Abstract

Glycopeptide antibiotics are an important class of therapeutic agents with vancomycin and teicoplanin currently in clinical use. In addition, second-generation compounds obtained by semisynthesis have been developed. Glycopeptides are considered drugs of last resort for the treatment of life-threatening infections caused by Gram-positive bacteria. They inhibit bacterial growth by interfering with cell wall biosynthesis. This occurs through binding to and sequestering lipid II from the action of bacterial enzymes. Resistance to glycopeptides is also of clinical concern. It occurs through the reprogramming of peptidoglycan formation, in which a d -lactate unit replaces the terminal d -alanine in lipid II, a substitution sufficient to prevent glycopeptide binding. Glycopeptides, which are naturally produced by several actinomycete soil bacteria, consist of a heptapeptide skeleton highly modified through cross-linking of the aromatic moieties. Further embellishments of the cross-linked aglycone can occur, such as glycosylation, chlorination, and acylation. The biosynthesis of glycopeptides has been analyzed in different producer strains and requires about 40 different enzymatic activities. Recent genetic and biochemical studies have revealed some fascinating mechanisms through which actinomycetes synthesize these complex compounds.

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