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Mechanism of enzymatic extradiol aromatic ring cleavage reactions

ReferenceB04835
Principal Investigator / Supervisor Professor Timothy Bugg
Co-Investigators /
Co-Supervisors
Institution University of Southampton
DepartmentSch of Chemistry
Funding typeResearch
Value (£) 128,365
StatusCompleted
TypeResearch Grant
Start date 15/01/1996
End date 07/05/1999
Duration40 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 TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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