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

• Published in: Archives of Biochemistry and Biophysics Vol. 428; no. 1; pp. 22 - 31
• Main Authors: Brazeau, Brian J., Johnson, Bryan J., Wilmot, Carrie M.
• Format: Book Review Journal Article
• Language: English
• Published: United States Elsevier Inc 01.08.2004
• Subjects: Amine Oxidase (Copper-Containing) - chemistry; Amine Oxidase (Copper-Containing) - metabolism; Catalysis; Coenzymes - chemistry; Coenzymes - metabolism; Copper metalloenzyme; Copper-containing amine oxidases; Dihydroxyphenylalanine - analogs & derivatives; Dihydroxyphenylalanine - chemistry; Dihydroxyphenylalanine - metabolism; Enzyme Activation; Models, Molecular; Oxidation-Reduction; Oxygen activation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Quinone cofactor; Species Specificity; Structure-Activity Relationship; TPQ; X-ray crystallography; X-ray crystallography; Copper metalloenzyme; Oxygen activation; TPQ; Quinone cofactor; Copper-containing amine oxidases
• ISSN: 0003-9861; 1096-0384
• DOI: 10.1016/j.abb.2004.03.034

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.