{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T00:04:17Z","timestamp":1787011457163,"version":"build-2736575974"},"reference-count":40,"publisher":"International Union of Crystallography (IUCr)","issue":"12","license":[{"start":{"date-parts":[[2015,11,26]],"date-time":"2015-11-26T00:00:00Z","timestamp":1448496000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2015,11,26]],"date-time":"2015-11-26T00:00:00Z","timestamp":1448496000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr D Biol Crystallogr","Acta Crystallogr D","Acta Crystallogr D Biol Cryst","Acta Cryst D","Acta Cryst D Biol Crystallogr","Acta Cryst D Biol Cryst","Acta Cryst Sect D","Acta Cryst Sect D Biol Cryst","Acta Crystallogr Sect D","Acta Crystallogr Sect D Biol Crystallogr"],"published-print":{"date-parts":[[2015,12,1]]},"abstract":"<jats:p>\n                    Carbonic anhydrase (CA) is a zinc enzyme that catalyzes the reversible conversion of carbon dioxide to bicarbonate (hydrogen carbonate) and a proton. CAs have been extensively investigated owing to their involvement in numerous physiological and pathological processes. Currently, CA inhibitors are widely used as antiglaucoma, anticancer and anti-obesity drugs and for the treatment of neurological disorders. Recently, the potential use of CA inhibitors to fight infections caused by protozoa, fungi and bacteria has emerged as a new research direction. In this article, the cloning and kinetic characterization of the \u03b2-CA from\n                    <jats:italic>Vibrio cholerae<\/jats:italic>\n                    (VchCA\u03b2) are reported. The X-ray crystal structure of this new enzyme was solved at 1.9\u2005\u00c5 resolution from a crystal that was perfectly merohedrally twinned, revealing a tetrameric type II \u03b2-CA with a closed active site in which the zinc is tetrahedrally coordinated to Cys42, Asp44, His98 and Cys101. The substrate bicarbonate was found bound in a noncatalytic binding pocket close to the zinc ion, as reported for a few other \u03b2-CAs, such as those from\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    and\n                    <jats:italic>Haemophilus influenzae<\/jats:italic>\n                    . At pH 8.3, the enzyme showed a significant catalytic activity for the physiological reaction of the hydration of CO\n                    <jats:sub>2<\/jats:sub>\n                    to bicarbonate and protons, with the following kinetic parameters: a\n                    <jats:italic>k<\/jats:italic>\n                    <jats:sub>cat<\/jats:sub>\n                    of 3.34 \u00d7 10\n                    <jats:sup>5<\/jats:sup>\n                    \u2005s\n                    <jats:sup>\u22121<\/jats:sup>\n                    and a\n                    <jats:italic>k<\/jats:italic>\n                    <jats:sub>cat<\/jats:sub>\n                    \/\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>m<\/jats:sub>\n                    of 4.1 \u00d7 10\n                    <jats:sup>7<\/jats:sup>\n                    \u2005\n                    <jats:italic>M<\/jats:italic>\n                    <jats:sup>\u22121<\/jats:sup>\n                    \u2005s\n                    <jats:sup>\u22121<\/jats:sup>\n                    . The new enzyme, on the other hand, was poorly inhibited by acetazolamide (\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>i<\/jats:sub>\n                    of 4.5\u2005\u00b5\n                    <jats:italic>M<\/jats:italic>\n                    ). As this bacterial pathogen encodes at least three CAs, an \u03b1-CA, a \u03b2-CA and a \u03b3-CA, these enzymes probably play an important role in the life cycle and pathogenicity of\n                    <jats:italic>Vibrio<\/jats:italic>\n                    , and it cannot be excluded that interference with their activity may be exploited therapeutically to obtain antibiotics with a different mechanism of action.\n                  <\/jats:p>","DOI":"10.1107\/s1399004715018635","type":"journal-article","created":{"date-parts":[[2015,11,25]],"date-time":"2015-11-25T11:39:42Z","timestamp":1448451582000},"page":"2449-2456","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":111,"title":["Crystal structure and kinetic studies of a tetrameric type II \u03b2-carbonic anhydrase from the pathogenic bacterium\n                    <i>Vibrio cholerae<\/i>"],"prefix":"10.1107","volume":"71","author":[{"given":"Marta","family":"Ferraroni","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sonia","family":"Del Prete","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniela","family":"Vullo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Clemente","family":"Capasso","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudiu T.","family":"Supuran","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2015,11,26]]},"reference":[{"key":"mn5102_bb1","doi-asserted-by":"crossref","first-page":"4111","DOI":"10.1128\/IAI.00409-09","volume":"77","author":"Abuaita","year":"2009","journal-title":"Infect. 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