1ksi

From Proteopedia

Revision as of 09:56, 30 October 2007

CRYSTAL STRUCTURE OF A EUKARYOTIC (PEA SEEDLING) COPPER-CONTAINING AMINE OXIDASE AT 2.2A RESOLUTION

Overview

BACKGROUND: Copper-containing amine oxidases catalyze the oxidative, deamination of primary amines to aldehydes, in a reaction that requires, free radicals. These enzymes are important in many biological processes, including cell differentiation and growth, would healing, detoxification, and signalling. The catalytic reaction requires a redox cofactor, topa, quinone (TPQ), which is derived by post-translational modification of an, invariant tyrosine residue. Both the biogenesis of the TPQ cofactor and, the reaction catalyzed by the enzyme require the presence of a copper atom, at the active site. The crystal structure of a prokaryotic copper amine, oxidase from E. coli (ECAO) has recently been reported. RESULTS: The first, structure of a eukaryotic (pea seedling) amine oxidase (PSAO) has ... [(full description)]

About this Structure

1KSI is a [Single protein] structure of sequence from [Pivum sativum] with NAG, CU and MN as [ligands]. Active as [Amine oxidase (copper-containing)], with EC number [1.4.3.6]. Structure known Active Sites: ACA and ACB. Full crystallographic information is available from [OCA].

Reference

Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 A resolution., Kumar V, Dooley DM, Freeman HC, Guss JM, Harvey I, McGuirl MA, Wilce MC, Zubak VM, Structure. 1996 Aug 15;4(8):943-55. PMID:8805580

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