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Acceptor specificity and inhibition of the bacterial cell-wall glycosyltransferase murg

Academic Article
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Overview

related to degree

  • Liu, Haitian, Ph.D. in Chemistry, Scripps Research 1999 - 2005
  • Ritter, Thomas Kurt, Ph.D. in Chemistry, Scripps Research 1998 - 2003

authors

  • Liu, Haitian
  • Ritter, Thomas Kurt
  • Sadamoto, R.
  • Sears, Pamela
  • Wu, M.
  • Wong, Chi-Huey

publication date

  • July 2003

journal

  • ChemBioChem  Journal

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.

subject areas

  • Bacterial Outer Membrane Proteins
  • Bambermycins
  • Cell Wall
  • Enzyme Inhibitors
  • Escherichia coli
  • Inhibitory Concentration 50
  • Lipid Metabolism
  • Lipids
  • Monosaccharides
  • N-Acetylglucosaminyltransferases
  • Oligopeptides
  • Substrate Specificity
  • Vancomycin
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Research

keywords

  • enzyme catalysis
  • glycosyltansferases
  • inhibitors
  • lipids
  • substrate specificity
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Identity

International Standard Serial Number (ISSN)

  • 1439-4227

Digital Object Identifier (DOI)

  • 10.1002/cbic.200300557

PubMed ID

  • 12851929
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Additional Document Info

start page

  • 603

end page

  • 609

volume

  • 4

issue

  • 7

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