ArticleJournal of enzyme inhibition and medicinal chemistry2018
Activation of β- and γ-carbonic anhydrases from pathogenic bacteria with tripeptides.
Article in Journal of enzyme inhibition and medicinal chemistry, 2018. 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, 37 citations in OpenAlex.
- Synthesis, Biological and In Silico Studies of Griseofulvin and Usnic Acid Sulfonamide Derivatives as Fungal, Bacterial and Human Carbonic Anhydrase Inhibitors.International journal of molecular sciences · 2023Article
- Activation studies with amino acids and amines of a β-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2022Article
- Pyrazolo[4,3-c]pyridine Sulfonamides as Carbonic Anhydrase Inhibitors: Synthesis, Biological and In Silico Studies.Pharmaceuticals (Basel, Switzerland) · 2022Article
- An Update on Synthesis of Coumarin Sulfonamides as Enzyme Inhibitors and Anticancer Agents.Molecules (Basel, Switzerland) · 2022Review
- Amine- and Amino Acid-Based Compounds as Carbonic Anhydrase Activators.Molecules (Basel, Switzerland) · 2021Review
- Effect of amino acids and amines on the activity of the recombinant ι-carbonic anhydrase from the Gram-negative bacteriumJournal of enzyme inhibition and medicinal chemistry · 2021Article
- New Sulfanilamide Derivatives Incorporating Heterocyclic Carboxamide Moieties as Carbonic Anhydrase Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Activation studies of the β-carbonic anhydrases fromJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Crystal Structure of a Tetrameric Type II β-Carbonic Anhydrase from the Pathogenic BacteriumMolecules (Basel, Switzerland) · 2020Article
- The first activation study of the β-carbonic anhydrases from the pathogenic bacteriaJournal 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
- (Hetero)aryl substituted thiazol-2,4-yl scaffold as human carbonic anhydrase I, II, VII and XIV activators.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Activation Studies of the γ-Carbonic Anhydrases from the Antarctic Marine BacteriaMarine drugs · 2019Article
- Accelerated CO₂ Hydration with ThermostableInternational journal of molecular sciences · 2019Article
- Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Six tripeptides incorporating acidic amino acid residues were prepared for investigation as activators of β- and γ-carbonic anhydrases (CAs, EC 4.2.1.1) from the pathogenic bacteria Vibrio cholerae, Mycobacterium tuberculosis, and Burkholderia pseudomallei. The primary amino acid residues that are involved in the catalytic mechanisms of these CA classes are poorly understood, although glutamic acid residues near the active site appear to be involved. The tripeptides that contain Glu or Asp residues can effectively activate VchCAβ and VchCAγ (enzymes from V. cholerae), Rv3273 CA (mtCA3, a β-CA from M. tuberculosis) and BpsCAγ (γ-CA from B. pseudomallei) at 0.21-18.1 µM levels. The position of the acidic residues in the peptide sequences can significantly affect bioactivity. For three of the enzymes, tripeptides were identified that are more effective activators than both l-Glu and l-Asp. The tripeptides are also relatively selective because they do not activate prototypical α-CAs (human carbonic anhydrases I and II). Because the role of CA activators in the pathogenicity and life cycles of these infectious bacteria are poorly understood, this study provides new molecular probes to explore such processes.
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