Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective.
作者： Brian J. Brazeau , Bryan J. Johnson , Carrie M. Wilmot
DOI: 10.1016/J.ABB.2004.03.034
关键词: Biogenesis 、 Active site 、 Quinone 、 Enzyme activator 、 Catalysis 、 Enzyme 、 Cofactor 、 Amine gas treating 、 Photochemistry 、 Chemistry 、 Combinatorial chemistry
摘要: This review will focus on how X-ray crystallographic studies of copper-containing amine oxidases have complemented the solution, kinetic, and spectroscopic research this ubiquitous class enzymes. These enzymes not only contain a copper ion at active site, but also unique organic cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ), which is absolutely required for catalysis. Structural data shed light catalytic mechanism enzyme, converts primary amines, using molecular oxygen, to aldehydes, ammonia, hydrogen peroxide, biogenesis cofactor. The cofactor derived from tyrosine in enzyme amino acid sequence requires addition copper(II) oxygen self-processing event.
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