Structural and Biochemical Characterization of a Cold-Active PMGL3 Esterase with Unusual Oligomeric Structure

Structural and Biochemical Characterization of a Cold-Active PMGL3 Esterase with Unusual Oligomeric Structure

The gene coding for a novel cold-active esterase PMGL3 was previously obtained from a Siberian permafrost metagenomic DNA library and expressed in <i>Escherichia coli</i>. We elucidated the 3D structure of the enzyme which belongs to the hormone-sensitive lipase (HSL) family. Similar to...

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Bibliographic Details
Main Authors: Konstantin M. Boyko, Mariya V. Kryukova, Lada E. Petrovskaya, Elena A. Kryukova, Alena Y. Nikolaeva, Dmitry A. Korzhenevsky, Galina Yu. Lomakina, Ksenia A. Novototskaya-Vlasova, Elizaveta M. Rivkina, Dmitry A. Dolgikh, Mikhail P. Kirpichnikov, Vladimir O. Popov
Format: Article
Language:English
Published: MDPI AG 2021-01-01
Series:Biomolecules
Subjects:
PMGL3 esterase, HSL family, tetramer, dimer, GDSAG subfamily, mutagenesis, cold-active proteins
Online Access:https://www.mdpi.com/2218-273X/11/1/57

Internet

https://www.mdpi.com/2218-273X/11/1/57

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