Abstract
UDP-galactopyranose mutase (UGM or Glf), which catalyzes the interconversion of UDP-galactopyranose and UDP-galactofuranose, is implicated in the viability and virulence of multiple pathogenic microorganisms. Here we report the synthesis of high-affinity ligands for UGM homologues from Klebsiella pneumoniae and Mycobacterium tuberculosis. The potency of these compounds stems from their ability to access both the substrate binding pocket and an adjacent site.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Catalysis
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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Galactose / analogs & derivatives*
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Galactose / chemical synthesis
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Galactose / chemistry
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Galactose / pharmacology
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Intramolecular Transferases / antagonists & inhibitors*
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Klebsiella pneumoniae / enzymology
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Ligands
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Mycobacterium tuberculosis / enzymology
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Uridine Diphosphate / analogs & derivatives*
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Uridine Diphosphate / chemical synthesis
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Uridine Diphosphate / chemistry
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Uridine Diphosphate / pharmacology
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Uridine Diphosphate Galactose / chemical synthesis
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Uridine Diphosphate Galactose / chemistry
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Uridine Diphosphate Galactose / pharmacology*
Substances
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Enzyme Inhibitors
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Ligands
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uridine diphosphate galactofuranose
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Uridine Diphosphate Galactose
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Uridine Diphosphate
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Intramolecular Transferases
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UDP-galactopyranose mutase
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Galactose