Article
Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.
Biochemistry - 30 Oct 2001
Murray J M, Kurtis C R, Tambyrajah W, Saysell C G, Wilmot C M, Parsons M R, Phillips S E, Knowles P F, McPherson M J
Abstract excerpt
Copper amine oxidases are homodimeric enzymes that catalyze two reactions: first, a self-processing reaction to generate the 2,4,5-trihydroxyphenylalanine (TPQ) cofactor from an active site tyrosine by a single turnover mechanism; second, the oxidative deamination of primary amine substrates with the production of aldehyde, hydrogen peroxide, and ammonia catalyzed by the mature enzyme. The importance of active...
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