Structure and mechanism of lanthipeptide biosynthetic enzymes

Research output: Contribution to journalReview article

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.

Original languageEnglish (US)
Pages (from-to)58-66
Number of pages9
JournalCurrent Opinion in Structural Biology
Volume29
DOIs
StatePublished - Dec 1 2014

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Peptides
Sulfides
Enzymes
Post Translational Protein Processing
Biological Products
Dehydration
Sulfhydryl Compounds
Acids

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Structure and mechanism of lanthipeptide biosynthetic enzymes. / van der Donk, Wilfred A.; Nair, Satish K.

In: Current Opinion in Structural Biology, Vol. 29, 01.12.2014, p. 58-66.

Research output: Contribution to journalReview article

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