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Mechanism of enzymatic extradiol aromatic ring cleavage reactions
Reference
B04835
Principal Investigator / Supervisor
Professor Timothy Bugg
Co-Investigators /
Co-Supervisors
Institution
University of Southampton
Department
Sch of Chemistry
Funding type
Research
Value (£)
128,365
Status
Completed
Type
Research Grant
Start date
15/01/1996
End date
07/05/1999
Duration
40 months
Abstract
The objective of the proposed research is to elucidate the kinetic and chemical mechanism of extradiol dioxygenase MhpB and hydrolase MhpC of the phenylproprionate catabolic pathway of Escherichia coli. Pre-steady state kinetics will be used to elucidate the kinetic mechanism of both enzymes and the existence of kinetically competent intermediates. Kinetic and chemical trapping methods will be used to investigate the existence of an acyl enzyme intermediate on the MhpC reaction. The absolute stereochemistry of the MhpC reaction will be elucidated by 3H labelling and enzymatic degradation. The mechanism of the corresponding dioxygenase and hydrolase enzymes on the biphenyl catabolic pathway of Pseudomonas LB400 will be examined by 18O and 2H labelling methods.
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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