Enterobactin synthetase-catalyzed formation of P1,P 3-diadenosine-5′-tetraphosphate

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 4A, a molecule that is implicated in regulating cell division during oxidative stress. We propose that the expression of EntE during iron starvation produces Ap4A to slow growth until intracellular iron stores can be restored.

Original languageEnglish (US)
Pages (from-to)10827-10829
Number of pages3
JournalBiochemistry
Volume48
Issue number46
DOIs
StatePublished - Nov 24 2009

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Iron
Enterobactin
Siderophores
Oxidative stress
Starvation
Cell Division
Carrier Proteins
Oxidative Stress
Cells
Molecules
Enzymes
Growth
enterobactin synthetase
diadenosine tetraphosphate
2,3-dihydroxybenzoic acid
4'-phosphopantetheine

ASJC Scopus subject areas

  • Biochemistry

Cite this

Enterobactin synthetase-catalyzed formation of P1,P 3-diadenosine-5′-tetraphosphate. / Sikora, Alison L.; Cahill, Sean M.; Blanchard, John S.

In: Biochemistry, Vol. 48, No. 46, 24.11.2009, p. 10827-10829.

Research output: Contribution to journalArticle

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