Cloning, expression and biochemical characterization of a beta-carbonic anhydrase from the soil bacterium Enterobacter sp B13

dc.contributor.authorEminoglu, Aysenur
dc.contributor.authorVullo, Daniela
dc.contributor.authorAsik, Aycan
dc.contributor.authorColak, Dilsat Nigar
dc.contributor.authorSupuran, Claudiu T.
dc.contributor.authorCanakci, Sabriye
dc.contributor.authorBelduz, Ali Osman
dc.date.accessioned2020-03-26T19:23:21Z
dc.date.available2020-03-26T19:23:21Z
dc.date.issued2016
dc.departmentSelçuk Üniversitesien_US
dc.description.abstractA recombinant carbonic anhydrase (CA, EC 4.2.1.1) from the soil-dwelling bacterium Enterobacter sp. B13 was cloned and purified by Co2+ affinity chromatography. Bioinformatic analysis showed that the new enzyme (denominated here B13-CA) belongs to the beta-class CAs and to possess 95% homology with the ortholog enzyme from Escherichia coli encoded by the can gene, whereas its sequence homology with the other such enzyme from E. coli (encoded by the cynT gene) was of 33%. B13-CA was characterized kinetically as a catalyst for carbon dioxide hydration to bicarbonate and protons. The enzyme shows a significant catalytic activity, with the following kinetic parameters at 20 degrees C and pH of 8.3: k(cat) of 4.8 x 10(5) s(-1) and k(cat)/K-m of 5.6 x 10(7) M-1 x s(-1). This activity was potently inhibited by acetazolamide which showed a K-l of 78.9 nM. Although only this compound was investigated for the moment as B13-CA inhibitor, further studies may reveal new classes of inhibitors/activators of this enzyme which may show biomedical or environmental applications, considering the posssible role of this enzyme in CaCO3 biomineralization processes.en_US
dc.identifier.doi10.3109/14756366.2015.1100176en_US
dc.identifier.endpage1118en_US
dc.identifier.issn1475-6366en_US
dc.identifier.issn1475-6374en_US
dc.identifier.issue6en_US
dc.identifier.pmid26497870en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage1111en_US
dc.identifier.urihttps://dx.doi.org/10.3109/14756366.2015.1100176
dc.identifier.urihttps://hdl.handle.net/20.500.12395/33361
dc.identifier.volume31en_US
dc.identifier.wosWOS:000385270300030en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherTAYLOR & FRANCIS LTDen_US
dc.relation.ispartofJOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRYen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.selcuk20240510_oaigen_US
dc.subjectbeta-Carbonic anhydraseen_US
dc.subjectEnterobacter sp.en_US
dc.subjectkineticsen_US
dc.titleCloning, expression and biochemical characterization of a beta-carbonic anhydrase from the soil bacterium Enterobacter sp B13en_US
dc.typeArticleen_US

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