{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T01:52:44Z","timestamp":1772761964677,"version":"3.50.1"},"reference-count":77,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2021,1,8]],"date-time":"2021-01-08T00:00:00Z","timestamp":1610064000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Carbonic anhydrases (CAs) are essential metalloenzymes in nature, catalyzing the carbon dioxide reversible hydration into bicarbonate and proton. In humans, breathing and many other critical physiological processes depend on this enzymatic activity. The CA superfamily function and inhibition in pathogenic bacteria has recently been the object of significant advances, being demonstrated to affect microbial survival\/virulence. Targeting bacterial CAs may thus be a valid alternative to expand the pharmacological arsenal against the emergence of widespread antibiotic resistance. Here, we report an extensive study on the inhibition profile of the recently discovered \u03b9-CA class present in some bacteria, including Burkholderia territorii, namely BteCA\u03b9, using substituted benzene-sulfonamides and clinically licensed sulfonamide-, sulfamate- and sulfamide-type drugs. The BteCA\u03b9 inhibition profile showed: (i) several benzene-sulfonamides with an inhibition constant lower than 100 nM; (ii) a different behavior with respect to other \u03b1, \u03b2 and \u03b3-CAs; (iii) clinically used drugs having a micromolar affinity. This prototype study contributes to the initial recognition of compounds which efficiently and selectively inhibit a bacterial member of the \u03b9-CA class, for which such a selective inhibition with respect to other protein isoforms present in the host is highly desired and may contribute to the development of novel antimicrobials.<\/jats:p>","DOI":"10.3390\/ijms22020571","type":"journal-article","created":{"date-parts":[[2021,1,10]],"date-time":"2021-01-10T19:55:56Z","timestamp":1610308556000},"page":"571","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":29,"title":["Effect of Sulfonamides and Their Structurally Related Derivatives on the Activity of \u03b9-Carbonic Anhydrase from Burkholderia territorii"],"prefix":"10.3390","volume":"22","author":[{"given":"Viviana","family":"De Luca","sequence":"first","affiliation":[{"name":"Institute of Biosciences and Bioresources, CNR, via Pietro Castellino 111, 80131 Napoli, Italy"},{"name":"Proteomics &amp; Mass Spectrometry Laboratory, ISPAAM, CNR, via Argine 1085, 80147 Napoli, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrea","family":"Petreni","sequence":"additional","affiliation":[{"name":"Section of Pharmaceutical and Nutraceutical Sciences, Department of Neurofarba, University of Florence, via U. Schiff 6, 50019 Florence, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3342-702X","authenticated-orcid":false,"given":"Alessio","family":"Nocentini","sequence":"additional","affiliation":[{"name":"Section of Pharmaceutical and Nutraceutical Sciences, Department of Neurofarba, University of Florence, via U. Schiff 6, 50019 Florence, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrea","family":"Scaloni","sequence":"additional","affiliation":[{"name":"Proteomics &amp; Mass Spectrometry Laboratory, ISPAAM, CNR, via Argine 1085, 80147 Napoli, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4262-0323","authenticated-orcid":false,"given":"Claudiu T.","family":"Supuran","sequence":"additional","affiliation":[{"name":"Section of Pharmaceutical and Nutraceutical Sciences, Department of Neurofarba, University of Florence, via U. Schiff 6, 50019 Florence, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3314-2411","authenticated-orcid":false,"given":"Clemente","family":"Capasso","sequence":"additional","affiliation":[{"name":"Institute of Biosciences and Bioresources, CNR, via Pietro Castellino 111, 80131 Napoli, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,1,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1904","DOI":"10.1002\/cmdc.201600180","article-title":"Discovery of New Potential Anti-Infective Compounds Based on Carbonic Anhydrase Inhibitors by Rational Target-Focused Repurposing Approaches","volume":"11","author":"Annunziato","year":"2016","journal-title":"ChemMedChem"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"689","DOI":"10.3109\/14756366.2015.1059333","article-title":"A magnificent enzyme superfamily: Carbonic anhydrases, their purification and characterization","volume":"31","author":"Guler","year":"2016","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/j.bmc.2016.01.037","article-title":"Sulfonamide inhibition studies of the beta-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae","volume":"24","author":"Vullo","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1080\/14756366.2016.1217856","article-title":"Cloning, expression and purification of the complete domain of the eta-carbonic anhydrase from Plasmodium falciparum","volume":"31","author":"Supuran","year":"2016","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"2359","DOI":"10.2174\/1568026616666160413135522","article-title":"An Overview of the Carbonic Anhydrases from Two Pathogens of the Oral Cavity: Streptococcus mutans and Porphyromonas gingivalis","volume":"16","author":"Capasso","year":"2016","journal-title":"Curr. Top Med. Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"325","DOI":"10.3109\/14756366.2014.910202","article-title":"An overview of the alpha-, beta- and gamma-carbonic anhydrases from Bacteria: Can bacterial carbonic anhydrases shed new light on evolution of bacteria?","volume":"30","author":"Capasso","year":"2015","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Supuran, C.T., and Capasso, C. (2017). An Overview of the Bacterial Carbonic Anhydrases. Metabolites, 7.","DOI":"10.3390\/metabo7040056"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2023","DOI":"10.1042\/BCJ20160115","article-title":"Structure and function of carbonic anhydrases","volume":"473","author":"Supuran","year":"2016","journal-title":"BioChem. J."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1007\/978-94-007-7359-2_15","article-title":"Carbonic anhydrase inhibitors drug design","volume":"75","author":"McKenna","year":"2014","journal-title":"Subcell BioChem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1038\/nrd3554","article-title":"Interfering with pH regulation in tumours as a therapeutic strategy","volume":"10","author":"Neri","year":"2011","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1038\/nrd2467","article-title":"Carbonic anhydrases: Novel therapeutic applications for inhibitors and activators","volume":"7","author":"Supuran","year":"2008","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"603","DOI":"10.2174\/138161208783877884","article-title":"Carbonic anhydrases\u2014An overview","volume":"14","author":"Supuran","year":"2008","journal-title":"Curr. Pharm. Des."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1016\/j.bbapap.2009.10.021","article-title":"Evaluating the role of carbonic anhydrases in the transport of HCO3\u2212-related species","volume":"1804","author":"Boron","year":"2010","journal-title":"Biochim Biophys Acta"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1080\/13543776.2018.1497161","article-title":"Biomedical applications of prokaryotic carbonic anhydrases","volume":"28","author":"Supuran","year":"2018","journal-title":"Expert Opin Ther. Patents"},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Supuran, C.T., and Capasso, C. (2017). Carbonic Anhydrase from Porphyromonas Gingivalis as a Drug Target. Pathogens, 6.","DOI":"10.3390\/pathogens6030030"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"2130","DOI":"10.2174\/0929867321666141012174921","article-title":"An Overview of the Selectivity and Efficiency of the Bacterial Carbonic Anhydrase Inhibitors","volume":"22","author":"Capasso","year":"2015","journal-title":"Curr. Med. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1080\/14756366.2018.1559840","article-title":"Phaeodactylum tricornutum as a model organism for testing the membrane penetrability of sulphonamide carbonic anhydrase inhibitors","volume":"34","author":"Rogato","year":"2019","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1080\/14756366.2019.1571273","article-title":"Inhibition of alpha-, beta-, gamma-, delta-, zeta- and eta-class carbonic anhydrases from bacteria, fungi, algae, diatoms and protozoans with famotidine","volume":"34","author":"Angeli","year":"2019","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1080\/14756366.2018.1490733","article-title":"Inhibition of alpha-, beta-, gamma-, and delta-carbonic anhydrases from bacteria and diatoms with N\u2032-aryl-N-hydroxy-ureas","volume":"33","author":"Berrino","year":"2018","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.bioorg.2018.06.002","article-title":"The first activation studies of the eta-carbonic anhydrase from the malaria parasite Plasmodium falciparum with amines and amino acids","volume":"80","author":"Angeli","year":"2018","journal-title":"Bioorg. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1038\/nrd2201","article-title":"Drugs for bad bugs: Confronting the challenges of antibacterial discovery","volume":"6","author":"Payne","year":"2007","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1080\/14756366.2016.1201479","article-title":"New light on bacterial carbonic anhydrases phylogeny based on the analysis of signal peptide sequences","volume":"31","author":"Supuran","year":"2016","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"2094","DOI":"10.1038\/s41396-019-0426-8","article-title":"A new widespread subclass of carbonic anhydrase in marine phytoplankton","volume":"13","author":"Jensen","year":"2019","journal-title":"ISME J."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1016\/j.bmcl.2015.02.068","article-title":"Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense","volume":"25","author":"Monti","year":"2015","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1107\/S0907444913007208","article-title":"X-ray structure of the first \u2018extremo-alpha-carbonic anhydrase\u2019, a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1","volume":"69","author":"Capasso","year":"2013","journal-title":"Acta Cryst. D Biol. Cryst."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1016\/j.bmc.2016.01.019","article-title":"Kinetic and X-ray crystallographic investigations on carbonic anhydrase isoforms I, II, IX and XII of a thioureido analog of SLC-0111","volume":"24","author":"Lomelino","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2449","DOI":"10.1107\/S1399004715018635","article-title":"Crystal structure and kinetic studies of a tetrameric type II beta-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae","volume":"71","author":"Ferraroni","year":"2015","journal-title":"Acta Cryst. D Biol. Cryst."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2265","DOI":"10.1099\/ijs.0.000251","article-title":"Burkholderia stagnalis sp. nov. and Burkholderia territorii sp. nov., two novel Burkholderia cepacia complex species from environmental and human sources","volume":"65","author":"Mayo","year":"2015","journal-title":"Int. J. Syst. Evol. Microbiol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1060","DOI":"10.1080\/14756366.2020.1755852","article-title":"Bacterial iota-carbonic anhydrase: A new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii","volume":"35","author":"Nocentini","year":"2020","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"379","DOI":"10.3109\/14756366.2013.787422","article-title":"Sulfa and trimethoprim-like drugs\u2014Antimetabolites acting as carbonic anhydrase, dihydropteroate synthase and dihydrofolate reductase inhibitors","volume":"29","author":"Capasso","year":"2014","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"759","DOI":"10.3109\/14756366.2012.672983","article-title":"Structure-based drug discovery of carbonic anhydrase inhibitors","volume":"27","author":"Supuran","year":"2012","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1093\/jac\/17.6.689","article-title":"Domagk and the development of the sulphonamides","volume":"17","author":"Otten","year":"1986","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1038\/nsb0697-490","article-title":"Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase","volume":"4","author":"Achari","year":"1997","journal-title":"Nat. Struct. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1642","DOI":"10.3390\/molecules22101642","article-title":"Special Issue: Sulfonamides","volume":"22","author":"Supuran","year":"2017","journal-title":"Molecules"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1080\/14737175.2016.1193009","article-title":"Carbonic anhydrase inhibition and the management of neuropathic pain","volume":"16","author":"Supuran","year":"2016","journal-title":"Expert Rev. Neurother."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1517\/17425255.2016.1154534","article-title":"Drug interaction considerations in the therapeutic use of carbonic anhydrase inhibitors","volume":"12","author":"Supuran","year":"2016","journal-title":"Expert Opin. Drug Metab. Toxicol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1080\/17460441.2017.1253677","article-title":"Advances in structure-based drug discovery of carbonic anhydrase inhibitors","volume":"12","author":"Supuran","year":"2017","journal-title":"Expert Opin. Drug Discov."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1016\/j.bmc.2014.12.009","article-title":"Sulfonamide inhibition studies of the eta-class carbonic anhydrase from the malaria pathogen Plasmodium falciparum","volume":"23","author":"Vullo","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3550","DOI":"10.1016\/j.bmcl.2015.06.079","article-title":"Sulfonamide inhibition studies of the gamma-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis","volume":"25","author":"Vullo","year":"2015","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1728","DOI":"10.1016\/j.bmc.2015.02.045","article-title":"Sulfonamide inhibition studies of the gamma-carbonic anhydrase from the Antarctic cyanobacterium Nostoc commune","volume":"23","author":"Vullo","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2291","DOI":"10.1016\/j.bmcl.2015.04.037","article-title":"Sulfonamide inhibition study of the beta-class carbonic anhydrase from the caries producing pathogen Streptococcus mutans","volume":"25","author":"Dedeoglu","year":"2015","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"592","DOI":"10.3109\/14756366.2014.957202","article-title":"Inhibition studies of quinazoline-sulfonamide derivatives against the gamma-CA (PgiCA) from the pathogenic bacterium, Porphyromonas gingivalis","volume":"30","author":"Alafeefy","year":"2015","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"52","DOI":"10.3109\/14756366.2013.877897","article-title":"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","volume":"30","author":"Alafeefy","year":"2015","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1080\/14756366.2016.1187143","article-title":"A substituted sulfonamide and its Co (II), Cu (II), and Zn (II) complexes as potential antifungal agents","volume":"31","author":"Diaz","year":"2016","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1941","DOI":"10.1016\/j.bmcl.2016.01.072","article-title":"Comparison of the sulfonamide inhibition profiles of the alpha-, beta- and gamma-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae","volume":"26","author":"Vullo","year":"2016","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"4184","DOI":"10.1016\/j.bmcl.2016.07.060","article-title":"Cloning, expression, purification and sulfonamide inhibition profile of the complete domain of the eta-carbonic anhydrase from Plasmodium falciparum","volume":"26","author":"Vullo","year":"2016","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"3043","DOI":"10.1016\/j.bmc.2016.05.016","article-title":"Synthesis of 4-(thiazol-2-ylamino)-benzenesulfonamides with carbonic anhydrase I, II and IX inhibitory activity and cytotoxic effects against breast cancer cell lines","volume":"24","author":"Gawad","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Supuran, C.T. (2016). Legionella pneumophila Carbonic Anhydrases: Underexplored Antibacterial Drug Targets. Pathogens, 5.","DOI":"10.3390\/pathogens5020044"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2939","DOI":"10.1016\/j.bmc.2014.04.006","article-title":"Sulfonamide inhibition studies of two beta-carbonic anhydrases from the bacterial pathogen Legionella pneumophila","volume":"22","author":"Nishimori","year":"2014","journal-title":"Bioorg. Med. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"6706","DOI":"10.1016\/j.bmcl.2013.10.037","article-title":"Anion inhibition studies of a beta-carbonic anhydrase from Clostridium perfringens","volume":"23","author":"Vullo","year":"2013","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"3300","DOI":"10.2174\/138161210793429814","article-title":"The beta-carbonic anhydrases from Mycobacterium tuberculosis as drug targets","volume":"16","author":"Nishimori","year":"2010","journal-title":"Curr. Pharm. Des."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"6649","DOI":"10.1016\/j.bmcl.2009.10.009","article-title":"Carbonic anhydrase inhibitors. Characterization and inhibition studies of the most active beta-carbonic anhydrase from Mycobacterium tuberculosis, Rv3588c","volume":"19","author":"Carta","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_53","unstructured":"Nguyen, K., and Ahlawat, R. (2020). Famotidine, StatPearls."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"423","DOI":"10.3389\/fonc.2018.00423","article-title":"Updates in the Clinical Development of Epacadostat and Other Indoleamine 2,3-Dioxygenase 1 Inhibitors (IDO1) for Human Cancers","volume":"8","author":"Komiya","year":"2018","journal-title":"Front. Oncol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1080\/14756366.2019.1663416","article-title":"Anti-Helicobacter pylori activity of ethoxzolamide","volume":"34","author":"Modak","year":"2019","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1080\/14756366.2018.1539716","article-title":"Identification and characterization of the alpha-CA in the outer membrane vesicles produced by Helicobacter pylori","volume":"34","author":"Ronci","year":"2019","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2003","DOI":"10.1556\/oh.2010.28982","article-title":"Helicobacter pylori\u20142010","volume":"151","author":"Buzas","year":"2010","journal-title":"Orv. Hetil."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"4111","DOI":"10.1128\/IAI.00409-09","article-title":"Bicarbonate Induces Vibrio cholerae virulence gene expression by enhancing ToxT activity","volume":"77","author":"Abuaita","year":"2009","journal-title":"Infect. Immun."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1080\/14756366.2017.1295451","article-title":"Brucella suis carbonic anhydrases and their inhibitors: Towards alternative antibiotics?","volume":"32","author":"Kohler","year":"2017","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"449","DOI":"10.3109\/14756366.2013.800059","article-title":"3D-QSAR CoMFA studies on sulfonamide inhibitors of the Rv3588c beta-carbonic anhydrase from Mycobacterium tuberculosis and design of not yet synthesized new molecules","volume":"29","author":"Singh","year":"2014","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"686","DOI":"10.3109\/14756366.2013.842233","article-title":"Sulfonamides incorporating fluorine and 1,3,5-triazine moieties are effective inhibitors of three beta-class carbonic anhydrases from Mycobacterium tuberculosis","volume":"29","author":"Ceruso","year":"2014","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1649","DOI":"10.1128\/IAI.74.3.1649-1660.2006","article-title":"Salmonella enterica highly expressed genes are disease specific","volume":"74","author":"Rollenhagen","year":"2006","journal-title":"Infect. Immun."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"102080","DOI":"10.1016\/j.ceca.2019.102080","article-title":"Pseudomonas aeruginosa \u03b2-carbonic anhydrase, psCA1, is required for calcium deposition and contributes to virulence","volume":"84","author":"Lotlikar","year":"2019","journal-title":"Cell Calcium."},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Aspatwar, A., Kairys, V., Rala, S., Parikka, M., Bozdag, M., Carta, F., Supuran, C.T., and Parkkila, S. (2019). Mycobacterium tuberculosis beta-Carbonic Anhydrases: Novel Targets for Developing Antituberculosis Drugs. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20205153"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"9540","DOI":"10.1021\/acs.jmedchem.0c00734","article-title":"Optimization of Acetazolamide-Based Scaffold as Potent Inhibitors of Vancomycin-Resistant Enterococcus","volume":"63","author":"Kaur","year":"2020","journal-title":"J. Med. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. BioChem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1002\/mbo3.1027","article-title":"A protocol for recombinant protein quantification by densitometry","volume":"9","author":"Villela","year":"2020","journal-title":"Microbiologyopen"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"892","DOI":"10.3109\/14756366.2012.703185","article-title":"Biochemical properties of a novel and highly thermostable bacterial alpha-carbonic anhydrase from Sulfurihydrogenibium yellowstonense YO3AOP1","volume":"27","author":"Capasso","year":"2012","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"277","DOI":"10.3109\/14756366.2014.917085","article-title":"Protonography, a new technique for the analysis of carbonic anhydrase activity","volume":"30","author":"Supuran","year":"2015","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"3747","DOI":"10.1016\/j.bmc.2015.03.080","article-title":"Protonography, a powerful tool for analyzing the activity and the oligomeric state of the gamma-carbonic anhydrase identified in the genome of Porphyromonas gingivalis","volume":"23","author":"Iandolo","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"920","DOI":"10.3109\/14756366.2014.990963","article-title":"Protonography, a technique applicable for the analysis of eta-carbonic anhydrase activity","volume":"30","author":"Supuran","year":"2015","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.bioorg.2017.12.009","article-title":"Protonography and anion inhibition profile of the alpha-carbonic anhydrase (CruCA4) identified in the Mediterranean red coral Corallium rubrum","volume":"76","author":"Vullo","year":"2018","journal-title":"Bioorg. Chem."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2561","DOI":"10.1016\/S0021-9258(18)62326-9","article-title":"The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C","volume":"246","author":"Khalifah","year":"1971","journal-title":"J. Biol. Chem."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"3413","DOI":"10.1016\/j.bmc.2016.05.029","article-title":"Anion inhibition profiles of alpha-, beta- and gamma-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae","volume":"24","author":"Vullo","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"4410","DOI":"10.1016\/j.bmc.2016.07.034","article-title":"Anion inhibition profiles of the complete domain of the eta-carbonic anhydrase from Plasmodium falciparum","volume":"24","author":"Vullo","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1016\/j.bmc.2016.01.005","article-title":"Cloning, characterization and anion inhibition studies of a gamma-carbonic anhydrase from the Antarctic bacterium Colwellia psychrerythraea","volume":"24","author":"Vullo","year":"2016","journal-title":"Bioorg. Med. Chem."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/2\/571\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T05:08:33Z","timestamp":1760159313000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/2\/571"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,1,8]]},"references-count":77,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2021,1]]}},"alternative-id":["ijms22020571"],"URL":"https:\/\/doi.org\/10.3390\/ijms22020571","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,1,8]]}}}