ArticleChembiochem : a European journal of chemical biology2021
Using Mutability Landscapes To Guide Enzyme Thermostabilization.
Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Deep mutational scanning reveals a de novo disulfide bond and combinatorial mutations for engineering thermostable myoglobin.Protein science : a publication of the Protein Society · 2025Article
- Tuning Enzyme Thermostability via Computationally Guided Covalent Stapling and Structural Basis of Enhanced Stabilization.Biochemistry · 2022Article
- Enantiocomplementary Michael Additions of Acetaldehyde to Aliphatic Nitroalkenes Catalyzed by Proline-Based Carboligases.Chembiochem : a European journal of chemical biology · 2022Article
- Learning Strategies in Protein Directed Evolution.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Using Mutability Landscapes To Guide Enzyme Thermostabilization.Chembiochem : a European journal of chemical biology · 2021Article
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Authors and funding
6 authors.
Funding
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Abstract
Thermostabilizing enzymes while retaining their activity and enantioselectivity for applied biocatalysis is an important topic in protein engineering. Rational and computational design strategies as well as directed evolution have been used successfully to thermostabilize enzymes. Herein, we describe an alternative mutability-landscape approach that identified three single mutations (R11Y, R11I and A33D) within the enzyme 4-oxalocrotonate tautomerase (4-OT), which has potential as a biocatalyst for pharmaceutical synthesis, that gave rise to significant increases in apparent melting temperature T
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