ArticlePloS one2015
Structural Basis for the Inhibition of Helicobacter pylori α-Carbonic Anhydrase by Sulfonamides.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 52 citations in OpenAlex.
- Beyond Urease: New Potential Enzymatic Targets inACS omega · 2026Review
- Roles of three carbonic anhydrases inFEMS microbes · 2026Article
- Challenges and Prospects for Eradication ofPathogens (Basel, Switzerland) · 2025Review
- Sulfonamide-Based Inhibition of the β-Carbonic Anhydrase fromInternational journal of molecular sciences · 2024Article
- Inhibition studies with simple and complex (in)organic anions of the γ-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2023Article
- Repurposing FDA-approved sulphonamide carbonic anhydrase inhibitors for treatment ofJournal of enzyme inhibition and medicinal chemistry · 2022Article
- Inhibition of α-, β- and γ-carbonic anhydrases from the pathogenic bacteriumJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Carbonic Anhydrases: New Perspectives on Protein Functional Role and Inhibition inFrontiers in microbiology · 2021Review
- Benzoxaboroles: New Potent Inhibitors of the Carbonic Anhydrases of the Pathogenic BacteriumACS medicinal chemistry letters · 2020Article
- Alpha-Carbonic Anhydrases from Hydrothermal Vent Sources as Potential Carbon Dioxide Sequestration Agents:International journal of molecular sciences · 2020Article
- Flavodoxins as Novel Therapeutic Targets againstInternational journal of molecular sciences · 2020Review
- Antibacterial activity of ethoxzolamide againstGut pathogens · 2020Article
- Phaeodactylum tricornutum as a model organism for testing the membrane penetrability of sulphonamide carbonic anhydrase inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Anti-Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Seeking new approach for therapeutic treatment of cholera disease via inhibition of bacterial carbonic anhydrases: experimental and theoretical studies for sixteen benzenesulfonamide derivatives.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Crystal Structure of a Highly Thermostable α-Carbonic Anhydrase from Persephonella marina EX-H1.Molecules and cells · 2019Article
- Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- An Overview of the Bacterial Carbonic Anhydrases.Metabolites · 2017Review
- Carbonic Anhydrase from Porphyromonas Gingivalis as a Drug Target.Pathogens (Basel, Switzerland) · 2017Review
- Comparison of the Sulfonamide Inhibition Profiles of the β- and γ-Carbonic Anhydrases from the Pathogenic Bacterium Burkholderia pseudomallei.Molecules (Basel, Switzerland) · 2017Article
Corrections and comments
- Erratum issuedCorrection: Structural Basis for the Inhibition of Helicobacter pylori α-Carbonic Anhydrase by Sulfonamides.2015 · Modakh, Joyanta K [corrected to Modak, Joyanta K]
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Periplasmic α-carbonic anhydrase of Helicobacter pylori (HpαCA), an oncogenic bacterium in the human stomach, is essential for its acclimation to low pH. It catalyses the conversion of carbon dioxide to bicarbonate using Zn(II) as the cofactor. In H. pylori, Neisseria spp., Brucella suis and Streptococcus pneumoniae this enzyme is the target for sulfonamide antibacterial agents. We present structural analysis correlated with inhibition data, on the complexes of HpαCA with two pharmacological inhibitors of human carbonic anhydrases, acetazolamide and methazolamide. This analysis reveals that two sulfonamide oxygen atoms of the inhibitors are positioned proximal to the putative location of the oxygens of the CO2 substrate in the Michaelis complex, whilst the zinc-coordinating sulfonamide nitrogen occupies the position of the catalytic water molecule. The structures are consistent with acetazolamide acting as site-directed, nanomolar inhibitors of the enzyme by mimicking its reaction transition state. Additionally, inhibitor binding provides insights into the channel for substrate entry and product exit. This analysis has implications for the structure-based design of inhibitors of bacterial carbonic anhydrases.
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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.