6Y9K

Esterase EST8 with transacylase activity

This is a non-PDB format compatible entry.

Summary for 6Y9K

• Entry DOI: 10.2210/pdb6y9k/pdb
• Descriptor: Esterase Est8 (2 entities in total)
• Functional Keywords: ab hydrolase, transacetylase, transacylase, hydrolase
• Biological source: metagenome
• Total number of polymer chains: 4
• Total formula weight: 129861.66

Authors

Palm, G.J.,Lammers, M.,Berndt, L. (deposition date: 2020-03-09, release date: 2020-07-29, Last modification date: 2024-01-24)

Primary citation

Muller, H.,Becker, A.K.,Palm, G.J.,Berndt, L.,Badenhorst, C.P.S.,Godehard, S.P.,Reisky, L.,Lammers, M.,Bornscheuer, U.T.
Sequence-Based Prediction of Promiscuous Acyltransferase Activity in Hydrolases.
Angew.Chem.Int.Ed.Engl., 59:11607-11612, 2020

PubMed 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 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.

PubMed: 32243661
DOI: 10.1002/anie.202003635

Experimental method

X-RAY DIFFRACTION (2.298 Å)