Award details

Mechanistic studies on human kynureninase

ReferenceB18082
Principal Investigator / Supervisor Dr Nigel Botting
Co-Investigators /
Co-Supervisors
Professor Garry Taylor
Institution University of St Andrews
DepartmentBiology
Funding typeResearch
Value (£) 131,276
StatusCompleted
TypeResearch Grant
Start date 01/10/2002
End date 01/10/2004
Duration24 months

Abstract

The aim of the study is to investigate the chemical mechanism of the human form of kynureninase, a PLP dependent enzyme which catalyses the hydrolytic cleavage of the 3-hydroxykynurenine to give L-alanine and 3-hydroxyanthranilic acid. The enzyme plays a key regulatory role in the kynurenine pathway of tryptophan metabolism and is a potential target for drug action. The cloned human enzyme will be examined by a combination of structural (protein crystallography) and kinetic methods (isotope effect studies). The role of a newly discovered regulatory binding site on the enzyme will be explored. Novel inhibitors for the enzyme will be prepared as potential neuroprotective drugs.

Summary

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