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The enterobactin biosynthetic intermediate 2,3-dihydroxybenzoic acid is a competitive inhibitor of the Escherichia coli isochorismatase EntB

Author(s): Bin X; Pawelek PD;

The Escherichia coli enterobactin biosynthetic protein EntB is a bifunctional enzyme that catalyzes hydrolysis of isochorismate via its N-terminal isochorismatase (IC) domain, and then transfers phosphopantetheinylated 2,3-DHB to EntF via the EntB C-terminal aryl carrier protein (ArCP) domain. Here we used a fluorescence anisotropy binding assay to invest ...

Article GUID: 40400396


Evidence of isochorismate channeling between the Escherichia coli enterobactin biosynthetic enzymes EntC and EntB

Author(s): Bin X; Pawelek PD;

Enterobactin is a high-affinity iron chelator produced and secreted by Escherichia coli and Salmonella typhimurium to scavenge scarce extracellular Fe3+ as a micronutrient. EntC and EntB are the first two enzymes in the enterobactin biosynthetic pathway. Isochorismate, produced by EntC, is a substrate for EntB isochorismatase. By using a competing isochor ...

Article GUID: 39031458


Seamless site-directed mutagenesis of the Saccharomyces cerevisiae genome using CRISPR-Cas9.

Author(s): Biot-Pelletier D, Martin VJ

J Biol Eng. 2016;10:6 Authors: Biot-Pelletier D, Martin VJ

Article GUID: 27134651


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