Insights into the evolution of lanthipeptide biosynthesis

Yi Yu, Qi Zhang, Wilfred A. Van Der Donk

Research output: Contribution to journalReview articlepeer-review


Lanthipeptides are a group of posttranslationally modified peptide natural products that contain multiple thioether crosslinks. These crosslinks are formed by dehydration of Ser/Thr residues followed by addition of the thiols of Cys residues to the resulting dehydroamino acids. At least four different pathways to these polycyclic natural products have evolved, reflecting the high efficiency and evolvability of a posttranslational modification route to generate conformationally constrained peptides. The wealth of genomic information that has been made available in recent years has started to provide insights into how these remarkable pathways and their posttranslational modification machineries may have evolved. In this review, we discuss a model for the evolution of the lanthipeptide biosynthetic enzymes that has recently been developed based on the currently available data.

Original languageEnglish (US)
Pages (from-to)1478-1489
Number of pages12
JournalProtein Science
Issue number11
StatePublished - Nov 2013


  • Cyclic peptide
  • Dehydration
  • Glutamylation
  • Kinase
  • Labionin
  • Lanthionine
  • Lantibiotics
  • Nisin
  • Phosphothreonine lyase
  • Posttranslational modification

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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