ReviewPathogens (Basel, Switzerland)2016
Legionella pneumophila Carbonic Anhydrases: Underexplored Antibacterial Drug Targets.
Review in Pathogens (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 43 citations in OpenAlex.
- Article
- Carbonic Anhydrase Inhibitors as Novel Antibacterials in the Era of Antibiotic Resistance: Where Are We Now?Antibiotics (Basel, Switzerland) · 2023Review
- A Highlight on the Inhibition of Fungal Carbonic Anhydrases as Drug Targets for the Antifungal Armamentarium.International journal of molecular sciences · 2021Review
- Active Nanointerfaces Based on Enzyme Carbonic Anhydrase and Metal-Organic Framework for Carbon Dioxide Reduction.Nanomaterials (Basel, Switzerland) · 2021Article
- Effect of Sulfonamides and Their Structurally Related Derivatives on the Activity of ι-Carbonic Anhydrase fromInternational journal of molecular sciences · 2021Article
- Carbonic Anhydrases: New Perspectives on Protein Functional Role and Inhibition inFrontiers in microbiology · 2021Review
- Transcriptomic Analysis ofFrontiers in microbiology · 2021Article
- Microbiota, Bacterial Carbonic Anhydrases, and Modulators of Their Activity: Links to Human Diseases?Mediators of inflammation · 2021Review
- Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Anion Inhibition Studies of the β-Class Carbonic Anhydrase CAS3 from the Filamentous AscomyceteMetabolites · 2020Article
- Sulfonamide Inhibition Profile of the β-Carbonic Anhydrase fromMetabolites · 2020Article
- A Carbonic Anhydrase Pseudogene Sensitizes SelectJournal of bacteriology · 2019Article
- Comparison of the Sulfonamide Inhibition Profiles of the α-Carbonic Anhydrase Isoforms (SpiCA1, SpiCA2 and SpiCA3) Encoded by the Genome of the Scleractinian CoralMarine drugs · 2019Article
- Anion inhibition studies of a beta carbonic anhydrase from the malaria mosquito Anopheles gambiae.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- An Overview of the Bacterial Carbonic Anhydrases.Metabolites · 2017Review
- Comparison of the Sulfonamide Inhibition Profiles of the β- and γ-Carbonic Anhydrases from the Pathogenic Bacterium Burkholderia pseudomallei.Molecules (Basel, Switzerland) · 2017Article
- Microbial Carbonic Anhydrases in Biomimetic Carbon Sequestration for Mitigating Global Warming: Prospects and Perspectives.Frontiers in microbiology · 2017Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carbonic anhydrases (CAs, EC 4.2.1.1) are metalloenzymes which catalyze the hydration of carbon dioxide to bicarbonate and protons. Many pathogenic bacteria encode such enzymes belonging to the α-, β-, and/or γ-CA families. In the last decade, enzymes from some of these pathogens, including Legionella pneumophila, have been cloned and characterized in detail. These enzymes were shown to be efficient catalysts for CO₂ hydration, with kcat values in the range of (3.4-8.3) × 10⁵ s(-1) and kcat/KM values of (4.7-8.5) × 10⁷ M(-1)·s(-1). In vitro inhibition studies with various classes of inhibitors, such as anions, sulfonamides and sulfamates, were also reported for the two β-CAs from this pathogen, LpCA1 and LpCA2. Inorganic anions were millimolar inhibitors, whereas diethyldithiocarbamate, sulfamate, sulfamide, phenylboronic acid, and phenylarsonic acid were micromolar ones. The best LpCA1 inhibitors were aminobenzolamide and structurally similar sulfonylated aromatic sulfonamides, as well as acetazolamide and ethoxzolamide (KIs in the range of 40.3-90.5 nM). The best LpCA2 inhibitors belonged to the same class of sulfonylated sulfonamides, together with acetazolamide, methazolamide, and dichlorophenamide (KIs in the range of 25.2-88.5 nM). Considering such preliminary results, the two bacterial CAs from this pathogen represent promising yet underexplored targets for obtaining antibacterials devoid of the resistance problems common to most of the clinically used antibiotics, but further studies are needed to validate them in vivo as drug targets.
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