Abstract Hydrolases catalyze synthetic reactions in nonaqueous media, whereas they perform hydrolysis under aqueous solutions. An acyl transferase from Mycobacterium smegmatis (MsAcT) is able to catalyze synthetic reactions in buffer because of its highly hydrophobic active site, which enables efficient transesterification reactions even at 99.9% v/v buffer solution. This unique feature of MsAcT among hydrolases may open new ...
