Biocatalytic Synthesis of Phenyl Benzoate Esters Using the Amide Ligase ClxA

The 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 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.

Publication Details

Journal
White Rose Research Online (University of Leeds, The University of Sheffield, University of York)
Published
2025-10-08
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
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article

Biocatalytic Synthesis of Phenyl Benzoate Esters Using the Amide Ligase ClxA

White Rose Research Online (University of Leeds, The University of Sheffield, University of York)
Enzyme Catalysis and Immobilization
article

Biocatalytic Synthesis of Phenyl Benzoate Esters Using the Amide Ligase ClxA

article en

Abstract

The 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 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.

White Rose Research Online (University of Leeds, The University of Sheffield, University of York)
Clean water and sanitation
Openalex Percentile: Top 38%
Enzyme Catalysis and Immobilization
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