Award details

Structure and mechanism of the C-C hydrolases: investigation of a non-nucleophilic mechanism

Reference	B20468
Principal Investigator / Supervisor	Professor Stephen Wood
Co-Investigators / Co-Supervisors	Dr Alun Coker, Professor Jon Cooper
Institution	University of Southampton
Department	Centre for Biological Sciences
Funding type	Research
Value (£)	122,516
Status	Completed
Type	Research Grant
Start date	01/09/2003
End date	31/08/2005
Duration	24 months

Abstract

We have recently solved the X-ray structure of a complex between C-C hydrolase enzyme MhpC and the inhibitor 2,6-diketo-nona-1,9-dioic acid (DKNDA) at 2.8 A resolution, which has identified a number of amino acid residues (Ser110, His263, Asp235, His114, Ser40, Arg188) that are likely to contribute to substrate binding and catalysis. Previous mechanistic studies have implicated a non-nucleophilic role for the serine triad in this enzyme, a major departure in function for the serine hydrolases. We propose to investigate the role of Ser110 and other active site residues in MhpC, and related hydrolase BphD, by site-directed mutagenesis. The role of Ser110 in BphD will be examined using a Hammett plot approach. (Joint with grant number 20467).

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

Associated awards:

B20467 Structure and mechanism of the C-C hydrolases: investigation of a non-nucleophilic mechanism

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