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Steric course of 5-aminolevulinic acid synthase using chiral substrates

Reference	B09443
Principal Investigator / Supervisor	Professor Peter Shoolingin-Jordan
Co-Investigators / Co-Supervisors
Institution	University of Southampton
Department	Centre for Biological Sciences
Funding type	Research
Value (£)	187,352
Status	Completed
Type	Research Grant
Start date	01/04/1998
End date	01/04/2001
Duration	36 months

Abstract

Using chircal R-methylamine and S-methylamine as substrates for recombinant of 5- aminolevulinic acid synthase, it is proposed to elucidate the stereochemical course of the condensation and decarboxy-lation steps of the reaction catalysed by the enzyme and to determine which of the two steps contributes to the overall inversion of configuration during the enzymic synthesis of 5-aminolevulinic acid. The stereochemical course of the 5-aminolevulinic acid synthase mechanism will also be studied using several active site- directed histidine mutants of the enzyme designed to be unable to catalyse decarboxylation and therefore able to synthesise 5-aminolevulinic acid from methylamine but not from the natural substrate glycine. Spectroscopic intermediates of the reaction catalysed by wild-type and mutant enzymes with glycine and methylamine as substrates will be characterised using time resolved uv/vis spectroscopy.

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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