Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective

Brian J. Brazeau, Bryan J. Johnson, Carrie M. Wilmot

Research output: Contribution to journalShort surveypeer-review

96 Scopus citations

Abstract

This review will focus on how X-ray crystallographic studies of copper-containing amine oxidases have complemented the solution, kinetic, and spectroscopic research on this ubiquitous class of enzymes. These enzymes not only contain a copper ion at the active site, but also a unique organic cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ), which is absolutely required for catalysis. Structural data have not only shed light on the catalytic mechanism of the enzyme, which converts primary amines, using molecular oxygen, to aldehydes, ammonia, and hydrogen peroxide, but also on biogenesis of the cofactor. The cofactor is derived from a tyrosine in the enzyme amino acid sequence and requires only the addition of copper(II) and molecular oxygen in a self-processing event.

Original languageEnglish (US)
Pages (from-to)22-31
Number of pages10
JournalArchives of Biochemistry and Biophysics
Volume428
Issue number1
DOIs
StatePublished - Aug 1 2004

Keywords

  • Copper metalloenzyme
  • Copper-containing amine oxidases
  • Oxygen activation
  • Quinone cofactor
  • TPQ
  • X-ray crystallography

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