ArticleProtein engineering, design & selection : PEDS2012
Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II.
Article in Protein engineering, design & selection : PEDS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 59 citations in OpenAlex.
- Bioinspired Zinc Macrocycles Confined in UiO-67: A Heterogeneous Synzyme for Sustainable COChemSusChem · 2026Article
- Directed evolution of an ultrastable carbonic anhydrase fromComputational and structural biotechnology journal · 2025Article
- Article
- Switching the Inhibitor-Enzyme Recognition Profile via Chimeric Carbonic Anhydrase XII.ChemistryOpen · 2021Article
- Structural and thermodynamic analysis of factors governing the stability and thermal folding/unfolding of SazCA.PloS one · 2021Article
- Structural insights into a thermostable variant of human carbonic anhydrase II.Protein science : a publication of the Protein Society · 2018Article
- Microbial Carbonic Anhydrases in Biomimetic Carbon Sequestration for Mitigating Global Warming: Prospects and Perspectives.Frontiers in microbiology · 2017Review
- Engineering de novo disulfide bond in bacterial α-type carbonic anhydrase for thermostable carbon sequestration.Scientific reports · 2016Article
- Thermostable Carbonic Anhydrases in Biotechnological Applications.International journal of molecular sciences · 2015Review
- Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase II.The FEBS journal · 2015Article
- Interactions between Hofmeister anions and the binding pocket of a protein.Journal of the American Chemical Society · 2015Article
- Increased water flux induced by an aquaporin-1/carbonic anhydrase II interaction.Molecular biology of the cell · 2015Article
- Structural elucidation of the hormonal inhibition mechanism of the bile acid cholate on human carbonic anhydrase II.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Carbonic anhydrases and their biotechnological applications.Biomolecules · 2013Article
- Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond.Acta crystallographica. Section D, Biological crystallography · 2013Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Carbonic anhydrases (CAs) are ubiquitous enzymes that catalyze the reversible hydration/dehydration of carbon dioxide/bicarbonate. As such, there is enormous industrial interest in using CA as a bio-catalyst for carbon sequestration and biofuel production. However, to ensure cost-effective use of the enzyme under harsh industrial conditions, studies were initiated to produce variants with enhanced thermostability while retaining high solubility and catalytic activity. Kinetic and structural studies were conducted to determine the structural and functional effects of these mutations. X-ray crystallography revealed that a gain in surface hydrogen bonding contributes to stability while retaining proper active site geometry and electrostatics to sustain catalytic efficiency. The kinetic profiles determined under a variety of conditions show that the surface mutations did not negatively impact the carbon dioxide hydration or proton transfer activity of the enzyme. Together these results show that it is possible to enhance the thermal stability of human carbonic anhydrase II by specific replacements of surface hydrophobic residues of the enzyme. In addition, combining these stabilizing mutations with strategic active site changes have resulted in thermostable mutants with desirable kinetic properties.
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