Biomedical applications of prokaryotic carbonic anhydrases

References

• Annunziato G, Angeli A, D’Alba F, et al. Discovery of new potential anti-infective compounds based on carbonic anhydrase inhibitors by rational target-focused repurposing approaches. Chem Med Chem. 2016;11:1904–1914.
   Web of Science ®Google Scholar
• Ozensoy Guler O, Capasso C, Supuran CT. A magnificent enzyme superfamily: carbonic anhydrases, their purification and characterization. J Enzyme Inhib Med Chem. 2016;31:689–694.
   PubMed Web of Science ®Google Scholar
• Del Prete S, Vullo D, De Luca V, et al. Sulfonamide inhibition studies of the beta-carbonic anhydrase from the pathogenic bacterium vibrio cholerae. Bioorg Med Chem. 2016;24:1115–1120.
   PubMed Web of Science ®Google Scholar
• Del Prete S, Vullo D, Fisher GM, et al. Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum–the η-carbonic anhydrases. Bioorg Med Chem Lett. 2014;24:4389–4396.
   PubMed Web of Science ®Google Scholar
• 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;16:2359–2368.
   PubMed Web of Science ®Google Scholar
• Del Prete S, De Luca V, De Simone G, et al. Cloning, expression and purification of the complete domain of the eta-carbonic anhydrase from plasmodium falciparum. J Enzyme Inhib Med Chem. 2016;31:54–59.
   PubMed Web of Science ®Google Scholar
• Del Prete S, Vullo D, De Luca V, et al. Cloning, expression, purification and sulfonamide inhibition profile of the complete domain of the eta-carbonic anhydrase from plasmodium falciparum. Bioorg Med Chem Lett. 2016;26:4184–4190.
   PubMed Web of Science ®Google Scholar
• Del Prete S, Vullo D, De Luca V, et al. di Fonzo P, Osman SM, AlOthman Z, Supuran CT, Capasso C Anion inhibition profiles of the complete domain of the eta-carbonic anhydrase from plasmodium falciparum. Bioorg Med Chem. 2016;24:4410–4414.
   PubMed Web of Science ®Google Scholar
• Del Prete S, Vullo D, De Luca V, et al. Anion inhibition profiles of alpha-, beta- and gamma-carbonic anhydrases from the pathogenic bacterium vibrio cholerae. Bioorg Med Chem. 2016;24:3413–3417.
   PubMed Web of Science ®Google Scholar
• Abdel Gawad NM, Amin NH, Elsaadi MT, et al. Synthesis of 4-(thiazol-2-ylamino)-benzenesulfonamides with carbonic anhydrase i, ii and ix inhibitory activity and cytotoxic effects against breast cancer cell lines. Bioorg Med Chem. 2016;24:3043–3051.
   PubMed Web of Science ®Google Scholar
• Del Prete S, Vullo D, De Luca V, et al. Comparison of the sulfonamide inhibition profiles of the alpha-, beta- and gamma-carbonic anhydrases from the pathogenic bacterium vibrio cholerae. Bioorg Med Chem Lett. 2016;26:1941–1946.
   PubMed Web of Science ®Google Scholar
• Nishimori I, Onishi S, Takeuchi H, et al. The alpha and beta classes carbonic anhydrases from helicobacter pylori as novel drug targets. Curr Pharm Des. 2008;14:622–630.
   PubMed Web of Science ®Google Scholar
• Morishita S, Nishimori I, Minakuchi T, et al. Cloning, polymorphism, and inhibition of beta-carbonic anhydrase of helicobacter pylori. J Gastroenterol. 2008;43:849–857.
   PubMed Web of Science ®Google Scholar
• Capasso C, Supuran CT. Bacterial, fungal and protozoan carbonic anhydrases as drug targets. Expert Opin Ther Targets. 2015;19:1689–1704.
   PubMed Web of Science ®Google Scholar
• Supuran CT, Capasso C. The eta-class carbonic anhydrases as drug targets for antimalarial agents. Expert Opin Ther Targets. 2015;19:551–563.
   PubMed Web of Science ®Google Scholar
• Capasso C, Supuran CT. An overview of the selectivity and efficiency of the bacterial carbonic anhydrase inhibitors. Curr Med Chem. 2015;22:2130–2139.
   PubMed Web of Science ®Google Scholar
• 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;30:325–332.
   PubMed Web of Science ®Google Scholar
• Capasso C, Supuran CT. Sulfa and trimethoprim-like drugs - antimetabolites acting as carbonic anhydrase, dihydropteroate synthase and dihydrofolate reductase inhibitors. J Enzyme Inhib Med Chem. 2014;29:379–387.
   PubMed Web of Science ®Google Scholar
• Capasso C, Supuran CT. Anti-infective carbonic anhydrase inhibitors: A patent and literature review. Expert Opin Ther Pat. 2013;23:693–704.
   PubMed Web of Science ®Google Scholar
• Supuran CT, Capasso C. New light on bacterial carbonic anhydrases phylogeny based on the analysis of signal peptide sequences. J Enzyme Inhib Med Chem. 2016;31:1254–1260.
   PubMed Web of Science ®Google Scholar
• Kusian B, Sultemeyer D, Bowien B. Carbonic anhydrase is essential for growth of ralstonia eutropha at ambient co(2) concentrations. J Bacteriol. 2002;184:5018–5026.
   PubMed Web of Science ®Google Scholar
• Merlin C, Masters M, McAteer S, et al. Why is carbonic anhydrase essential to escherichia coli? J Bacteriol. 2003;185:6415–6424.
   PubMed Web of Science ®Google Scholar
• Cobaxin M, Martinez H, Ayala G, et al. Cholera toxin expression by el tor vibrio cholerae in shallow culture growth conditions. Microb Pathog. 2014;66:5–13.
   PubMed Web of Science ®Google Scholar
• Abuaita BH, Withey JH. Bicarbonate induces vibrio cholerae virulence gene expression by enhancing toxt activity. Infect Immun. 2009;77:4111–4120.
   PubMed Web of Science ®Google Scholar
• Joseph P, Ouahrani-Bettache S, Montero JL, et al. A new beta-carbonic anhydrase from brucella suis, its cloning, characterization, and inhibition with sulfonamides and sulfamates, leading to impaired pathogen growth. Bioorg Med Chem. 2011;19:1172–1178.
   PubMed Web of Science ®Google Scholar
• Modak JK, Liu YC, Machuca MA, et al. Structural basis for the inhibition of helicobacter pylori alpha-carbonic anhydrase by sulfonamides. PLoS One. 2015;10:e0127149.
   PubMed Web of Science ®Google Scholar
• Nishimori I, Vullo D, Minakuchi T, et al. Carbonic anhydrase inhibitors: cloning and sulfonamide inhibition studies of a carboxyterminal truncated alpha-carbonic anhydrase from helicobacter pylori. Bioorg Med Chem Lett. 2006;16:2182–2188.
   PubMed Web of Science ®Google Scholar
• Diaz JR, Fernandez Baldo M, Echeverria G, et al. A substituted sulfonamide and its co (ii), cu (ii), and zn (ii) complexes as potential antifungal agents. J Enzyme Inhib Med Chem. 2016;31:51–62.
   PubMed Web of Science ®Google Scholar
• Del Prete S, Isik S, Vullo D, et al. DNA cloning, characterization, and inhibition studies of an alpha-carbonic anhydrase from the pathogenic bacterium vibrio cholerae. J Med Chem. 2012;55:10742–10748.
   PubMed Web of Science ®Google Scholar
• Vullo D, Del Prete S, De Luca V, et al. Anion inhibition studies of the beta-carbonic anhydrase from the pathogenic bacterium vibrio cholerae. Bioorg Med Chem Lett. 2016;26:1406–1410.
   PubMed Web of Science ®Google Scholar
• Kohler S, Ouahrani-Bettache S, Winum JY. Brucella suis carbonic anhydrases and their inhibitors: towards alternative antibiotics? J Enzyme Inhib Med Chem. 2017;32:683–687.
   PubMed Web of Science ®Google Scholar
• Singh S, Supuran CT. 3d-qsar comfa studies on sulfonamide inhibitors of the rv3588c beta-carbonic anhydrase from mycobacterium tuberculosis and design of not yet synthesized new molecules. J Enzyme Inhib Med Chem. 2014;29:449–455.
   PubMed Web of Science ®Google Scholar
• Ceruso M, Vullo D, Scozzafava A, et al. Sulfonamides incorporating fluorine and 1,3,5-triazine moieties are effective inhibitors of three beta-class carbonic anhydrases from mycobacterium tuberculosis. J Enzyme Inhib Med Chem. 2014;29:686–689.
   PubMed Web of Science ®Google Scholar
• Carta F, Maresca A, Covarrubias AS, et al. Carbonic anhydrase inhibitors. Characterization and inhibition studies of the most active beta-carbonic anhydrase from mycobacterium tuberculosis, rv3588c. Bioorg Med Chem Lett. 2009;19:6649–6654.
   PubMed Web of Science ®Google Scholar
• Supuran CT, Capasso C. An overview of the bacterial carbonic anhydrases. Metabolites. 2017;7.
   Web of Science ®Google Scholar
• Pinard MA, Lotlikar SR, Boone CD, et al. Structure and inhibition studies of a type ii beta-carbonic anhydrase psca3 from pseudomonas aeruginosa. Bioorg Med Chem. 2015;23:4831–4838.
   PubMed Web of Science ®Google Scholar
• Ferraroni M, Del Prete S, Vullo D, et al. Crystal structure and kinetic studies of a tetrameric type ii beta-carbonic anhydrase from the pathogenic bacterium vibrio cholerae. Acta Crystallogr D Biol Crystallogr. 2015;71:2449–2456.
   PubMedGoogle Scholar
• De Simone G, Monti SM, Alterio V, et al. Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, sazca from the thermophilic bacterium Sulfurihydrogenibium azorense. Bioorg Med Chem Lett. 2015;25:2002–2006.
   PubMed Web of Science ®Google Scholar
• Zolnowska B, Slawinski J, Pogorzelska A, et al. Carbonic anhydrase inhibitors. Synthesis, and molecular structure of novel series n-substituted n’-(2-arylmethylthio-4-chloro-5-methylbenzenesulfonyl)guanidines and their inhibition of human cytosolic isozymes i and ii and the transmembrane tumor-associated isozymes ix and xii. European. J Med Chem. 2014;71:135–147.
   Web of Science ®Google Scholar
• De Luca L, Ferro S, Damiano FM, et al. Structure-based screening for the discovery of new carbonic anhydrase vii inhibitors. Eur J Med Chem. 2014;71:105–111.
   PubMed Web of Science ®Google Scholar
• Di Fiore A, Capasso C, De Luca V, et al. X-ray structure of the first `extremo-alpha-carbonic anhydrase’, a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense yo3aop1. Acta Crystallogr D Biol Crystallogr. 2013;69:1150–1159.
   PubMed Web of Science ®Google Scholar
• Supuran CT. Structure-based drug discovery of carbonic anhydrase inhibitors. J Enzyme Inhib Med Chem. 2012;27:759–772.
   PubMed Web of Science ®Google Scholar
• Supuran CT. Carbonic anhydrases–an overview. Curr Pharm Des. 2008;14:603–614.
   PubMed Web of Science ®Google Scholar
• Kisker C, Schindelin H, Alber BE, et al. A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila. EMBO J. 1996;15:2323–2330.
   PubMed Web of Science ®Google Scholar
• Supuran CT. How many carbonic anhydrase inhibition mechanisms exist? J Enzyme Inhib Med Chem. 2016;31:345–360.
   PubMed Web of Science ®Google Scholar
• Supuran CT. Advances in structure-based drug discovery of carbonic anhydrase inhibitors. Expert Opin Drug Discov. 2017;12:61–88.
   PubMed Web of Science ®Google Scholar
• Supuran CT. Structure and function of carbonic anhydrases. Biochem J. 2016;473:2023–2032.
   PubMed Web of Science ®Google Scholar
• Supuran CT. Carbonic anhydrase inhibition and the management of neuropathic pain. Expert Rev Neurother. 2016;16:961–968.
   PubMed Web of Science ®Google Scholar
• Supuran CT. Drug interaction considerations in the therapeutic use of carbonic anhydrase inhibitors. Expert Opin Drug Metab Toxicol. 2016;12:423–431.
   PubMed Web of Science ®Google Scholar
• Otten H. Domagk and the development of the sulphonamides. J Antimicrob Chemother. 1986;17:689–696.
   PubMed Web of Science ®Google Scholar
• Achari A, Somers DO, Champness JN, et al. Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase. Nat Struct Biol. 1997;4:490–497.
   PubMedGoogle Scholar
• Vullo D, Del Prete S, Fisher GM, et al. Sulfonamide inhibition studies of the eta-class carbonic anhydrase from the malaria pathogen plasmodium falciparum. Bioorg Med Chem. 2015;23:526–531.
   PubMed Web of Science ®Google Scholar
• Vullo D, De Luca V, Del Prete S, et al. Sulfonamide inhibition studies of the gamma-carbonic anhydrase from the antarctic bacterium pseudoalteromonas haloplanktis. Bioorg Med Chem Lett. 2015;25:3550–3555.
   PubMed Web of Science ®Google Scholar
• Vullo D, De Luca V, Del Prete S, et al. Sulfonamide inhibition studies of the gamma-carbonic anhydrase from the antarctic cyanobacterium nostoc commune. Bioorg Med Chem. 2015;23:1728–1734.
   PubMed Web of Science ®Google Scholar
• Dedeoglu N, DeLuca V, Isik S, et al. Sulfonamide inhibition study of the beta-class carbonic anhydrase from the caries producing pathogen streptococcus mutans. Bioorg Med Chem Lett. 2015;25:2291–2297.
   PubMed Web of Science ®Google Scholar
• Alafeefy AM, Ceruso M, Al-Tamimi AM, et al. Inhibition studies of quinazoline-sulfonamide derivatives against the gamma-ca (pgica) from the pathogenic bacterium, porphyromonas gingivalis. J Enzyme Inhib Med Chem. 2015;30:592–596.
   PubMed Web of Science ®Google Scholar
• Alafeefy AM, Abdel-Aziz HA, Vullo D, et al. Inhibition of human carbonic anhydrase isozymes i, ii, ix and xii with a new series of sulfonamides incorporating aroylhydrazone-, [1,2,4]triazolo[3,4-b][1,3,4]thiadiazinyl- or 2-(cyanophenylmethylene)-1,3,4-thiadiazol-3(2h)-yl moieties. J Enzyme Inhib Med Chem. 2015;30:52–56.
   PubMed Web of Science ®Google Scholar
• Supuran CT. Legionella pneumophila carbonic anhydrases: underexplored antibacterial drug targets. Pathogens. 2016;5.
   PubMed Web of Science ®Google Scholar
• Nishimori I, Vullo D, Minakuchi T, et al. Sulfonamide inhibition studies of two beta-carbonic anhydrases from the bacterial pathogen legionella pneumophila. Bioorg Med Chem. 2014;22:2939–2946.
   PubMed Web of Science ®Google Scholar
• Vullo D, Sai Kumar RS, Scozzafava A, et al. Anion inhibition studies of a beta-carbonic anhydrase from clostridium perfringens. Bioorg Med Chem Lett. 2013;23:6706–6710.
   PubMed Web of Science ®Google Scholar
• Nishimori I, Minakuchi T, Maresca A, et al. The beta-carbonic anhydrases from mycobacterium tuberculosis as drug targets. Curr Pharm Des. 2010;16:3300–3309.
   PubMed Web of Science ®Google Scholar
• Supuran CT. Acetazolamide for the treatment of idiopathic intracranial hypertension. Expert Rev Neurother. 2015;15:851–856.
   PubMed Web of Science ®Google Scholar
• Del Prete S, Vullo D, Osman SM, et al. Sulfonamide inhibition profiles of the beta-carbonic anhydrase from the pathogenic bacterium francisella tularensis responsible of the febrile illness tularemia. Bioorg Med Chem. 2017;25:3555–3561.
   PubMed Web of Science ®Google Scholar
• Vullo D, Del Prete S, Di Fonzo P, et al. Comparison of the sulfonamide inhibition profiles of the beta- and gamma-carbonic anhydrases from the pathogenic bacterium burkholderia pseudomallei. Molecules. 2017;22.
   Web of Science ®Google Scholar
• Cau Y, Mori M, Supuran CT, et al. Mycobacterial carbonic anhydrase inhibition with phenolic acids and esters: kinetic and computational investigations. Org Biomol Chem. 2016;14:8322–8330.
   PubMed Web of Science ®Google Scholar
• Modak JK, Liu YC, Supuran CT, et al. Structure-activity relationship for sulfonamide inhibition of helicobacter pylori alpha-carbonic anhydrase. J Med Chem. 2016;59:11098–11109.
   PubMed Web of Science ®Google Scholar
• Supuran CT. Bortezomib inhibits bacterial and fungal beta-carbonic anhydrases. Bioorg Med Chem. 2016;24:4406–4409.
   PubMed Web of Science ®Google Scholar
• Vullo D, Kumar RSS, Scozzafava A, et al. Sulphonamide inhibition studies of the beta-carbonic anhydrase from the bacterial pathogen clostridium perfringens. J Enzyme Inhib Med Chem. 2018;33:31–36.
   PubMed Web of Science ®Google Scholar
• Shahidzadeh R, Opekun A, Shiotani A, et al. Effect of the carbonic anhydrase inhibitor, acetazolamide, on helicobacter pylori infection in vivo: A pilot study. Helicobacter. 2005;10:136–138.
   PubMed Web of Science ®Google Scholar
• Capasso C, Supuran C. Inhibition of bacterial carbonic anhydrases as a novel approach to escape drug resistance. Curr Top Med Chem. 2017;17:1237–1248.
   PubMed Web of Science ®Google Scholar
• Licsandru E, Tanc M, Kocsis I, et al. A class of carbonic anhydrase i - selective activators. J Enzyme Inhib Med Chem. 2017;32:37–46.
   PubMed Web of Science ®Google Scholar
• Supuran CT. Carbonic anhydrase inhibitors and activators for novel therapeutic applications. Future Med Chem. 2011;3:1165–1180.
   PubMed Web of Science ®Google Scholar
• Supuran CT. Carbonic anhydrases: from biomedical applications of the inhibitors and activators to biotechnological use for co(2) capture. J Enzyme Inhib Med Chem. 2013;28:229–230.
   PubMed Web of Science ®Google Scholar
• Vullo D, Del Prete S, Capasso C, et al. Carbonic anhydrase activators: activation of the beta-carbonic anhydrase from malassezia globosa with amines and amino acids. Bioorg Med Chem Lett. 2016;26:1381–1385.
   PubMed Web of Science ®Google Scholar
• Vullo D, Del Prete S, Osman SM, et al. Burkholderia pseudomallei gamma-carbonic anhydrase is strongly activated by amino acids and amines. Bioorg Med Chem Lett. 2017;27:77–80.
   PubMed Web of Science ®Google Scholar
• Akdemir A, Vullo D, De Luca V, et al. The extremo-alpha-carbonic anhydrase (ca) from Sulfurihydrogenibium azorense, the fastest ca known, is highly activated by amino acids and amines. Bioorg Med Chem Lett. 2013;23:1087–1090.
   PubMed Web of Science ®Google Scholar
• El Harrad L, Bourais I, Mohammadi H, et al. Recent advances in electrochemical biosensors based on enzyme inhibition for clinical and pharmaceutical applications. Sensors (Basel). 2018;18:164–188.
   Web of Science ®Google Scholar
• Hicks N, Vik U, Taylor P, et al. Using prokaryotes for carbon capture storage. Trends Biotechnol. 2017;35:22–32.
   PubMed Web of Science ®Google Scholar
• Alafeefy AM, Abdel-Aziz HA, Vullo D, et al. Inhibition of carbonic anhydrases from the extremophilic bacteria sulfurihydrogenibium yellostonense (sspca) and S. azorense (sazca) with a new series of sulfonamides incorporating aroylhydrazone-, [1,2,4]triazolo[3,4-b][1,3,4]thiadiazinyl- or 2-(cyanophenylmethylene)-1,3,4-thiadiazol-3(2h)-yl moieties. Bioorg Med Chem. 2014;22:141–147.
   PubMed Web of Science ®Google Scholar
• Vullo D, De Luca V, Scozzafava A, et al. The extremo-alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium azorense is highly inhibited by sulfonamides. Bioorg Med Chem. 2013;21:4521–4525.
   PubMed Web of Science ®Google Scholar
• Vullo D, Luca VD, Scozzafava A, et al. The alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense yo3aop1 is highly susceptible to inhibition by sulfonamides. Bioorg Med Chem. 2013;21:1534–1538.
   PubMed Web of Science ®Google Scholar
• De Luca V, Vullo D, Scozzafava A, et al. Anion inhibition studies of an alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense yo3aop1. Bioorg Med Chem Lett. 2012;22:5630–5634.
   PubMed Web of Science ®Google Scholar
• Vullo D, De Luca V, Scozzafava A, et al. Anion inhibition studies of the fastest carbonic anhydrase (ca) known, the extremo-ca from the bacterium Sulfurihydrogenibium azorense. Bioorg Med Chem Lett. 2012;22:7142–7145.
   PubMed Web of Science ®Google Scholar
• Vullo D, De Luca V, Scozzafava A, et al. The first activation study of a bacterial carbonic anhydrase (ca) The thermostable alpha-ca from Sulfurihydrogenibium yellowstonense yo3aop1 is highly activated by amino acids and amines. Bioorg Med Chem Lett. 2012;22:6324–6327.
   PubMed Web of Science ®Google Scholar
• Arazawa DT, Oh H-I, Ye S-H, et al. Immobilized carbonic anhydrase on hollow fiber membranes accelerates co(2) removal from blood. J Memb Sci. 2012;404:25–31.
   PubMedGoogle Scholar
• Supuran CT. CA IX stratification based on cancer treatment: A patent evaluation of us2016/0002350. Expert Opin Ther Pat. 2016;26:1105–1109.
   PubMed Web of Science ®Google Scholar
• Lomelino C, McKenna R. Carbonic anhydrase inhibitors: A review on the progress of patent literature (2011–2016). Expert Opin Ther Pat. 2016;26:947–956.
   PubMed Web of Science ®Google Scholar
• Monti SM, Supuran CT, De Simone G. Anticancer carbonic anhydrase inhibitors: A patent review (2008–2013). Expert Opin Ther Pat. 2013;23:737–749.
   PubMed Web of Science ®Google Scholar
• Masini E, Carta F, Scozzafava A, et al. Antiglaucoma carbonic anhydrase inhibitors: A patent review. Expert Opin Ther Pat. 2013;23:705–716.
   PubMed Web of Science ®Google Scholar
• Scozzafava A, Supuran CT, Carta F. Antiobesity carbonic anhydrase inhibitors: A literature and patent review. Expert Opin Ther Pat. 2013;23:725–735.
   PubMed Web of Science ®Google Scholar
• Aggarwal M, Kondeti B, McKenna R. Anticonvulsant/antiepileptic carbonic anhydrase inhibitors: A patent review. Expert Opin Ther Pat. 2013;23:717–724.
   PubMed Web of Science ®Google Scholar
• Carta F, Supuran CT. Diuretics with carbonic anhydrase inhibitory action: A patent and literature review (2005–2013). Expert Opin Ther Pat. 2013;23:681–691.
   PubMed Web of Science ®Google Scholar
• Winum JY, Capasso C. Novel antibody to a carbonic anhydrase: patent evaluation of WO2011138279a1. Expert Opin Ther Pat. 2013;23:757–760.
   PubMed Web of Science ®Google Scholar
• Aggarwal M, McKenna R. Update on carbonic anhydrase inhibitors: A patent review (2008–2011). Expert Opin Ther Pat. 2012;22:903–915.
   PubMed Web of Science ®Google Scholar
• Carta F, Scozzafava A, Supuran CT. Sulfonamides: A patent review (2008–2012). Expert Opin Ther Pat. 2012;22:747–758.
   PubMed Web of Science ®Google Scholar
• Carta F, Supuran CT, Scozzafava A. Novel therapies for glaucoma: A patent review 2007–2011. Expert Opin Ther Pat. 2012;22:79–88.
   PubMed Web of Science ®Google Scholar
• Poulsen SA. Carbonic anhydrase inhibition as a cancer therapy: A review of patent literature, 2007–2009. Expert Opin Ther Pat. 2010;20:795–806.
   PubMed Web of Science ®Google Scholar
• Park AA, Swanson E, Zhao H, et al. Methods and systems for capturing and storing carbon dioxide. US2017333840; 2017
   Google Scholar
• Voyer N, Daigle R, Madore E, et al. CO2 capture methods using Thermovibrio ammonificans carbonic anhydrase. CN106999842. 2017.
   Google Scholar
• Qian C, Yi H, Wan K. Method for accelerating microbial mineralization of alkaline solid waste. CN106966673. 2017.
   Google Scholar
• Sun C, Zhu Y, Ma N. Calcium carbonate producing actinomycetes and application thereof. CN106635882. 2017.
   Google Scholar
• Nam YS, Jeong KJ, et al. Transformant with increased carbon dioxide hydration using carbonic anhydrase from Neisseria gonorrhoeae. KR20170052496. 2017.
   Google Scholar
• Nam YS, Jeong KJ, Song SY, et al. Transformant having increased carbonic anhydration activity, using Neisseria gonorrhoeae- derived carbonic anhydrase. WO2017078422. 2017.
   Google Scholar
• Ge J, Hua L, Poulose AJ, et al. Thermostable carbonic anhydrase and methods of use thereof. US2017081653. 2017.
   Google Scholar
• Voyer N, Daigle R, Madore É, et al. Variants of Thermovibrio ammonificans carbonic anhydrase and CO2 capture methods using Thermovibrio ammonificans carbonic anhydrase variants. WO2017035667. 2017.
   Google Scholar
• Cha HJ, Park TY, Park HJ, et al. The engineered thermostable carbonic anhydrase having a de novo disulfide bond and use thereof. KR20160098652. 2016.
   Google Scholar
• Cai X, Zhuang Q, Wu Z, et al. Carbon dioxide determination kit and preparation method thereof. CN105928937. 2016.
   Google Scholar
• Cha HJ, Jo Byung H, Seo JH, et al. Carbonic anhydrase with stability at high temperature and capturing agent for carbon dioxide comprising the same. US2016222371. 2016.
   Google Scholar
• Pack SP. Novel carbonic anhydrase from Caminibacter mediatlanticus and use thereof. KR20150133497. 2015.
   Google Scholar
• Cha HJ, Im Seul K, Jo BH. Composition for CO2 capture comprising marine bacterium-derived recombinant biocatalyst, method for preparing the same, and method of CO2 capture using the same. KR101591786. 2016.
   Google Scholar
• DAigle R, Madore É, Fradette S, et al. Techniques for CO2 capture using Sulfurihydrogenibium sp. carbonic anhydrase. US2015283502. 2015.
   Google Scholar
• Martin B, Paria S Heat-stable carbonic anhydrase and use thereof. JP6068523. 2017.
   Google Scholar
• Borchert MS Heat-stable Persephonella carbonic anhydrases and their use. US2015175997. 2015.
   Google Scholar
• Medium for culture of Actinobacillus succinogen for production of succinic acid, using carbonic anhydrase. KR20150036951. 2015.
   Google Scholar
• Pack SP Novel carbonic anhydrase from Persephonella marina EX-H1 and use thereof. KR20140139787. 2014.
   Google Scholar
• Ye J, Li D, Shi Y. Method for removing calcium carbonate scales by using microbial extracellular carbonic anhydrase. CN104071890. 2015.
   Google Scholar
• MCFarland S, Brown S, Luttringer S, et al. Recombinant microorganisms for production C4-dicarboxylic acids. CN10391764. 2014.
   Google Scholar
• Alvizo O, Benoit M, Novick SJ, et al. Highly stable beta-class carbonic anhydrases useful in carbon capture systems. US8512989. 2013.
   Google Scholar