The dehydratase activity of lacticin 481 synthetase is highly processive

Leah M. Miller, Champak Chatterjee, Wilfred A. Van Der Donk, Neu L. Kelleher*

*Corresponding author for this work

Research output: Contribution to journalArticle

29 Scopus citations

Abstract

Lacticin 481 synthetase (LctM) is a bifunctional enzyme that undertakes dehydration and cyclization in the structural region of the pre-lacticin peptide (LctA) to introduce three thioether rings and one dehydrobutyrine residue. The order and timing of these events has been investigated employing high-resolution ESI-FTMS-based tandem MS/MS techniques and chemical derivatization. LctM demonstrates highly processive behavior as seen by MS analysis of the reaction course of dehydration. Furthermore, cyclization is not tightly coupled to dehydration and follows at a later stage of the enzymatic reaction.

Original languageEnglish (US)
Pages (from-to)1420-1421
Number of pages2
JournalJournal of the American Chemical Society
Volume128
Issue number5
DOIs
StatePublished - Feb 8 2006

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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