Year: 2025
Type: article
Abstract: , initially reported to have roles in amide bond formation in the biosynthesis of benzoxazole antibiotics, is an effective catalyst for the formation of phenyl benzoate esters from acid and phenol substrates using ATP in an aqueous medium. The structure of ClxA in a complex with both AMP and 3,4-aminohydroxybenzoic acid was determined by X-ray crystallography to 2.15 Å resolution and used as a platform to engineer the enzyme to create variants N226L and K140A possessing broader substrate specificity for ester formation, and also the ability to enable the synthesis of native amide product oligomers.
Source: RSC Chemical Biology
Institution: University of York
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $1,962
OpenAlex ID: W4414961175
