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Characterising the active site of pyrophosphate: fructose 6-phosphate 1-phosphotransferase from plants
Reference
C01603
Principal Investigator / Supervisor
Dr Nicholas Kruger
Co-Investigators /
Co-Supervisors
Institution
University of Oxford
Department
Plant Sciences
Funding type
Research
Value (£)
148,735
Status
Completed
Type
Research Grant
Start date
21/10/1994
End date
31/07/1999
Duration
57 months
Abstract
The aim of this work is to elucidate the reaction mechanism of pyrophosphate: fructose 6-phosphate 1-phosphotransferase (PFP). cDNA constructs encoding the two subunits of potato PFP will be expressed in E. coli. The influence of both chemical modification and site-directed mutagenesis on the kinetic and physical properties of recombinant PFP will be used to address three important considerations. First, the relative roles of the distinct alpha and beta subunits of PFP in catalysis and activation by fructose 2,6- bisphosphate will be established. Secondly, the identity of specific residues at the active-site and their contribution to substrate binding and catalysis will be determined. Thirdly, residues involved in the binding of fructose 2,6-bisphosphate will be identified and the contribution of each to enzyme activation will be quantified.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
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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