Structural highlights
Publication Abstract from PubMed
Metagenomics is a modern approach to discovery of new enzymes with novel properties. This article reports the structure of a new lipase, belonging to family I.1, obtained by means of metagenomics. Its structure presents a fold typical of alpha/beta hydrolases, with the lid in closed conformation. The protein was previously shown to present high thermostability and to be stable in aqueous solutions of polar organic solvents at high concentrations [30% (V/V)]. Molecular dynamics studies showed that the protein maintains its structure well in organic solvents. They also suggested that its thermostability might be enhanced if it were mutated to present a disulfide bond similar to that typically found in lipase family I.2. These findings identify this lipase as a good candidate for further improvement through protein engineering.
Structure solution and analyses of the first true lipase obtained from metagenomics indicate potential for increased thermostability.,Martini VP, Krieger N, Glogauer A, Souza EM, Iulek J N Biotechnol. 2019 Jul 12;53:65-72. doi: 10.1016/j.nbt.2019.07.001. PMID:31306784[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Martini VP, Krieger N, Glogauer A, Souza EM, Iulek J. Structure solution and analyses of the first true lipase obtained from metagenomics indicate potential for increased thermostability. N Biotechnol. 2019 Jul 12;53:65-72. doi: 10.1016/j.nbt.2019.07.001. PMID:31306784 doi:http://dx.doi.org/10.1016/j.nbt.2019.07.001
