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Updated: Jun 19, 2026

A Purification and In Vitro Activity Assay for a (p)ppGpp Synthetase from Clostridium difficile
Published on: November 3, 2018
Enterobactin synthetase-catalyzed formation of P(1),P(3)-diadenosine-5'-tetraphosphate
Alison L Sikora1, Sean M Cahill, John S Blanchard
1Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Abstract:
The EntE enzyme, involved in the synthesis of the iron siderophore enterobactin, catalyzes the adenylation of 2,3-dihydroxybenzoic acid, followed by its transfer to the phosphopantetheine arm of holo-EntB, an aryl carrier protein. In the absence of EntB, EntE catalyzes the formation of Ap(4)A, a molecule that is implicated in regulating cell division during oxidative stress. We propose that the expression of EntE during iron starvation produces Ap(4)A to slow growth until intracellular iron stores can be restored.
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