Publication Date:
1999-11-27
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilmot, C M -- Hajdu, J -- McPherson, M J -- Knowles, P F -- Phillips, S E -- New York, N.Y. -- Science. 1999 Nov 26;286(5445):1724-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Astbury Centre for Structural Molecular Biology, School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10576737" target="_blank"〉PubMed〈/a〉
Keywords:
Aerobiosis
;
Amine Oxidase (Copper-Containing)/*chemistry/*metabolism
;
Anaerobiosis
;
Aspartic Acid/chemistry/metabolism
;
Binding Sites
;
Catalysis
;
Copper/*metabolism
;
Crystallography, X-Ray
;
Dihydroxyphenylalanine/*analogs & derivatives/chemistry/metabolism
;
Dimerization
;
Electrons
;
Escherichia coli/enzymology
;
Hydrogen Bonding
;
Nitric Oxide/metabolism
;
Oxidation-Reduction
;
Oxygen/*metabolism
;
Phenethylamines/metabolism
;
Protein Conformation
;
Protein Structure, Secondary
;
Protons
;
Spectrum Analysis
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
