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Updated: Aug 13, 2026

An Assay for Measuring the Activity of Escherichia coli Inducible Lysine Decarboxyase
Published on: December 19, 2010
The dehydratase activity of lacticin 481 synthetase is highly processive
Leah M Miller1, Champak Chatterjee, Wilfred A van der Donk
1Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
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.
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