Abstract
A continuous fluorescence coupled enzyme assay was developed to study the acceptor specificity of the glycosyltransferase MurG toward different lipid I analogues with various substituents replacing the undecaprenyl moiety. It was found that most lipid I analogues are accepted as substrates and, amongst these, the saturated C14 analogue exhibits the best activity. This substrate was used to evaluate the inhibition activity of such antibiotics as moenomycin, vancomycin, and two chlorobiphenyl vancomycin derivatives. A vancomycin derivative with a chlorobiphenyl moiety on the aglycon section was identified as a potent inhibitor of MurG.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Outer Membrane Proteins / antagonists & inhibitors
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Bacterial Outer Membrane Proteins / metabolism*
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Bambermycins / chemistry
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Bambermycins / pharmacology
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Cell Wall / enzymology
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Cell Wall / metabolism
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / metabolism*
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Enzyme Inhibitors / pharmacology*
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Escherichia coli / enzymology
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Inhibitory Concentration 50
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Lipid Metabolism
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Lipids / chemistry
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Monosaccharides / chemistry
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Monosaccharides / metabolism*
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Monosaccharides / pharmacology
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N-Acetylglucosaminyltransferases / antagonists & inhibitors*
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N-Acetylglucosaminyltransferases / metabolism*
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Oligopeptides / chemistry
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Oligopeptides / metabolism*
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Oligopeptides / pharmacology
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Substrate Specificity
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Vancomycin / analogs & derivatives
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Vancomycin / pharmacology
Substances
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Bacterial Outer Membrane Proteins
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Enzyme Inhibitors
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Lipids
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Monosaccharides
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Oligopeptides
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lipid I
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Bambermycins
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Vancomycin
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N-Acetylglucosaminyltransferases
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UDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase