Abstract 1543 Identifying serine hydrolase activity in E. coli utilizing gene knockout strains

Serine hydrolases compose a diverse enzyme family capable of acting as catalysts for various reactions including esterase, thioesterase, epoxidase, and amidase activities. With this diverse reactivity, serine hydrolases have found utility in a wide array of biocatalytic applications such as in performing organic synthesis and monitoring cellular processes. The identification of novel serine hydrolase activity in Escherichia coli is of interest because discoveries could be exploited to develop prodrugs for targeted antimicrobial resistance.