The Active Site Base Controls Cofactor Reactivity in Escherichia coli Amine Oxidase: X-ray Crystallographic Studies with Mutational Variants

Amine oxidases utilize a proton abstraction mechanism following binding of the amine substrate to the C5 position of the cofactor, the quinone form of trihydroxyphenylalanine (TPQ). Previous work [Wilmot, C. M., et al. (1997) Biochemistry 36, 1608−1620] has shown that Asp383 in Escherichia coli amin...

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Veröffentlicht in:	Biochemistry (Easton) 1999-06, Vol.38 (26), p.8217-8227
Hauptverfasser:	Murray, Jeremy M, Saysell, Colin G, Wilmot, Carrie M, Tambyrajah, Winston S, Jaeger, Joachim, Knowles, Peter F, Phillips, Simon E. V, McPherson, Michael J
Format:	Artikel
Sprache:	eng
Schlagworte:	Amine Oxidase (Copper-Containing) - antagonists & inhibitors Amine Oxidase (Copper-Containing) - chemistry Amine Oxidase (Copper-Containing) - genetics Asparagine - genetics Aspartic Acid - genetics Binding Sites - genetics Crystallization Crystallography, X-Ray Enzyme Activation - genetics Enzyme Inhibitors - chemistry Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Glutamic Acid - genetics Kinetics Mass Spectrometry Metals - chemistry Models, Molecular Mutagenesis, Site-Directed Pyridones - chemistry Spectrophotometry, Ultraviolet
Online-Zugang:	Volltext
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