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Penicillin acylase - its mechanism and processing investigated by protein engineering
Reference
B06005
Principal Investigator / Supervisor
Professor Keith Wilson
Co-Investigators /
Co-Supervisors
Professor George Dodson
Institution
University of York
Department
Chemistry
Funding type
Research
Value (£)
128,321
Status
Completed
Type
Research Grant
Start date
01/10/1996
End date
01/10/1999
Duration
36 months
Abstract
Penicillin acylase (PA) is an enzyme of considerable industrial interest, used in the production of semi-synthetic penicillins. We have determined its 3-D crystal structure at 1.9 Angstroms resolution. This has revealed a novel mechanism for the activation of the catalytic nucleophile, the molecular basis of product inhibition and the presence of a calcium-binding site which may be important for stability and folding. This programme of research builds on this knowledge to explore and exploit some of the questions that the structure has raised regarding post-translational processing, substrate specificity and evolutionary and biochemical relationships with other proteins which have been discovered to share structural and mechanistic similarities.
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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