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Structural studies on two gamma lactamase enzymes with opposite stereoselectivity
Reference
B15025
Principal Investigator / Supervisor
Professor Jennifer Littlechild
Co-Investigators /
Co-Supervisors
Dr Mikhail Isupov
Institution
University of Exeter
Department
Biosciences
Funding type
Research
Value (£)
222,340
Status
Completed
Type
Research Grant
Start date
01/07/2001
End date
01/07/2004
Duration
36 months
Abstract
This study will 1). solve the structure of a novel (+) gamma lactamase enzyme from a Comomonas acidovorans species. This enzyme is related to a group of proteins that include acetamidase and formamidase; no structural information is currently available for any member of this group; 2). solve the structure of substrate and inhibitor complexes of the enzyme to understand the overall mechanism; 3). characterise active site mutants of the enzyme in regard to their activity and substrate specificity; and 4). initiate structural studies and characterise an unrelated (-) gamma lactamase enzyme from Aureobacterium species that has opposite stereoselectivity for the lactam substrate and shows sequence homology to non-cofactor containing haloperoxidases.
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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