Structure and mechanism of lanthipeptide biosynthetic enzymes

Curr Opin Struct Biol. 2014 Dec:29:58-66. doi: 10.1016/j.sbi.2014.09.006. Epub 2014 Oct 14.

Abstract

Lanthipeptides are members of the ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. They contain thioether crosslinks generated by dehydration of Ser and Thr residues followed by the addition of the thiol of Cys residues to the dehydroamino acids. Recent studies have revealed unexpected mechanisms of the post-translational modifications, and structural studies have started to provide insights into recognition of the peptide substrates by the modification enzymes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Anti-Bacterial Agents / biosynthesis
  • Anti-Bacterial Agents / chemistry
  • Bacteria / metabolism
  • Bacteriocins / biosynthesis*
  • Bacteriocins / chemistry*
  • Hydro-Lyases / chemistry
  • Oxidoreductases / chemistry
  • Peptide Hydrolases / chemistry*
  • Peptides / chemistry*
  • Protein Conformation
  • Protein Processing, Post-Translational*
  • Ribosomes / metabolism

Substances

  • Anti-Bacterial Agents
  • Bacteriocins
  • Peptides
  • epilancin 15X
  • Oxidoreductases
  • Peptide Hydrolases
  • Hydro-Lyases