1d6y
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CRYSTAL STRUCTURE OF E. COLI COPPER-CONTAINING AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE AND COMPLEXED WITH NITRIC OXIDE.
OverviewOverview
X-ray crystal structures of three species related to the oxidative half of, the reaction of the copper-containing quinoprotein amine oxidase from, Escherichia coli have been determined. Crystals were freeze-trapped either, anaerobically or aerobically after exposure to substrate, and structures, were determined to resolutions between 2.1 and 2.4 angstroms. The, oxidation state of the quinone cofactor was investigated by single-crystal, spectrophotometry. The structures reveal the site of bound dioxygen and, the proton transfer pathways involved in oxygen reduction. The quinone, cofactor is regenerated from the iminoquinone intermediate by hydrolysis, involving Asp383, the catalytic base in the reductive half-reaction., Product aldehyde inhibits the hydrolysis, making release of product the, rate-determining step of the reaction in the crystal.
About this StructureAbout this Structure
1D6Y is a Single protein structure of sequence from Escherichia coli with CU, CA, HY1, NO, PEA and GOL as ligands. Active as Amine oxidase (copper-containing), with EC number 1.4.3.6 Full crystallographic information is available from OCA.
ReferenceReference
Visualization of dioxygen bound to copper during enzyme catalysis., Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE, Science. 1999 Nov 26;286(5445):1724-8. PMID:10576737
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