{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,25]],"date-time":"2026-02-25T18:41:45Z","timestamp":1772044905880,"version":"3.50.1"},"reference-count":58,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2017,6,18]],"date-time":"2017-06-18T00:00:00Z","timestamp":1497744000000},"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>In order to elucidate the elementary mechanism of the promiscuous esterase activity of human carbonic anhydrase (h-CA), we present an accurate theoretical investigation on the hydrolysis of fully-acetylated d-glucose functionalized as sulfamate. This h-CA\u2019s inhibitor is of potential relevance in cancer therapy. The study has been performed within the framework of three-layer ONIOM (QM-high:QM\u2019-medium:MM-low) hybrid approach. The computations revealed that the hydrolysis process is not energetically favored, in agreement with the observed weak carbonic anhydrase\u2019s esterase activity.<\/jats:p>","DOI":"10.3390\/molecules22061009","type":"journal-article","created":{"date-parts":[[2017,6,19]],"date-time":"2017-06-19T10:29:26Z","timestamp":1497868166000},"page":"1009","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Mechanistic Explanation of the Weak Carbonic Anhydrase\u2019s Esterase Activity"],"prefix":"10.3390","volume":"22","author":[{"given":"Paolo","family":"Piazzetta","sequence":"first","affiliation":[{"name":"Dipartimento di Chimica e Tecnologie Chimiche (CTC), Universit\u00e0 della Calabria, 87036 Arcavacata di Rende (CS), Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2386-9078","authenticated-orcid":false,"given":"Tiziana","family":"Marino","sequence":"additional","affiliation":[{"name":"Dipartimento di Chimica e Tecnologie Chimiche (CTC), Universit\u00e0 della Calabria, 87036 Arcavacata di Rende (CS), Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3826-3386","authenticated-orcid":false,"given":"Nino","family":"Russo","sequence":"additional","affiliation":[{"name":"Dipartimento di Chimica e Tecnologie Chimiche (CTC), Universit\u00e0 della Calabria, 87036 Arcavacata di Rende (CS), Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2017,6,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2954","DOI":"10.1021\/cs400806a","article-title":"Artificial Metalloenzymes and Metallopeptide Catalysts for Organic Synthesis","volume":"3","author":"Lewis","year":"2013","journal-title":"ACS Catal."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1021\/acscentsci.5b00056","article-title":"Enantioselective Enzyme-Catalyzed Aziridination Enabled by Active-Site Evolution of a Cytochrome P450","volume":"1","author":"Farwell","year":"2015","journal-title":"ACS Cent. 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