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Study of the novel mechanism of dipyrromethane cofactor assembly in porphobilinogen deaminase

Reference	B08011
Principal Investigator / Supervisor	Professor Peter Shoolingin-Jordan
Co-Investigators / Co-Supervisors
Institution	University of Southampton
Department	Centre for Biological Sciences
Funding type	Research
Value (£)	155,647
Status	Completed
Type	Research Grant
Start date	01/04/1997
End date	01/04/2000
Duration	36 months

Abstract

It has been discovered recently in our laboratory that the dipyrromethane cofactor of porphobilinogen deaminase holoenzyme is not assembled from two individual pyrrole unit binding sequentially to the apoenzyme, as had first been surmised. Instead, the apoenzyme initially reacts with a molecule of the 'tetrapyrrole' product, preformed by active holoenzyme, the two pyrrole rings of the dipyrromethane cofactor arising from fragmentation of this tetrapyrrole precursor. Experiments will be carried out using site-directed mutagenesis, circular dichroism, X-ray crystallography and inhibitors to study this novel cofactor assembly process and to determine the amino acid residues of the apoenzyme that are involved in the recognition and reaction of the tetrapyrrole. The importance of domain 3, to which the cofactor is covalently anchored, will also be investigated by the above techniques.

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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