Chemists and biochemists have long appreciated the wealth of reactions catalyzed by a/� hydrolases. The catalytic and substrate promiscuity of a/� hydrolases allows them to perform diverse chemical transformations from ester, thioester, epoxide, and amide hydrolysis to carbon-carbon bond formation. This combination of promiscuity and ambiguity, however, makes the prediction of endogenous and exogenous substrates and biological functions difficult for a/� hydrolases. In this research, we synthesized a library of latent fluorophore substrates based on di(methyl ether) fluorescein with diverse esterase functionalities and used microplate assays to determine the substrate specificity of diverse bacterial esterases. Esterases essential to the pathogenicity of highly virulent bacteria were screened for substrate specificities and the substrate specificity compared to endogenous mammalian esterases. Distinct profiles of substrate specificity emerged that confirmed the broad substrate specificity of many bacterial esterases, but also suggested unique specificities that could be exploited for antibiotic development.

Distinct substrate profiles of bacterial esterases determined using a library of latent fluorophores

243rd National Meeting (2012)

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