期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 59, 期 28, 页码 11607-11612出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202003635
关键词
acylation; acyltransferases; biocatalysis; esterases; transesterification
资金
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [231396381/GRK1947]
- Bundesministerium fur Bildung und Forschung [031B0354B]
- Helmholtz Zentrum Berlin fur Materialien und Energie
- Freie Universitat Berlin
- Humboldt-Universitat zu Berlin
- Max-Del-bruck Centrum
- Leibniz-Institut fur Molekulare Pharmakologie
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.
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