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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 Escherichia coli. We elucidated the 3D structure of the enzyme which belongs to the hormone-sensitive lipase (HSL) family. Similar to other bacterial HSL...

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Detalles Bibliográficos
Autores principales:	Boyko, Konstantin M., Kryukova, Mariya V., Petrovskaya, Lada E., Kryukova, Elena A., Nikolaeva, Alena Y., Korzhenevsky, Dmitry A., Lomakina, Galina Yu., Novototskaya-Vlasova, Ksenia A., Rivkina, Elizaveta M., Dolgikh, Dmitry A., Kirpichnikov, Mikhail P., Popov, Vladimir O.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2021
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7824956/ https://www.ncbi.nlm.nih.gov/pubmed/33466452 http://dx.doi.org/10.3390/biom11010057

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