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Transition states and substrate switching in metallophosphatases

Reference	C18734
Principal Investigator / Supervisor	Professor Nicholas Williams
Co-Investigators / Co-Supervisors	Dr Ihtshamul Haq, Dr P Lee-Robichaud
Institution	University of Sheffield
Department	Chemistry
Funding type	Research
Value (£)	188,828
Status	Completed
Type	Research Grant
Start date	29/09/2003
End date	28/09/2006
Duration	36 months

Abstract

The serine and threonine phosphatases are a family of dinuclear metallophosphatases with very similar active sites. To be able to understand their extraordinary catalytic efficiency, we propose to study the transition state for monoester hydrolysis catalysed by PP1 by kinetically characterising the hydrolysis of small homologous substrates and constructing LFERs. Comparing the results with similar analysis of mutants will shed light on the roles of the key active site. We shall develop and use a novel assay based on ITC, which allows continuous reaction monitoring using only the enthalpy change of the reaction. We shall search for diesterase activity with both wild type and mutants, and similarly characterise the transition state.

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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