original languageEnglish (US)
Pages (from-to)365-377
Number of pages13
JournalBiomolecular Concepts
Volume2
Issue number5
DOIs
StatePublished - Oct 1 2011

Keywords

  • L-amino acid oxidase
  • enzyme mechanism
  • flavoproteins
  • lysine-specific demethylase
  • monoamine oxidase
  • polyamine oxidase
  • protein structure
  • spermine oxidase

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Cellular and Molecular Neuroscience

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