Characterization of Leader Peptide Binding during Catalysis by the Nisin Dehydratase NisB

Lindsay M. Repka, Kenton J. Hetrick, See Hyun Chee, Wilfred A. Van Der Donk

Research output: Contribution to journalArticlepeer-review


The dehydratase NisB performs stepwise tRNAGlu-dependent glutamylation of Ser/Thr residues and subsequent glutamate elimination to effect eight dehydrations in the biosynthesis of the antibacterial peptide nisin. Its substrate, NisA, bears a C-terminal core peptide that is modified and an N-terminal leader peptide (LP) that is not modified but that is required for efficient dehydration. To elucidate the mechanism of LP-NisB interactions during dehydration, we engineered a disulfide that covalently links the NisA LP to NisB. The enzyme fully dehydrated tethered NisA, confirming the functional LP binding site and supporting a mechanism where NisB uses a single LP binding site for glutamylation and elimination. We also show an order of NisA and tRNAGlu binding to NisB that enables dehydration.

Original languageEnglish (US)
Pages (from-to)4200-4203
Number of pages4
JournalJournal of the American Chemical Society
Issue number12
StatePublished - Mar 28 2018

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


Dive into the research topics of 'Characterization of Leader Peptide Binding during Catalysis by the Nisin Dehydratase NisB'. Together they form a unique fingerprint.

Cite this