6y9k

Esterase EST8 with transacylase activity

spinqualitylabelsall models 6y9k, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6y9k is a 4 chain structure with sequence from Metagenome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.298Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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