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Award details
The mechanism, specificity and inhibition of enzymes belonging to the xanthine oxidase family
Reference
BBS/E/J/00004135
Principal Investigator / Supervisor
Professor David John Lowe
Co-Investigators /
Co-Supervisors
Institution
John Innes Centre
Department
John Innes Centre Department
Funding type
Research
Value (£)
115,489
Status
Completed
Type
Institute Project
Start date
01/04/2000
End date
31/03/2004
Duration
48 months
Abstract
To understand in terms of biomolecular structure, how enzymes of the xanthine oxidase family function at the atomic, molecular and physiological levels, how their specificity is controlled and how new inhibitors can be designed. This will give important insights into modifying their reactivity in order to catalyse new reactions, with possible uses in manufacturing and waste treatment, and into making inhibitors, with a view to using these as pharmaceuticals. Enzymes of the family hydroxylate a wide variety of compounds at a site determined by the amino acid residues in the oxidisible-substrate binding pocket. They are also causally implicated in a number of pathological conditions and in drug metabolism.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
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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