In Vitro Kinetic Analysis of Substrate Specificity in Enterobactin Biosynthetic Lower Pathway Enzymes Provides Insight into the Biochemical Function of the Hot Dog-Fold Thioesterase EntH

被引：22

作者：

Chen, Danqi ^{[1
]}

Wu, Rui ^{[1
]}

Bryan, Tyre L. ^{[1
]}

Dunaway-Mariano, Debra ^{[1
]}

机构：

[1] Univ New Mexico, Dept Chem & Chem Biol, Albuquerque, NM 87131 USA

来源：

BIOCHEMISTRY | 2009年 / 48卷 / 03期

关键词：

IRON;

D O I：

10.1021/bi802207t

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Escherichia coli siderophore enterobactin is assembled from 2,3-dihydroxybenzoate (2,3-DHB) and L-serine by the nonribosomal peptide synthetases EntB and EntF. The processive thiol-template strategy used can be sabotaged by EntB misacylation. Through in vitro kinetic analysis, we demonstrate two potential routes to EntB misacylation and provide evidence for two mechanisms by which the hot dog-fold thioesterase EntH can potentially prevent or reverse EntB misacylation.

引用

页码：511 / 513

页数：3

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