The enterobactin biosynthetic intermediate 2,3-dihydroxybenzoic acid is a competitive inhibitor of the Escherichia coli isochorismatase EntB.

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_D = 0.54 μM). Furthermore, apo-EntB was found to bind to 2,3-DHB with moderate affinity (K_D = 8.95 μM), despite the fact that this intermediate is neither a substrate nor a product of EntB. Molecular docking simulations predicted a top-ranked ensemble

SUBMITTER: Bin X 

PROVIDER: S-EPMC12096016 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature