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Structure function and mechanism of UDP-galactomutase
Reference
B11756
Principal Investigator / Supervisor
Professor James Naismith
Co-Investigators /
Co-Supervisors
Institution
University of St Andrews
Department
Biology
Funding type
Research
Value (£)
168,052
Status
Completed
Type
Research Grant
Start date
01/02/2000
End date
31/10/2003
Duration
45 months
Abstract
UDP-galactopyranose mutase is an enzyme responsible for the conversion of UDP- galactose pyranose (six membered ring) into UDP- galactose furanose (five membered ring). This mechanistically fascinating transformation is accomplished using two co-factors FAD and NAD(P)H. The role of these co-factors is unknown. UDP- galactofuranose is a key component in cell walls of many pathogenic bacteria including Mycobacteria tuberculosis and Klebsiella pneumoniae. We propose to solve the structure of this enzyme from three organisms and determine the mechanism. We have obtained diffraction data from one source (E. coli), crystals from a second (K. pneumoniae) and expressed protein from the third (M. tuberculosis).
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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