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Molecular and chemical mechanism underlying human CYP17 catalysis

ReferenceC15658
Principal Investigator / Supervisor Dr P Lee-Robichaud
Co-Investigators /
Co-Supervisors
Institution University of Sheffield
DepartmentChemistry
Funding typeResearch
Value (£) 177,252
StatusCompleted
TypeResearch Grant
Start date 01/02/2002
End date 01/02/2005
Duration36 months

Abstract

CYP17 is a microsomal protein that is involved in the biosynthesis of glucocorticoids and sex hormones. To achieve this CYP17 catalyses two different generic reactions at the same active site; hydroxylation and carbon-carbon bond cleavage. Both activities require the presence of a redox protein, NADPH-cytochrome P450 reductase, but expression of the second activity is dependent on a third microsomal protein, cytochrome b5. PCR-site-directed mutagenesis, recombinant protein technology, chemical synthesis, 19F-NMR and a variety of biophysical techniques will be used to characterise the binding interaction between b5 and CYP17 and to delineate the molecular mechanism by which b5 subtly modulates the catalytic properties of human CYP17.

Summary

unavailable
Committee Closed Committee - Biochemistry & Cell Biology (BCB)
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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