The dehydratase activity of lacticin 481 synthetase is highly processive

被引：28

作者：

Miller, LM ^{[1
]}

Chatterjee, C ^{[1
]}

van der Donk, WA ^{[1
]}

Kelleher, NL ^{[1
]}

机构：

[1] Univ Illinois, Dept Chem, Urbana, IL 61801 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2006年 / 128卷 / 05期

关键词：

D O I：

10.1021/ja057203d

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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. Copyright © 2006 American Chemical Society.

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页码：1420 / 1421

页数：2

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