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dc.contributor.authorRohatgi, Neha
dc.contributor.authorGuðmundsson, Steinn
dc.contributor.authorRolfsson, Óttar
dc.date.accessioned2016-03-07T17:59:28Zen
dc.date.available2016-03-07T17:59:28Zen
dc.date.issued2015-11-30en
dc.date.submitted2016en
dc.identifier.citationFEBS Lett. 2015, 589 (23):3548-55en
dc.identifier.issn1873-3468en
dc.identifier.pmid26505675en
dc.identifier.doi10.1016/j.febslet.2015.10.024en
dc.identifier.urihttp://hdl.handle.net/2336/600764en
dc.descriptionTo access publisher's full text version of this article click on the hyperlink at the bottom of the pageen
dc.description.abstractGluconate is a commonly encountered nutrient, which is degraded by the enzyme gluconokinase to generate 6-phosphogluconate. Here we used isothermal titration calorimetry to study the properties of this reaction. ΔH, KM and kcat are reported along with substrate binding data. We propose that the reaction follows a ternary complex mechanism, with ATP binding first. The reaction is inhibited by gluconate, as it binds to an Enzyme-ADP complex forming a dead-end complex. The study exemplifies that ITC can be used to determine mechanisms of enzyme catalyzed reactions, for which it is currently not commonly applied.
dc.description.sponsorshipinfo:eu-repo/grantAgreement/EC/FP7/232816 RANNIS grant number: 130591-053.en
dc.language.isoenen
dc.publisherElsevier Science BVen
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/232816en
dc.relation.urlhttp://dx.doi.org/10.1016/j.febslet.2015.10.024en
dc.rightsrestrictedAccessen
dc.subject.meshAdenosine Diphosphateen
dc.subject.meshCalorimetryen
dc.subject.meshDose-Response Relationship, Drugen
dc.subject.meshEnzyme Inhibitorsen
dc.subject.meshGluconatesen
dc.subject.meshHumansen
dc.subject.meshKineticsen
dc.subject.meshPhosphorylationen
dc.subject.meshPhosphotransferases (Alcohol Group Acceptor)en
dc.subject.meshTemperatureen
dc.titleKinetic analysis of gluconate phosphorylation by human gluconokinase using isothermal titration calorimetry.en
dc.typearticleen
dc.contributor.departmentUniv Iceland, Ctr Syst Biol, IS-101 Reykjavik, Iceland, Univ Iceland, Biomed Ctr, IS-101 Reykjavik, Icelanden
dc.identifier.journalFEBS lettersen
dc.rights.accessNational Consortium - Landsaðganguren
html.description.abstractGluconate is a commonly encountered nutrient, which is degraded by the enzyme gluconokinase to generate 6-phosphogluconate. Here we used isothermal titration calorimetry to study the properties of this reaction. ΔH, KM and kcat are reported along with substrate binding data. We propose that the reaction follows a ternary complex mechanism, with ATP binding first. The reaction is inhibited by gluconate, as it binds to an Enzyme-ADP complex forming a dead-end complex. The study exemplifies that ITC can be used to determine mechanisms of enzyme catalyzed reactions, for which it is currently not commonly applied.


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