ArticleMolecular and cellular biochemistry2017
Thirty-degree shift in optimum temperature of a thermophilic lipase by a single-point mutation: effect of serine to threonine mutation on structural flexibility.
Article in Molecular and cellular biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Structural and Functional Variations of Enzymes Indicate Latitudinal Adaptations of Subarctic and Arctic Sea Urchins.Ecology and evolution · 2025Article
- Establishment of mesophilic-like catalytic properties in a thermophilic enzyme without affecting its thermal stability.Scientific reports · 2019Article
- Changes of Thermostability, Organic Solvent, and pH Stability inInternational journal of molecular sciences · 2019Article
- Point mutation Arg153-His at surface of Bacillus lipase contributing towards increased thermostability and ester synthesis: insight into molecular network.Molecular and cellular biochemistry · 2018Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In order to understand the molecular basis of cold adaptation, we have used directed evolution to transform a thermophilic lipase LipR1 into its psychrophilic counterpart. A single round of random mutagenesis followed by screening for improved variants yielded a mutant with single-point mutation LipR1M1 (S130T), with optimum activity at 20 °C. Its activity at 50 °C is only 20% as compared to wild type (100%). It showed catalytic rate constant (k
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