ArticleThe journal of physical chemistry. B2022
Thermoadaptation in an Ancestral Diterpene Cyclase by Altered Loop Stability.
Article in The journal of physical chemistry. B, 2022. 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, 20 citations in OpenAlex.
- Progress and future outlook towards a safe and sustainable production and use of chemicals.Communications chemistry · 2025Review
- Automated Engineering Protein Dynamics via Loop Grafting: ImprovingACS catalysis · 2025Article
- Ancestral Sequence Reconstruction for Designing Biocatalysts and Investigating their Functional Mechanisms.JACS Au · 2024Review
- MEnTaT: A machine-learning approach for the identification of mutations to increase protein stability.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermostability is the key to maintain the structural integrity and catalytic activity of enzymes in industrial biotechnological processes, such as terpene cyclase-mediated generation of medicines, chiral synthons, and fine chemicals. However, affording a large increase in the thermostability of enzymes through site-directed protein engineering techniques can constitute a challenge. In this paper, we used ancestral sequence reconstruction to create a hyperstable variant of the
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