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Enterobactin synthetase-catalyzed formation of P(1),P(3)-diadenosine-5'-tetraphosphate.


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.

SUBMITTER: Sikora AL 

PROVIDER: S-EPMC2783875 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature

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Enterobactin synthetase-catalyzed formation of P(1),P(3)-diadenosine-5'-tetraphosphate.

Sikora Alison L AL   Cahill Sean M SM   Blanchard John S JS  

Biochemistry 20091101 46


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 stor  ...[more]

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