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Study of the mechanism of pyrrole polymerisation with human mutant enzymes that accumulate stable catalytic intermediates
Reference
B17399
Principal Investigator / Supervisor
Professor Peter Shoolingin-Jordan
Co-Investigators /
Co-Supervisors
Institution
University of Southampton
Department
Centre for Biological Sciences
Funding type
Research
Value (£)
186,213
Status
Completed
Type
Research Grant
Start date
01/07/2002
End date
31/12/2005
Duration
42 months
Abstract
The mechanism by which the pyrrole, porphobilinogen, is polymerised enzymically to give preuroporphyrinogen, the tetrapyrrole intermediate of haem synthesis, will be investigated using two naturally occurring human mutants of porphobilinogen deaminase that are defective in the chain extension mechanism. The mutants will be isolated as their stable mono, di, tri and tetrapyrrole enzyme-intermediate complexes and the individual X-ray structures will be solved. The structures will reveal the precise detail of the stepwise mechanism of tetrapyrrole chain synthesis. Other naturally occurring human mutants will be employed to investigate the assembly of the novel dipyrromethane cofactor that acts as the primer for tetrapyrrole chain synthesis.
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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