Fluorogenic structure activity library pinpoints molecular variations in substrate specificity of structurally homologous esterases.

ABSTRACT: Cellular esterases catalyze many essential biological functions by performing hydrolysis reactions on diverse substrates. The promiscuity of esterases complicates assignment of their substrate preferences and biological functions. To identify universal factors controlling esterase substrate recognition, we designed a 32-member structure-activity relationship (SAR) library of fluorogenic ester substrates and used this library to systematically interrogate esterase preference for chain length, branching patterns, and polarity to differentiate common classes of esterase substrates. Two structurally homologous bacterial esterases were screened against this library, refining their previously broad overlapping substrate specificity. Vibrio cholerae esterase ybfF displayed a preference for

SUBMITTER: White A 

PROVIDER: S-EPMC6130942 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature