Recombinant E.coli entC1 protein

EntC1 is a recombinant protein derived from the entC gene, which encodes a key enzyme involved in the biosynthesis of enterobactin, a high-affinity iron-chelating siderophore produced by *Escherichia coli* and other Gram-negative bacteria. Siderophores like enterobactin play a critical role in bacterial iron acquisition, enabling pathogens to scavenge limited iron resources from host environments during infection. The entC gene is part of the *entCEBA* operon responsible for converting chorismic acid into 2.3-dihydroxybenzoate (DHB), a precursor for enterobactin assembly. Specifically, EntC1 functions as an isomerase, catalyzing the conversion of isochorismate to 2.3-dihydro-2.3-dihydroxybenzoate during the DHB synthesis pathway.

Recombinant EntC1 is typically produced by cloning the entC gene into expression vectors (e.g., pET or pGEX systems) and overexpressing it in heterologous hosts like *E. coli*. This allows for high-yield purification and characterization of the enzyme. Studies on EntC1 have focused on elucidating its structure-function relationships, substrate specificity, and regulatory mechanisms, providing insights into bacterial iron metabolism and virulence. Its role in enterobactin production makes it a potential target for antimicrobial strategies, as disrupting iron uptake could attenuate bacterial pathogenicity. Additionally, recombinant EntC1 is used in biochemical assays to screen for inhibitors or to engineer synthetic siderophore pathways in biotechnological applications. Recent structural analyses, including X-ray crystallography, have revealed details about its active site and catalytic residues, aiding rational drug design. Research on EntC1 also contributes to understanding antibiotic resistance mechanisms, as siderophore-mediated iron acquisition is linked to bacterial survival under stress. Overall, EntC1 serves as a model system for studying microbial metallobiology and developing novel therapeutic interventions.