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Quinoenzyme engineering: the copper amine oxidase from Escherichia coli

Reference	B04841
Principal Investigator / Supervisor	Professor Michael McPherson
Co-Investigators / Co-Supervisors	Professor Peter Knowles, Professor Simon Phillips
Institution	University of Leeds
Department	Inst of Molecular & Cellular Biology
Funding type	Research
Value (£)	159,222
Status	Completed
Type	Research Grant
Start date	01/05/1996
End date	01/05/1999
Duration	36 months

Abstract

Copper amine oxidase are ubiquitous and act as regulators of developmental processes through the oxidation of a range of biogenic amines via free radical intermediates. These dimeric quinoenzymes contain one copper atom and an amino acid-derived trihydroxyphenylalanine quinone cofactor per subunit. We have now determined, by X-ray crystallography, the first 3D structure of a bacterial amine oxidase (manuscript in preparation for Science) and we therefore have a lead position for exploitation of this structural knowledge in an internationally competitive field of biocatalysis. We propose a programme of protein engineering, spectroscopy and steady state kinetic characterisation of the wild type and variant forms of E. coli copper amine oxidase to address the catalytic mechanism, substrate stereoselectivity, inter-subunit communication and domain structure.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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