Sequence-Based Prediction of Promiscuous Acyltransferase Activity in Hydrolases.

ABSTRACT: Certain hydrolases preferentially catalyze acyl transfer over hydrolysis in an aqueous environment. However, the molecular and structural reasons for this phenomenon are still unclear. Herein, we provide evidence that acyltransferase activity in esterases highly correlates with the hydrophobicity of the substrate-binding pocket. A hydrophobicity scoring system developed in this work allows accurate prediction of promiscuous acyltransferase activity solely from the amino acid sequence of the cap domain. This concept was experimentally verified by systematic investigation of several homologous esterases, leading to the discovery of five novel promiscuous acyltransferases. We also developed a simple yet versatile colorimetric assay for rapid characterization of novel acyltransferases. This st

SUBMITTER: Muller H 

PROVIDER: S-EPMC7383625 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature