Details of Grant 

EPSRC Reference:	GR/J00311/01
Title:	X-RAY STRUCTURE OF E.COLI 5-AMINOLAEVULINATE DEHYDRATASE
Principal Investigator:	Cooper, Professor J
Other Investigators:	Jordan, Professor P Wood, Professor SP Shoolingin-Jordan, Professor P
Researcher Co-Investigators:
Project Partners:
Department:	Unknown
Organisation:	Birkbeck College
Scheme:	Standard Research (Pre-FEC)
Starts:	01 October 1993	Ends:	31 March 1996	Value (£):	120,449
EPSRC Research Topic Classifications:	Biological & Medicinal Chem.
EPSRC Industrial Sector Classifications:
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Summary on Grant Application Form
The enzyme 5-aminolaevulinate dehydratase catalyses one step in the biosynthesis of essential tetrapyrroles such as haem and chlorophyll. The reaction involves the condensation of two 5-aminolaevulinate residues yielding the pyrrole, porphobilinogen. We have cloned and over-expressed 5-aminolaevulinate debydratase from E.coli and have crystallised the purified enzyme. The crystals diffract to beyond 2.7A resolution and several heavy atom derivatives have been obtained for structure analysis.We request support to allow the structure determination of this fascinating octameric enzyme to be completed. In addition we will analyse active site directed mutants of the enzyme to characterise its reaction mechanism. Our results will have broad implications for understanding how enzymes can stabilise carbanion intermediates.
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