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Errey, 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. 
ORCID: https://orcid.org/0000-0001-8574-0275
(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
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: | 25 Sep 2024 18:07 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/96602 |
| DOI: | 10.1039/b815549f |
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