Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii

References

• (a) Supuran CT. Structure and function of carbonic anhydrases. Biochem J 2016;473:2023–32.
   PubMed Web of Science ®Google Scholar
  (b) Capasso C, Supuran CT. An overview of the alpha-, beta- and gamma-carbonic anhydrases from Bacteria: can bacterial carbonic anhydrases shed new light on evolution of bacteria? J Enzyme Inhib Med Chem 2015;30:325–32.
   PubMed Web of Science ®Google Scholar
  (c) Mishra CB, Tiwari M, Supuran CT. Progress in the development of human carbonic anhydrase inhibitors and their pharmacological applications: where are we today? Med Res Rev 2020;40:2485–565.
   PubMed Web of Science ®Google Scholar
• (a) Jensen EL, Clement R, Kosta A, et al. A new widespread subclass of carbonic anhydrase in marine phytoplankton. Isme J 2019;13:2094–106.
   PubMed Web of Science ®Google Scholar
  (b) Del Prete S, Nocentini A, Supuran CT, Capasso C. Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii. J Enzyme Inhib Med Chem 2020;35:1060–8.
   PubMed Web of Science ®Google Scholar
• (a) Ozensoy Guler O, Capasso C, Supuran CT. A magnificent enzyme superfamily: carbonic anhydrases, their purification and characterization. J Enzyme Inhib Med Chem 2016;31:689–94.
   PubMed Web of Science ®Google Scholar
  (b) Kikutani S, Nakajima K, Nagasato C, et al. Thylakoid luminal theta-carbonic anhydrase critical for growth and photosynthesis in the marine diatom Phaeodactylum tricornutum. Proc Natl Acad Sci U S A 2016;113:9828–33.
   PubMed Web of Science ®Google Scholar
  (c) Jin S, Vullo D, Bua S, et al. Structural and biochemical characterization of novel carbonic anhydrases from Phaeodactylum tricornutum. Acta Crystallogr D Struct Biol 2020;76:676–86.
   PubMedGoogle Scholar
  (d) Del Prete S, Bua S, Supuran CT, Capasso C. Escherichia coli γ-carbonic anhydrase: characterisation and effects of simple aromatic/heterocyclic sulphonamide inhibitors. J Enzyme Inhib Med Chem 2020;35:1545–54.
   PubMed Web of Science ®Google Scholar
• (a) Capasso C, Supuran CT. Bacterial, fungal and protozoan carbonic anhydrases as drug targets. Expert Opin Ther Targets 2015;19:1689–704.
   PubMed Web of Science ®Google Scholar
  (b) Supuran CT, Capasso C. The eta-class carbonic anhydrases as drug targets for antimalarial agents. Expert Opin Ther Targets 2015;19:551–63.
   PubMed Web of Science ®Google Scholar
  (c) Supuran CT, Capasso C. Antibacterial carbonic anhydrase inhibitors: an update on the recent literature. Expert Opin Ther Pat 2020.
   Web of Science ®Google Scholar
• (a) Supuran CT. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov 2008;7:168–81.
   PubMed Web of Science ®Google Scholar
  (b) Neri D, Supuran CT. Interfering with pH regulation in tumours as a therapeutic strategy. Nat Rev Drug Discov 2011; 10:767–77.
   PubMed Web of Science ®Google Scholar
  (c) Supuran CT. Carbonic anhydrases and metabolism. Metabolites 2018; 8:25.
   PubMed Web of Science ®Google Scholar
  (d) Supuran CT. Exploring the multiple binding modes of inhibitors to carbonic anhydrases for novel drug discovery. Expert Opin Drug Discov 2020;15:671–86.
   PubMed Web of Science ®Google Scholar
• (a) Urbański LJ, Di Fiore A, Azizi L, et al. Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase from Trichomonas vaginalis. J Enzyme Inhib Med Chem 2020;35:1292–9.
   PubMed Web of Science ®Google Scholar
  (b) Nocentini A, Supuran CT. Advances in the structural annotation of human carbonic anhydrases and impact on future drug discovery. Expert Opin Drug Discov 2019; 14:1175–97.
   PubMed Web of Science ®Google Scholar
  (c) Supuran CT. Structure-based drug discovery of carbonic anhydrase inhibitors. J. Enzyme Inhib. Med. Chem 2012; 27:759–72.
   PubMed Web of Science ®Google Scholar
  (d) Supuran CT. How many carbonic anhydrase inhibition mechanisms exist? J Enzyme Inhib Med Chem 2016; 31:345–60.
   PubMed Web of Science ®Google Scholar
• (a) Alterio V, Di Fiore A, D’Ambrosio K, et al. Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms? Chem Rev 2012; 112:4421–68.
   PubMed Web of Science ®Google Scholar
  (b) Angeli A, Carta F, Nocentini A, et al. Carbonic anhydrase inhibitors targeting metabolism and tumor microenvironment. Metabolites 2020;10:412.
   PubMed Web of Science ®Google Scholar
  (c) Supuran CT, Alterio V, Di Fiore A, et al. Inhibition of carbonic anhydrase IX targets primary tumors, metastases, and cancer stem cells: three for the price of one. Med Res Rev 2018;38:1799–836.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. Carbonic anhydrase inhibitors and their potential in a range of therapeutic areas. Expert Opin Ther Pat 2018;28:709–12.
   PubMed Web of Science ®Google Scholar
  (b) Scozzafava A, Supuran CT, Carta F. Antiobesity carbonic anhydrase inhibitors: a literature and patent review. Expert Opin Ther Pat 2013; 23:725–35.
   PubMed Web of Science ®Google Scholar
  (c) Di Cesare Mannelli L, Micheli L, Carta F, et al. Carbonic anhydrase inhibition for the management of cerebral ischemia: in vivo evaluation of sulfonamide and coumarin inhibitors. Enzyme Inhib Med Chem 2016;31:894–9.
   PubMed Web of Science ®Google Scholar
  (d) Supuran CT, Altamimi ASA, Carta F. Carbonic anhydrase inhibition and the management of glaucoma: a literature and patent review 2013–2019. Expert Opin Ther Pat 2019; 29:781–92.
   PubMed Web of Science ®Google Scholar
  (e) Supuran CT. The management of glaucoma and macular degeneration. Expert Opin Ther Pat 2019; 29:745–7.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. Carbonic anhydrase activators. Future Med Chem 2018;10:561–73.
   PubMed Web of Science ®Google Scholar
  (b) Blandina P, Provensi G, Passani MB, et al. Carbonic anhydrase 5. Implications for the treatment of cognitive disorders. J Enzyme Inhib Med Chem 2020;35:1206–14.
   PubMed Web of Science ®Google Scholar
  (c) Nocentini A, Cuffaro D, Ciccone L, et al. Activation of carbonic anhydrases from human brain by amino alcohol oxime ethers: towards human carbonic anhydrase VII selective activators. J Enzyme Inhib Med Chem 2021;36:48–57.
   PubMed Web of Science ®Google Scholar
• (a) Schmidt SD, Costa A, Rani B, et al. The role of carbonic anhydrases in extinction of contextual fear memory. Proc Natl Acad Sci U S A 2020;117:16000–8.
   PubMed Web of Science ®Google Scholar
  (b) Canto de Souza L, Provensi G, Vullo D, et al. Carbonic anhydrase activation enhances object recognition memory in mice through phosphorylation of the extracellular signal-regulated kinase in the cortex and the hippocampus. Neuropharmacology 2017;118:148–56.
   PubMed Web of Science ®Google Scholar
• (a) Del Prete S, De Luca V, Bua S, et al. The effect of substituted benzene-sulfonamides and clinically licensed drugs on the catalytic activity of CynT2, a carbonic anhydrase crucial for Escherichia coli life cycle. Int J Mol Sci 2020; 21:4175.
   PubMed Web of Science ®Google Scholar
  (b) Angeli A, Ferraroni M, Pinteala M, et al. Crystal structure of a tetrameric type II β-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei. Molecules 2020; 25:2269.
   Web of Science ®Google Scholar
  (c) Gitto R, De Luca L, Mancuso F, et al. Seeking new approach for therapeutic treatment of cholera disease via inhibition of bacterial carbonic anhydrases: experimental and theoretical studies for sixteen benzenesulfonamide derivatives. J Enzyme Inhib Med Chem 2019; 34:1186–92.
   PubMed Web of Science ®Google Scholar
  (d) Angeli A, Pinteala M, Maier SS, et al. Inhibition of α-, β-, γ-, δ-, ζ- and η-class carbonic anhydrases from bacteria, fungi, algae, diatoms and protozoans with famotidine. J Enzyme Inhib Med Chem 2019; 34:644–50.
   PubMed Web of Science ®Google Scholar
• (a) Capasso C, Supuran CT. An overview of the selectivity and efficiency of the bacterial carbonic anhydrase inhibitors. Curr Med Chem 2015;22:2130–9.
   PubMed Web of Science ®Google Scholar
  (b) Capasso C, Supuran CT. An overview of the carbonic anhydrases from two pathogens of the oral cavity: Streptococcus mutans and Porphyromonas gingivalis. Curr Top Med Chem 2016;16:2359–68.
   PubMed Web of Science ®Google Scholar
• Kaur J, Cao X, Abutaleb NS, et al. Optimization of acetazolamide-based scaffold as potent inhibitors of vancomycin-resistant Enterococcus. J Med Chem 2020;63:9540–62.
   PubMed Web of Science ®Google Scholar
• (a) D'Ambrosio K, Supuran CT, De Simone G. Are carbonic anhydrases suitable targets to fight protozoan parasitic diseases? Curr Med Chem 2018;25:5266–78.
   PubMed Web of Science ®Google Scholar
  (b) Nocentini A, Osman SM, Almeida IA, et al. Appraisal of anti-protozoan activity of nitroaromatic benzenesulfonamides inhibiting carbonic anhydrases from Trypanosoma cruzi and Leishmania donovani. J Enzyme Inhib Med Chem 2019;34:1164–71.
   PubMed Web of Science ®Google Scholar
  (c) da Silva Cardoso V, Vermelho AB, Ricci Junior E, et al. Antileishmanial activity of sulphonamide nanoemulsions targeting the β-carbonic anhydrase from Leishmania species. J Enzyme Inhib Med Chem 2018;33:850–7.
   PubMed Web of Science ®Google Scholar
• (a) Vermelho AB, Rodrigues GC, Supuran CT. Why hasn’t there been more progress in new Chagas disease drug discovery? Expert Opin Drug Discov 2020;15:145–58.
   PubMed Web of Science ®Google Scholar
  (b) Angeli A, Etxebeste-Mitxeltorena M, Sanmartín C, et al. Tellurides bearing sulfonamides as novel inhibitors of leishmanial carbonic anhydrase with potent antileishmanial activity. J Med Chem 2020;63:4306–14.
   PubMed Web of Science ®Google Scholar
  (c) Vermelho AB, da Silva Cardoso V, Ricci Junior E, et al. Nanoemulsions of sulfonamide carbonic anhydrase inhibitors strongly inhibit the growth of Trypanosoma cruzi. J Enzyme Inhib Med Chem 2018;33:139–46.
   PubMed Web of Science ®Google Scholar
  (d) Vermelho AB, Capaci GR, Rodrigues IA, et al. Carbonic anhydrases from Trypanosoma and Leishmania as anti-protozoan drug targets. Bioorg Med Chem 2017;25:1543–55.
   PubMed Web of Science ®Google Scholar
• (a) Del Prete S, Vullo D, Ghobril C, et al. Cloning, purification, and characterization of a beta-carbonic anhydrase from Malassezia restricta, an opportunistic pathogen involved in dandruff and seborrheic dermatitis. Int J Mol Sci 2019;20:2447.
   PubMed Web of Science ®Google Scholar
  (b) Angeli A, Prete SD, Ghobril C, et al. Activation studies of the β-carbonic anhydrases from Malassezia restricta with amines and amino acids. J Enzyme Inhib Med Chem 2020;35:824–30.
   PubMed Web of Science ®Google Scholar
• (a) Nocentini A, Vullo D, Del Prete S, et al. Inhibition of the β-carbonic anhydrase from the dandruff-producing fungus Malassezia globosa with monothiocarbamates. J Enzyme Inhib Med Chem 2017;32:1064–70.
   PubMed Web of Science ®Google Scholar
  (b) Angiolella L, Carradori S, Maccallini C, et al. Targeting Malassezia species for novel synthetic and natural antidandruff agents. Curr Med Chem 2017;24:2392–412.
   PubMed Web of Science ®Google Scholar
  (c) Hewitson KS, Vullo D, Scozzafava A, et al. Molecular cloning, characterization, and inhibition studies of a β-carbonic anhydrase from Malassezia globosa, a potential antidandruff target. J Med Chem 2012;55:3513–20.
   PubMed Web of Science ®Google Scholar
• (a) De Luca V, Del Prete S, Supuran CT, Capasso C. Protonography, a new technique for the analysis of carbonic anhydrase activity. J Enzyme Inhib Med Chem 2015;30:277–82.
   PubMed Web of Science ®Google Scholar
  (b) Del Prete S, De Luca V, Supuran CT, Capasso C. Protonography, a technique applicable for the analysis of η-carbonic anhydrase activity. J Enzyme Inhib Med Chem 2015;30:920–4.
   PubMed Web of Science ®Google Scholar
  (c) Del Prete S, De Luca V, Iandolo E, et al. Protonography, a powerful tool for analyzing the activity and the oligomeric state of the γ-carbonic anhydrase identified in the genome of Porphyromonas gingivalis. Bioorg Med Chem 2015;23:3747–50.
   PubMed Web of Science ®Google Scholar
• (a) De Simone G, Supuran CT. (In)organic anions as carbonic anhydrase inhibitors. J Inorg Biochem 2012;111:117–29.
   PubMed Web of Science ®Google Scholar
  (b) Bertucci A, Moya A, Tambutté S, et al. Carbonic anhydrases in anthozoan corals – a review. Bioorg Med Chem 2013;21:1437–50.
   PubMed Web of Science ®Google Scholar
• Khalifah RG. The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C. J Biol Chem 1971; 246:2561–73.
   PubMed Web of Science ®Google Scholar
• (a) Maresca A, Scozzafava A, Supuran C7. 8-Disubstituted- but not 6,7-disubstituted coumarins selectively inhibit the transmembrane, tumor-associated carbonic anhydrase isoforms IX and XII over the cytosolic ones I and II in the low nanomolar/subnanomolar range. Bioorg Med Chem Lett 2010;20:7255–8.
   PubMed Web of Science ®Google Scholar
  (b) Innocenti A, Gülçin I, Scozzafava A, Supuran CT. Carbonic anhydrase inhibitors. Antioxidant polyphenols effectively inhibit mammalian isoforms I-XV. Bioorg Med Chem Lett 2010;20:5050–3.
   PubMed Web of Science ®Google Scholar
  (c) Supuran CT, Nicolae A, Popescu A. Carbonic anhydrase inhibitors. Part 35. Synthesis of Schiff bases derived from sulfanilamide and aromatic aldehydes: the first inhibitors with equally high affinity towards cytosolic and membrane-bound isozymes. Eur J Med Chem 1996; 31:431–8.
   Web of Science ®Google Scholar
  (d) Beyza Öztürk Sarıkaya S, Gülçin İ, Supuran CT. Carbonic anhydrase inhibitors: Inhibition of human erythrocyte isozymes I and II with a series of phenolic acids. Chem Biol Drug Des 2010; 75:515–20.
   PubMed Web of Science ®Google Scholar
• (a) Tripp BC, Bell CB 3rd, Cruz F, et al. A role for iron in an ancient carbonic anhydrase. J Biol Chem 2004;279:6683–7.
   PubMed Web of Science ®Google Scholar
  (b) Zimmerman SA, Ferry JG, Supuran CT. Inhibition of the archaeal β-class (Cab) and γ-class (Cam) carbonic anhydrases. Curr Top Med Chem 2007; 7:901–8.
   PubMed Web of Science ®Google Scholar
• (a) Xu Y, Feng L, Jeffrey PD, et al. Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms. Nature 2008;452:56–61.
   PubMed Web of Science ®Google Scholar
  (b) Viparelli F, Monti SM, De Simone G, et al. Inhibition of the R1 fragment of the cadmium-containing zeta-class carbonic anhydrase from the diatom Thalassiosira weissflogii with anions. Bioorg Med Chem Lett 2010; 20:4745–8.
   PubMed Web of Science ®Google Scholar
  (c) Alterio V, Langella E, Viparelli F, et al. Structural and inhibition insights into carbonic anhydrase CDCA1 from the marine diatom Thalassiosira weissflogii. Biochimie 2012; 94:1232–41.
   PubMed Web of Science ®Google Scholar
• Del Prete S, De Luca V, Nocentini A, et al. Anion inhibition studies of the beta-carbonic anhydrase from Escherichia coli. Molecules 2020;25:2564.
   PubMed Web of Science ®Google Scholar