ArticleScientific reports2017
Two strategies to engineer flexible loops for improved enzyme thermostability.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers, 1 of them a synthesis that pooled it.
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71 citing papers in PubMed, 1 synthesis or guideline pooled it, 196 citations in OpenAlex.
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- Temperature-Dependent Thumb Domain Dynamics of Xylanase TsaGH11: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2026Article
- Designing Novel Aspartic Protease (NAP) Using Ancestral Sequence Reconstruction (ASR) for Cheesemaking.Molecular biotechnology · 2026Article
- SegDesign: A modular framework for controllable protein segment engineering.Protein science : a publication of the Protein Society · 2026Article
- Molecular dynamics simulations of temperature-dependent PET binding in PETase, ThermoPETase, and FAST-PETase.RSC advances · 2026Article
- Discovery of novel natural compounds as PKCθ inhibitors: structure-based virtual screening and in vitro evaluation.Journal of computer-aided molecular design · 2026Article
- Enzyme-Embedded Biodegradable Plastic for Sustainable Applications: Advances, Challenges, and Perspectives.ACS applied bio materials · 2025Review
- A thermostable and highly active fungal GH3 β-glucosidase generated by random and saturation mutagenesis.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025Article
- Improved Enzymatic Properties of Chitosanase CsnMY002 fromInternational journal of molecular sciences · 2025Article
- Increasing thermostability of the key photorespiratory enzyme glycerate 3-kinase by structure-based recombination.Plant biotechnology journal · 2025Article
- Engineering Protein Dynamics through Mutational Energy Landscape Traps.Journal of chemical information and modeling · 2025Article
- Amino acid sequence encodes protein abundance shaped by protein stability at reduced synthesis cost.Protein science : a publication of the Protein Society · 2025Article
- Enzyme stabilisation due to incorporation of a fluorinated non-natural amino acid at the protein surface.Scientific reports · 2024Article
- Two-substrate enzyme engineering using small libraries that combine the substrate preferences from two different variant lineages.Scientific reports · 2024Article
- Superior protein thermophilicity prediction with protein language model embeddings.NAR genomics and bioinformatics · 2023Article
- Biochemical and molecular characterization of a novel glycerol dehydratase from Klebsiella pneumoniae 2e with high tolerance against crude glycerol impurities.Biotechnology for biofuels and bioproducts · 2023Article
- Targeted Mutation of a Non-catalytic Gating Residue Increases the Rate ofJournal of agricultural and food chemistry · 2023Article
- Customized multiple sequence alignment as an effective strategy to improve performance of Taq DNA polymerase.Applied microbiology and biotechnology · 2023Article
11 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flexible sites are potential targets for engineering the stability of enzymes. Nevertheless, the success rate of the rigidifying flexible sites (RFS) strategy is still low due to a limited understanding of how to determine the best mutation candidates. In this study, two parallel strategies were applied to identify mutation candidates within the flexible loops of Escherichia coli transketolase (TK). The first was a "back to consensus mutations" approach, and the second was computational design based on ΔΔG calculations in Rosetta. Forty-nine single variants were generated and characterised experimentally. From these, three single-variants I189H, A282P, D143K were found to be more thermostable than wild-type TK. The combination of A282P with H192P, a variant constructed previously, resulted in the best all-round variant with a 3-fold improved half-life at 60 °C, 5-fold increased specific activity at 65 °C, 1.3-fold improved k
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