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Conformational changes in porphobilinogen deaminase during polypyrrole chain elongation

Reference	B03881
Principal Investigator / Supervisor	Professor Peter Shoolingin-Jordan
Co-Investigators / Co-Supervisors
Institution	University of Southampton
Department	Centre for Biological Sciences
Funding type	Research
Value (£)	202,686
Status	Completed
Type	Research Grant
Start date	01/10/1995
End date	01/10/1998
Duration	36 months

Abstract

Two possible models by which the porphobilinogen deaminase structure adjusts to the elongation of the polypyrrole chain during the polymerisation of the pyrrole, porphobilinogen, will be investigated. These are (i) the sliding polymer model involving translocation of the growing polymer through the catalytic site and (ii) the sliding active site model involving translocation of the catalytic site along the growing polymer. These models will be investigated by the following approaches; a) chemical synthesis of substrate analogues and inhibitors; b) chemical modification of the enzyme at different stages of the polymerisation; c) mutagenesis of the interdomain boundary residues to identify key residues; d) the use of fluorescence energy transfer techniques to determine distance changes between protein domains during polymer chain elongation; e) supporting X-ray crystallography of mutants and enzyme intermediate complexes.

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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