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Structural Relationships in Microbial Peptides

Abstract

THE biosynthesis of a considerable number of peptide antibiotics is independent of the processes involved in protein biosynthesis1,2. Mauger has suggested2 that microbial peptides are derived wholly, or in part, by enzymatically controlled condensations and ring expansions of diketopiperazine units (DKPs) because they are virtually all cyclic and they often co-occur with DKPs containing amino-acids found in the peptide. In addition, Mauger drew some interesting correlations between the observed distribution of D-ammo-acids in some peptides arid the possible role of epimerized DKPs as biosynthetic precursors. No mechanism was advanced, however, for the epimerization step, apart from an analogy drawn with the base catalysed chemical epimerization of cis (L-L) DKPs to the thermodynamically more stable trans (L-D) form3.

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BYCROFT, B. Structural Relationships in Microbial Peptides. Nature 224, 595–597 (1969). https://doi.org/10.1038/224595a0

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