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Publication Abstract from PubMed

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 study demonstrates that promiscuous acyltransferase activity is not as rare as previously thought and provides access to a vast number of novel acyltransferases with diverse substrate specificity and potential applications.

Sequence-Based Prediction of Promiscuous Acyltransferase Activity in Hydrolases.,Muller H, Becker AK, Palm GJ, Berndt L, Badenhorst CPS, Godehard SP, Reisky L, Lammers M, Bornscheuer UT Angew Chem Int Ed Engl. 2020 Jul 6;59(28):11607-11612. doi:, 10.1002/anie.202003635. Epub 2020 May 11. PMID:32243661^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.