Biochemical and Structural Characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL family

Biochemical and Structural Characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL family

A novel esterase, EstD11, has been discovered in a hot spring metagenomic library. It is a thermophilic and thermostable esterase with an optimum temperature of 60°C. A detailed substrate preference analysis of EstD11 was done using a library of chromogenic ester substrate that revealed the broad su...

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Bibliographic Details
Main Authors: Vega Miguel-Ruano, Ivanna Rivera, Jelena Rajkovic, Kamila Knapik, Ana Torrado, José Manuel Otero, Elisa Beneventi, Manuel Becerra, Mercedes Sánchez-Costa, Aurelio Hidalgo, José Berenguer, María-Isabel González-Siso, Jacobo Cruces, María L. Rúa, Juan A. Hermoso
Format: Article
Language:English
Published: Elsevier 2021-01-01
Series:Computational and Structural Biotechnology Journal
Subjects:
Crystal structure
Metagenomic
Thermophilic esterase
α/β hydrolase fold
Enzyme-substrate complex
Online Access:http://www.sciencedirect.com/science/article/pii/S2001037021000519

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http://www.sciencedirect.com/science/article/pii/S2001037021000519

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