Glycopeptide and lipoglycopeptide antibiotics.

By D. Kahne, Catherine Leimkuhler, W. Lu, C. Walsh. Chemical Reviews, 2005

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How antibiotics kill bacteria: from targets to networks (2010, background): “By contrast, most actinobacterium-derived glycopeptide antibiotics (for example, vancomycin) inhibit peptidoglycan synthesis by binding peptidoglycan units (at the D -alanyl- D -alanine dipeptide) and by blocking transglycosylase and PBP activit”
Action and resistance mechanisms of antibiotics: A guide for clinicians (2017, background): “The peptidoglycan undergoes cross-linking of the glycan strands by the action of transglycosidases, and the peptide chains extend from the sugars in the polymers and form cross links, one peptide to another.[2] The D-alanyl-alanine portion of peptide chain is cross linked by glycine residues in the ”
Insights into secondary metabolism from a global analysis of prokaryotic biosynthetic gene clusters. (2014, background): “…antibiotics contain enzymes to synthesize the nonproteinogenic amino acids b-hydroxytyrosine, 4-hydroxyphenylglycine, and 3,5-dihydroxyphenylglycine that their core nonribosomal peptide synthetases use in the assembly of their peptidic scaffolds (Kahne et al., 2005; Pelzer et al., 1999).”
New antibiotics from bacterial natural products (2006, background): “The best known lipid II-targeting antibiotics are the vancomycin and teicoplanin class of glycopeptide”