9s3l
From Proteopedia
ClxA from Clostridium cavendishii (apo)
Structural highlights
FunctionPublication Abstract from PubMedThe synthesis of ester bonds using lipases is one of the most frequently performed reactions in biocatalysis, yet examples of the enzymatic synthesis of phenyl benzoate esters are comparatively rare. In this report we show that the ligase ClxA, from Clostridium cavendishii, 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 A 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. Biocatalytic synthesis of phenyl benzoate esters using the amide ligase ClxA.,Ascham A, Tang Q, Fairlamb IJS, Grogan G RSC Chem Biol. 2025 Oct 8. doi: 10.1039/d5cb00205b. PMID:41098411[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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