BBSRC Portfolio Analyser
Award details
The role of the active site metal ions and of a flexible loop in the catalytic mechanism of metallo-beta-lactamases
Reference
BBS/B/05885
Principal Investigator / Supervisor
Professor Gordon Roberts
Co-Investigators /
Co-Supervisors
Dr Christian Damblon
Institution
University of Leicester
Department
Biochemistry
Funding type
Research
Value (£)
185,169
Status
Completed
Type
Research Grant
Start date
20/07/2004
End date
19/07/2007
Duration
36 months
Abstract
Metallo-beta-lactamases are a source of antibiotic resistance, notably due to their ability to hydrolyse carbapenems. This study will provide structural information necessary to understand the catalytic mechanisms of these enzymes. NMR methods will be used (i) to study the binding of the two active-site metal ions in the presence of substrate analogues to enzymes which are activated and inhibited by the binding of the second metal (from A. hydrophila and B. cereus), and (ii) to determine the solution structure of these enzymes in the presence of substrate analogues, with particular reference to the role of a flexible loop near the active site.
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
I accept the
terms and conditions of use
(opens in new window)
export PDF file
back to list
new search