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The dehydratase activity of lacticin 481 synthetase is highly processive.


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.

SUBMITTER: Miller LM 

PROVIDER: S-EPMC2532561 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature

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The dehydratase activity of lacticin 481 synthetase is highly processive.

Miller Leah M LM   Chatterjee Champak C   van der Donk Wilfred A WA   Kelleher Neil L NL  

Journal of the American Chemical Society 20060201 5


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,  ...[more]

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