ArticleInternational journal of molecular sciences2018
The Crystal Structure of a hCA VII Variant Provides Insights into the Molecular Determinants Responsible for Its Catalytic Behavior.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- Novel 1,3,5-Triazinyl Aminobenzenesulfonamides Incorporating Aminoalcohol, Aminochalcone and Aminostilbene Structural Motifs as Potent Anti-VRE Agents, and Carbonic Anhydrases I, II, VII, IX, and XII Inhibitors.International journal of molecular sciences · 2021Article
- Combined effect of starch and sucrose on carbonic anhydrase VI activity in saliva and biofilm of children with early childhood caries. Exposure to starch and sucrose alters carbonic anhydrase VI activity in saliva and biofilm.Clinical oral investigations · 2021Article
- The role of mechanical control of biofilm in the salivary pH after sucrose exposure in children with early childhood caries.Scientific reports · 2021Article
- Intrinsically disordered features of carbonic anhydrase IX proteoglycan-like domain.Cellular and molecular life sciences : CMLS · 2021Review
- Activation studies of the β-carbonic anhydrases fromJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Phenyl(thio)phosphon(amid)ate Benzenesulfonamides as Potent and Selective Inhibitors of Human Carbonic Anhydrases II and VII Counteract Allodynia in a Mouse Model of Oxaliplatin-Induced Neuropathy.Journal of medicinal chemistry · 2020Article
- Study of the role of MgJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Exploration of the residues modulating the catalytic features of human carbonic anhydrase XIII by a site-specific mutagenesis approach.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Activation of human α-carbonic anhydrase isoforms I, II, IV and VII with bis-histamine schiff bases and bis-spinaceamine substituted derivatives.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Mechanism of Action of Non-Synonymous Single Nucleotide Variations Associated withMolecules (Basel, Switzerland) · 2019Article
- Protective Role of Carbonic Anhydrases III and VII in Cellular Defense Mechanisms upon Redox Unbalance.Oxidative medicine and cellular longevity · 2018Review
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Authors and funding
7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Although important progress has been achieved in understanding the catalytic mechanism of Carbonic Anhydrases, a detailed picture of all factors influencing the catalytic efficiency of the various human isoforms is still missing. In this paper we report a detailed structural study and theoretical pKa calculations on a hCA VII variant. The obtained data were compared with those already known for another thoroughly investigated cytosolic isoform, hCA II. Our structural studies show that in hCA VII the network of ordered water molecules, which connects the zinc bound solvent molecule to the proton shuttle His64, is altered compared to hCA II, causing a reduction of the catalytic efficiency. Theoretical calculations suggest that changes in solvent network are related to the difference in pKa of the proton shuttle in the two enzymes. The residue that plays a major role in determining the diverse pKa values of the proton shuttle is the one in position four, namely His for hCA II and Gly for hCA VII. This residue is located on the protein surface, outside of the active site cavity. These findings are in agreement with our previous studies that highlighted the importance of histidines on the protein surface of hCA II (among which His4) as crucial residues for the high catalytic efficiency of this isoform.
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