Sulfonamide inhibition studies of the beta-carbonic anhydrase from the newly discovered bacterium Enterobacter sp B13

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dc.contributor.authorEminoglu, Aysenur
dc.contributor.authorVullo, Daniela
dc.contributor.authorAsik, Aycan
dc.contributor.authorColak, Dilsat Nigar
dc.contributor.authorCanakci, Sabriye
dc.contributor.authorBelduz, Ali Osman
dc.contributor.authorSupuran, Claudiu T.
dc.date.accessioned2020-03-26T19:26:39Z
dc.date.available2020-03-26T19:26:39Z
dc.date.issued2016
dc.departmentSelçuk Üniversitesien_US
dc.description.abstractThe genome of the newly identified bacterium Enterobacter sp. B13 encodes for a beta-class carbonic anhydrases (CAs, EC 4.2.1.1), EspCA. This enzyme was recently cloned, and characterized kinetically by this group (J. Enzyme Inhib. Med. Chem. 2016, 31). Here we report an inhibition study with sulfonamides and sulfamates of this enzyme. The best EspCA inhibitors were some sulfanylated sulfonamides with elongated molecules, metanilamide, 4-aminoalkyl-benzenesulfonamides, acetazolamide, and deacetylated methazolamide (K(I)s in the range of 58.7-96.5 nM). Clinically used agents such as methazolamide, ethoxzolamide, dorzolamide, brinzolamide, benzolamide, zonisamide, sulthiame, sulpiride, topiramate and valdecoxib were slightly less effective inhibitors (K(I)s in the range of 103-138 nM). Saccharin, celecoxib, dichlorophenamide and many simple benzenesulfonamides were even less effective as EspCA inhibitors, with K(I)s in the range of 384-938 nM. Identification of effective inhibitors of this bacterial enzyme may lead to pharmacological tools useful for understanding the physiological role(s) of the beta-class CAs in bacterial pathogenicity/virulence. (C) 2016 Elsevier Ltd. All rights reserved.en_US
dc.description.sponsorshipFP7 European Union Project [HEALTH-F2-2010-261460]en_US
dc.description.sponsorshipThis work was supported in part by an FP7 European Union Project (Gums & Joints, Grant agreement Number HEALTH-F2-2010-261460).en_US
dc.identifier.doi10.1016/j.bmcl.2016.02.032en_US
dc.identifier.endpage1826en_US
dc.identifier.issn0960-894Xen_US
dc.identifier.issn1464-3405en_US
dc.identifier.issue7en_US
dc.identifier.pmid26920803en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage1821en_US
dc.identifier.urihttps://dx.doi.org/10.1016/j.bmcl.2016.02.032
dc.identifier.urihttps://hdl.handle.net/20.500.12395/34036
dc.identifier.volume26en_US
dc.identifier.wosWOS:000371344600036en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherPERGAMON-ELSEVIER SCIENCE LTDen_US
dc.relation.ispartofBIOORGANIC & MEDICINAL CHEMISTRY LETTERSen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.selcuk20240510_oaigen_US
dc.subjectCarbonic anhydraseen_US
dc.subjectMetalloenzymesen_US
dc.subjectInhibitorsen_US
dc.subjectSulfonamideen_US
dc.subjectPathogenic bacteriaen_US
dc.subjectEnterobacter spp. B13en_US
dc.titleSulfonamide inhibition studies of the beta-carbonic anhydrase from the newly discovered bacterium Enterobacter sp B13en_US
dc.typeArticleen_US

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