Mutasynthesis of glycopeptide antibiotics: variations of vancomycin's AB-ring amino acid 3,5-dihydroxyphenylglycine.

@article{Weist2004MutasynthesisOG,
  title={Mutasynthesis of glycopeptide antibiotics: variations of vancomycin's AB-ring amino acid 3,5-dihydroxyphenylglycine.},
  author={Stefan Weist and Claudia Kittel and Daniel Bischoff and Bojan Bister and Volker Pfeifer and Graeme J. Nicholson and Wolfgang Wohlleben and Roderich D S{\"u}ssmuth},
  journal={Journal of the American Chemical Society},
  year={2004},
  volume={126 19},
  pages={5942-3}
}
In the mutasynthetic approach, the DeltadpgA mutant of the vancomycin-type glycopeptide antibiotic producer Amycolatopsis balhimycina, which is deficient in the synthesis of 3,5-dihydroxyphenylglycine (DPg), was supplemented with synthetic DPg analogues to obtain the corresponding modified glycopeptides. Sterically more demanding 3,5-disubstituted methoxy derivatives as well as monosubstituted DPg analogues were accepted as substrates. These facts indicate that steric and electronic… CONTINUE READING