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ToolsErrey, James C., Mann, Maretta C., Fairhurst, Shirley A., Hill, Lionel, McNeil, Michael R., Naismith, James H., Percy, Jonathan M., Whitfield, Chris and Field, Robert A. (2009) Sugar nucleotide recognition by Klebsiella pneumoniae UDP-d-galactopyranose mutase:Fluorinated substrates, kinetics and equilibria. Organic and Biomolecular Chemistry, 7 (5). pp. 1009-1016. ISSN 1477-0520
Full text not available from this repository. (Request a copy)Abstract
A series of selectively fluorinated and other substituted UDP-d-galactose derivatives have been evaluated as substrates for Klebsiella pneumoniae UDP-d-galactopyranose mutase. This enzyme, which catalyses the interconversion of the pyranose and furanose forms of galactose as its UDP adduct, is a prospective drug target for a variety of microbial infections. We show that none of the 2″-, 3″- or 6″-hydroxyl groups of UDP-d- galactopyranose are essential for substrate binding and turnover. However, steric factors appear to play an important role in limiting the range of substitutions that can be accommodated at C-2″ and C-6″ of the sugar nucleotide substrate. Attempts to invert the C-2″ stereochemistry from equatorial to axial, changing d-galacto- to d-talo-configuration, in an attempt to exploit the higher percentage of furanose at equilibrium in the talo-series, met with no turnover of substrate.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | biochemistry,physical and theoretical chemistry,organic chemistry ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
| Faculty \ School: | Faculty of Science > School of Chemical Sciences and Pharmacy (former - to 2009) Faculty of Science > School of Chemistry, Pharmacy and Pharmacology Faculty of Science > School of Biological Sciences |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 06 Sep 2024 13:35 |
| Last Modified: | 06 Feb 2025 12:14 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/96602 |
| DOI: | 10.1039/b815549f |
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