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Catalytic mechanism and protein engineering of the catechol dioxygenases
Reference
B16501
Principal Investigator / Supervisor
Professor Timothy Bugg
Co-Investigators /
Co-Supervisors
Institution
University of Warwick
Department
Chemistry
Funding type
Research
Value (£)
119,972
Status
Completed
Type
Research Grant
Start date
24/08/2002
End date
24/08/2004
Duration
24 months
Abstract
The objective of this proposed research is to elucidate the acid/base catalysis of the non-haem iron(II)-dependent extradiol dioxygenases, using site-directed mutagenesis. Biomimetic studies of extradiol catechol cleavage show a requirement for a catalytic base, proposed to be His-179 in E. coli MhpB, and a proton donor, proposed to be His-115 in MhpB. The roles of these residues in acid/base catalysis in Class II and III extradiol dioxygenases will be studied by site-directed mutagenesis. The final step of the reaction, lactone hydrolysis, will be studied in isolation. Directed evolution will be used to change the selectivity of an intradiol dioxygenase, catechol 1,2-dioxygenase, to extradiol cleavage.
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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