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Structure and mechanism of NADH / Mn dependant glycoside hydrolases
Reference
B13588
Principal Investigator / Supervisor
Professor Gideon Davies
Co-Investigators /
Co-Supervisors
Institution
University of York
Department
Chemistry
Funding type
Research
Value (£)
120,053
Status
Completed
Type
Research Grant
Start date
01/10/2000
End date
01/10/2002
Duration
24 months
Abstract
The cleavage of glycoside bonds is one of the most fundamentally important enzyme-catalysed reactions. Classical 'inverting' and 'retaining' glycoside hydrolysis reactions and the beta-elimination reaction catalysed by polysaccharide lyases are well-documented. The import of alpha- and beta-linked disaccharides into bacteria, however, involves a family of enzymes that utilise a novel, as yet undescribed, NAD(H) and Mn2+ catalysed mechanism for glycosidic bond cleavage. This family of enzymes is unique amongst 'hydrolytic' enzyme families in that closely related proteins may display absolute, but opposite, anomeric specificities. The structural basis for ligand recognition and the unusual catalytic mechanism of this family will be investigated through the determination of the structures and ligand complexes of the B. subtilis GlvA and E. coli CelF proteins which favour alpha- and beta-linked substrates respectively.
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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