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Mechanistic studies on human kynureninase
Reference
B18082
Principal Investigator / Supervisor
Dr Nigel Botting
Co-Investigators /
Co-Supervisors
Professor Garry Taylor
Institution
University of St Andrews
Department
Biology
Funding type
Research
Value (£)
131,276
Status
Completed
Type
Research Grant
Start date
01/10/2002
End date
01/10/2004
Duration
24 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 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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