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Mechanistic enzymology of trehalose synthesis

Reference	B20376
Principal Investigator / Supervisor	Professor Gideon Davies
Co-Investigators / Co-Supervisors
Institution	University of York
Department	Chemistry
Funding type	Research
Value (£)	199,789
Status	Completed
Type	Research Grant
Start date	01/10/2003
End date	30/09/2006
Duration	36 months

Abstract

The synthesis of the glycosidic bond is quantitatively the most significant reaction on Earth. It is catalysed by activated-sugar dependant glycosyltransferases which act with either inversion or retention of configuration of their nucleotide-sugar donor. These enzymes have received little structural or mechanistic investigation. Trehalose, an unusual non-reducing disaccharide, is central to bacterial survival and persistence processes, protection from environmental stress and is essential for the unusual glycolipids of Mycobacterium tuberculosis. Trehalose is formed in a 2-step reaction catalysed by a UDP-Glc dependant glycosyltransferase, OtsA and a 6-phosphatase, OtsB. We use OtsA as a model for glycosyl transfer with retention. We will dissect the 3-D structure, kinetic and catalytic mechanism impacting both on the fundamental enzymology and laying the foundation for future therapeutic intervention.

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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