Article
Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue.
The Biochemical journal - 1 Aug 2002
Saysell Colin G, Tambyrajah Winston S, Murray Jeremy M, Wilmot Carrie M, Phillips Simon E V, McPherson Michael J, Knowles Peter F
Abstract excerpt
Copper amine oxidases are homodimeric enzymes containing one Cu(2+) ion and one 2,4,5-trihydroxyphenylalanine quinone (TPQ) per monomer. Previous studies with the copper amine oxidase from Escherichia coli (ECAO) have elucidated the structure of the active site and established the importance in catalysis of an active-site base, Asp-383. To explore the early interactions of substrate with enzyme, we have used...
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