Journal
BIOCHEMISTRY
Volume 48, Issue 46, Pages 10827-10829Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi901680m
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Funding
- National Institutes of Health [A160899, T32 GM08572, RR017998]
- NSF [DB19601607, D1310331934]
- HHMI Research Resources for Biomedical Sciences
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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 or 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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