Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.

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.

• Authors: Lindsay M Repka, Jonathan R Chekan, Satish K Nair, Wilfred A van der Donk
• Journal: Chemical reviews (Chem Rev) Vol. 117 Issue 8 Pg. 5457-5520 (Apr 26 2017) ISSN: 1520-6890 [Electronic] United States
• PMID: 28135077 (Publication Type: Journal Article, Review)

Chemical References

• Bacteriocins
• Enzymes
• Peptides

Topics

• Bacteriocins (metabolism)
• Enzymes (metabolism)
• Peptides (chemistry)
• Protein Processing, Post-Translational