Abstract 2003 Measuring the substrate specificity of esterases for alcohol substituents using terbium luminescence

Esterases are a large subfamily of hydrolytic enzymes capable of breaking ester bonds into their component carboxylic acid and alcohol subunits. With their broad substrate specificity, esterases have applications as biocatalysts in pharmaceutical and industrial settings. Currently, esterase biocatalyst design and the majority of ester substrate libraries have focused on shifts in their reactivity based on modifications in the carboxylic acid subunit of the ester. In this study, we synthesized an expanded library of thiopheneacetic acid esters with modifications to the alcohol subunits on the ester and used shifts in their terbium sensitization upon ester hydrolysis to characterize the alcohol substrate specificity of multiple model esterases.