Post-translational modifications during lantibiotic biosynthesis.

Lili Xie; Wilfred A van der Donk

doi:10.1016/j.cbpa.2004.08.005

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PubMed · 15450492

Post-translational modifications during lantibiotic biosynthesis.

Lili Xie·Wilfred A van der Donk

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Abstract

Recent reports have provided the first insights into the mechanisms of the extensive post-translational modifications involved in the biosynthesis of the lantibiotics, a class of peptide antimicrobial agents. These modifications involve dehydration of several serine and threonine residues followed by intramolecular conjugate additions of cysteines, resulting in extensively cross-linked polycyclic structures. Both in vivo and in vitro studies indicate low substrate specificity of the modification machinery, which has been explored for re-engineering of the structures of a number of members. In addition to these developments in understanding their biosynthesis, studies on the mode of action of several lantibiotics have shown a unique mechanism of binding to lipid II, an intermediate in cell wall biosynthesis.

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Amino Acid Sequence Anti-Bacterial Agents Bacteriocins Cell Wall Cysteine Lanatosides Lipid Metabolism Molecular Sequence Data Peptides Protein Processing, Post-Translational Serine Substrate Specificity Threonine Journal Article Research Support, U.S. Gov't, P.H.S.Review

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Lili Xie, Wilfred A van der Donk. 2004. Post-translational modifications during lantibiotic biosynthesis.. https://doi.org/10.1016/j.cbpa.2004.08.005

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