Acceptor specificity and inhibition of the bacterial cell-wall glycosyltransferase MurG.

@article{Liu2003AcceptorSA,
  title={Acceptor specificity and inhibition of the bacterial cell-wall glycosyltransferase MurG.},
  author={Haitian Liu and Thomas K. Ritter and Reiko Sadamoto and Pamela S Sears and Min Wu and C. -H. Wong},
  journal={Chembiochem : a European journal of chemical biology},
  year={2003},
  volume={4 7},
  pages={603-9}
}
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… CONTINUE READING

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