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Structure and mechanism of E. coli MhpC; a C-C hydrolase involved in bacterial degradation of aromatic compounds

Reference	B13775
Principal Investigator / Supervisor	Professor Stephen Wood
Co-Investigators / Co-Supervisors	Professor Timothy Bugg, Professor Jon Cooper
Institution	University of Southampton
Department	Centre for Biological Sciences
Funding type	Research
Value (£)	130,573
Status	Completed
Type	Research Grant
Start date	01/10/2000
End date	30/09/2002
Duration	24 months

Abstract

We have recently solved the X-ray structure of the Mhpc hydrolase by MAD methods using seleno-methionine. We now propose to refine the molecular model and define the active site structure by X-ray analysis of enzyme-substrate analogue complexes. This will guide production and kinetic evaluation of active site mutants in order to probe the enzyme mechanism. While some evidence suggests that this rather rare C-C bond cleavage reaction involves an active site serine nucleophile as in serine proteases, it has not proved possible to trap an acyl enzyme intermediate and other data favour a gem-diol transition state. The structure will also guide mutagenesis to engineer enzymes with novel synthetic capabilities.

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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