ArticleIUCrJ2020
Structural insights into the effect of active-site mutation on the catalytic mechanism of carbonic anhydrase.
Article in IUCrJ, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Introduction to Carbonic Anhydrase.Sub-cellular biochemistry · 2026Review
- Suppressing Glycerol-3-phosphate Phosphatase and Enhancing Glycerol-3-Phosphate Shuttle Flux Crucial for High-Efficiency Fatty Acid Production in the Fast-Growing Oleaginous Schizochytrium.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Conformational flexibility of His200 enables catalytic activity in the T200H mutant of carbonic anhydrase II.Molecules and cells · 2025Article
- Fast product release requires active-site water dynamics in carbonic anhydrase.Nature communications · 2025Article
- A comprehensive investigation of the anion inhibition profile of a β-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2024Article
- Carbonic anhydrase inhibitory activity of phthalimide-capped benzene sulphonamide derivatives.Journal of enzyme inhibition and medicinal chemistry · 2023Article
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Authors and funding
7 authors.
Funding
Abstract
Enzymes are catalysts of biological processes. Significant insight into their catalytic mechanisms has been obtained by relating site-directed mutagenesis studies to kinetic activity assays. However, revealing the detailed relationship between structural modifications and functional changes remains challenging owing to the lack of information on reaction intermediates and of a systematic way of connecting them to the measured kinetic parameters. Here, a systematic approach to investigate the effect of an active-site-residue mutation on a model enzyme, human carbonic anhydrase II (CA II), is described. Firstly, structural analysis is performed on the crystallographic intermediate states of native CA II and its V143I variant. The structural comparison shows that the binding affinities and configurations of the substrate (CO
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