Understanding the early stages of peptide formation during the biosynthesis of teicoplanin and related glycopeptide antibiotics

@article{Kaniusaite2020UnderstandingTE,
  title={Understanding the early stages of peptide formation during the biosynthesis of teicoplanin and related glycopeptide antibiotics},
  author={Milda Kaniusaite and Julien Tailhades and Tiia Kittil{\"a} and Christopher D. Fage and Robert J A Goode and Ralf B. Schittenhelm and Max J. Cryle},
  journal={The FEBS Journal},
  year={2020},
  volume={288}
}
The biosynthesis of the glycopeptide antibiotics (GPAs) demonstrates the exceptional ability of nonribosomal peptide (NRP) synthesis to generate diverse and complex structures from an expanded array of amino acid precursors. Whilst the heptapeptide cores of GPAs share a conserved C terminus, including the aromatic residues involved cross‐linking and that are essential for the antibiotic activity of GPAs, most structural diversity is found within the N terminus of the peptide. Furthermore, the… 

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