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• W2017492018 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." @default.
• W2017492018 created "2016-06-24" @default.
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• W2017492018 date "2009-01-01" @default.
• W2017492018 modified "2023-09-26" @default.
• W2017492018 title "Sugar nucleotide recognition by Klebsiella pneumoniae UDP-d-galactopyranose mutase: Fluorinated substrates, kinetics and equilibria" @default.
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• W2017492018 doi "https://doi.org/10.1039/b815549f" @default.
• W2017492018 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3326532" @default.
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