ArticleNature communications2015
Rational engineering of a mesohalophilic carbonic anhydrase to an extreme halotolerant biocatalyst.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- The gift that shaped my career in science.Nature · 2025Article
- Exploring the Catalytic Mechanisms of a Newly Identified Salt-Activated Alginate Lyase fromMarine drugs · 2025Article
- Characterization of a NaWorld journal of microbiology & biotechnology · 2025Article
- Article
- Ion-combination specific effects driving the enzymatic activity of halophilic alcohol dehydrogenase 2 fromRSC sustainability · 2024Article
- Alpha Carbonic Anhydrase fromInternational journal of molecular sciences · 2024Article
- Engineering diaryl alcohol dehydrogenase KpADH reveals importance of retaining hydration shell in organic solvent tolerance.Protein science : a publication of the Protein Society · 2024Article
- Clustered surface amino acid residues modulate the acid stability of GH10 xylanase in fungi.Applied microbiology and biotechnology · 2024Article
- Functional characterisation of a new halotolerant seawater active glycoside hydrolase family 6 cellobiohydrolase from a salt marsh.Scientific reports · 2024Article
- Expression and functional study of DNA polymerases fromFrontiers in microbiology · 2024Article
- Biochemical characterization of a psychrophilic and halotolerant α-carbonic anhydrase from a deep-sea bacterium,AIMS microbiology · 2023Article
- Expression of a Salt-Tolerant Pseudolysin in Yeast for Efficient Protein Hydrolysis under High-Salt Conditions.Biomolecules · 2022Article
- Characterization of a Novel Polysaccharide Lyase Family 5 Alginate Lyase with PolyM Substrate Specificity.Foods (Basel, Switzerland) · 2022Article
- Activation and thermal stabilization of a recombinant γ-glutamyltranspeptidase from Bacillus licheniformis ATCC 27811 by monovalent cations.Applied microbiology and biotechnology · 2022Article
- Deletion of the Loop Linking Two Domains of Exo-Inulinase InuAMN8 Diminished the Enzymatic Thermo-Halo-Alcohol Tolerance.Frontiers in microbiology · 2022Article
- Proteins maintain hydration at high [KCl] concentration regardless of content in acidic amino acids.Biophysical journal · 2021Article
- Chimeric Phi29 DNA polymerase with helix-hairpin-helix motifs shows enhanced salt tolerance and replication performance.Microbial biotechnology · 2021Article
- Extremophilic Prokaryotic Endoxylanases: Diversity, Applicability, and Molecular Insights.Frontiers in microbiology · 2021Review
- DeepREx-WS: A web server for characterising protein-solvent interaction starting from sequence.Computational and structural biotechnology journal · 2021Article
- Engineering Robust Cellulases for Tailored Lignocellulosic Degradation Cocktails.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes expressed by highly salt-tolerant organisms show many modifications compared with salt-affected counterparts including biased amino acid and lower α-helix content, lower solvent accessibility and negative surface charge. Here, we show that halotolerance can be generated in an enzyme solely by modifying surface residues. Rational design of carbonic anhydrase II is undertaken in three stages replacing 18 residues in total, crystal structures confirm changes are confined to surface residues. Catalytic activities and thermal unfolding temperatures of the designed enzymes increase at high salt concentrations demonstrating their shift to halotolerance, whereas the opposite response is found in the wild-type enzyme. Molecular dynamics calculations reveal a key role for sodium ions in increasing halotolerant enzyme stability largely through interactions with the highly ordered first Na(+) hydration shell. For the first time, an approach to generate extreme halotolerance, a trait with broad application in industrial biocatalysis, in a wild-type enzyme is demonstrated.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.