ArticleProtein science : a publication of the Protein Society2025
The enterobactin biosynthetic intermediate 2,3-dihydroxybenzoic acid is a competitive inhibitor of the Escherichia coli isochorismatase EntB.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- EcoliTyper: a species-optimized computational pipeline for comprehensive genotyping and surveillance of Escherichia coli.BMC bioinformatics · 2026Article
- The enterobactin biosynthetic intermediate 2,3-dihydroxybenzoic acid is a competitive inhibitor of the Escherichia coli isochorismatase EntB.Protein science : a publication of the Protein Society · 2025Article
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2 authors.
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Abstract
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 investigate the ability of 2,3-DHB to bind to enzymes in the DHB synthetic arm of the pathway. We found that 2,3-DHB binds to EntE as a natural substrate with high affinity (K
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