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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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| Publicat a: | Biomolecules |
|---|---|
| Autors principals: | , , , , , , , , , , , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
MDPI
2021
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7824956/ https://ncbi.nlm.nih.gov/pubmed/33466452 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.3390/biom11010057 |
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