Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes

Lindsay M. Repka, Jonathan R. Chekan, Satish K. Nair, Wilfred A. Van Der Donk

Research output: Contribution to journalArticlepeer-review

Abstract

Lanthipeptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) that display a wide variety of biological activities, from antimicrobial to antiallodynic. Lanthipeptides that display antimicrobial activity are called lantibiotics. The post-translational modification reactions of lanthipeptides include dehydration of Ser and Thr residues to dehydroalanine and dehydrobutyrine, a transformation that is carried out in three unique ways in different classes of lanthipeptides. In a cyclization process, Cys residues then attack the dehydrated residues to generate the lanthionine and methyllanthionine thioether cross-linked amino acids from which lanthipeptides derive their name. The resulting polycyclic peptides have constrained conformations that confer their biological activities. After installation of the characteristic thioether cross-links, tailoring enzymes introduce additional post-translational modifications that are unique to each lanthipeptide and that fine-tune their activities and/or stability. This review focuses on studies published over the past decade that have provided much insight into the mechanisms of the enzymes that carry out the post-translational modifications.

Original languageEnglish (US)
Pages (from-to)5457-5520
Number of pages64
JournalChemical reviews
Volume117
Issue number8
DOIs
StatePublished - Apr 26 2017

ASJC Scopus subject areas

  • General Chemistry

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