{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T01:52:38Z","timestamp":1772761958247,"version":"3.50.1"},"reference-count":38,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2018,11,28]],"date-time":"2018-11-28T00:00:00Z","timestamp":1543363200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>We report the cloning and catalytic activity of a \u03b2-carbonic anhydrase (CA, EC 4.2.1.1), isolated from the pathogenic protozoan Entamoeba histolytica, EhiCA. This enzyme has a high catalytic activity for the physiologic CO2 hydration reaction, with a kcat of 6.7 \u00d7 105 s\u22121 and a kcat\/Km of 8.9 \u00d7 107 M\u22121 \u00d7 s\u22121. An anion inhibition study of EhiCA with inorganic\/organic anions and small molecules revealed that fluoride, chloride, cyanide, azide, pyrodiphosphate, perchlorate, tetrafluoroborate and sulfamic acid did not inhibit the enzyme activity, whereas pseudohalides (cyanate and thiocyanate), bicarbonate, nitrate, nitrite, diethyldithiocarbamate, and many complex inorganic anions showed inhibition in the millimolar range (KIs of 0.51\u20138.4 mM). The best EhiCA inhibitors were fluorosulfonate, sulfamide, phenylboronic acid and phenylarsonic acid (KIs in the range of 28\u201386 \u03bcM). Since \u03b2-CAs are not present in vertebrates, the present study may be useful for detecting lead compounds for the design of effective enzyme inhibitors, with potential to develop anti-infectives with alternative mechanisms of action.<\/jats:p>","DOI":"10.3390\/molecules23123112","type":"journal-article","created":{"date-parts":[[2018,11,28]],"date-time":"2018-11-28T11:43:44Z","timestamp":1543405424000},"page":"3112","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Cloning, Characterization and Anion Inhibition Studies of a \u03b2-Carbonic Anhydrase from the Pathogenic Protozoan Entamoeba histolytica"],"prefix":"10.3390","volume":"23","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3833-6629","authenticated-orcid":false,"given":"Susanna","family":"Haapanen","sequence":"first","affiliation":[{"name":"Faculty of Medicine and Health Technology, Tampere University, 33100 Tampere, Finland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0107-2682","authenticated-orcid":false,"given":"Silvia","family":"Bua","sequence":"additional","affiliation":[{"name":"Neurofarba Dept., Sezione di Scienze Farmaceutiche e Nutraceutiche, Universit\u00e0 degli Studi di Firenze, Via U. Schiff 6, Sesto Fiorentino, 50019 Florence, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marianne","family":"Kuuslahti","sequence":"additional","affiliation":[{"name":"Faculty of Medicine and Health Technology, Tampere University, 33100 Tampere, Finland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7323-8536","authenticated-orcid":false,"given":"Seppo","family":"Parkkila","sequence":"additional","affiliation":[{"name":"Faculty of Medicine and Health Technology, Tampere University, 33100 Tampere, Finland"},{"name":"Fimlab Ltd., Tampere University Hospital, 33100 Tampere, Finland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4262-0323","authenticated-orcid":false,"given":"Claudiu","family":"Supuran","sequence":"additional","affiliation":[{"name":"Neurofarba Dept., Sezione di Scienze Farmaceutiche e Nutraceutiche, Universit\u00e0 degli Studi di Firenze, Via U. Schiff 6, Sesto Fiorentino, 50019 Florence, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2018,11,28]]},"reference":[{"key":"ref_1","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_2","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_3","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. 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