1spu

From Proteopedia

Revision as of 13:59, 30 October 2007

STRUCTURE OF OXIDOREDUCTASE

Overview

The crystal structure of the complex between the copper amine oxidase from, Escherichia coli (ECAO) and a covalently bound inhibitor, 2-hydrazinopyridine, has been determined to a resolution of 2.0 A. The, inhibitor covalently binds at the 5 position of the quinone ring of the, cofactor, 2,4,5-trihydroxyphenylalaninequinone (TPQ). The inhibitor, complex is analogous to the substrate Schiff base formed during the, reaction with natural monoamine substrate. A proton is abstracted from a, methylene group adjacent to the amine group by a catalytic base during the, reaction. The inhibitor, however, has a nitrogen at this position, preventing proton abstraction and trapping the enzyme in a covalent, complex. The electron density shows this nitrogen is hydrogen bonded to, the side chain of ... [(full description)]

About this Structure

1SPU is a [Single protein] structure of sequence from [Escherichia coli] with CU and CA as [ligands]. Active as [Amine oxidase (copper-containing)], with EC number [1.4.3.6]. Structure known Active Sites: CUA, CUB, M1A, M1B, M2A and M2B. Full crystallographic information is available from [OCA].

Reference

Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction., Wilmot CM, Murray JM, Alton G, Parsons MR, Convery MA, Blakeley V, Corner AS, Palcic MM, Knowles PF, McPherson MJ, Phillips SE, Biochemistry. 1997 Feb 18;36(7):1608-20. PMID:9048544

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