dc.creator | Cabrera Paucar, Ricardo | |
dc.creator | Báez, Mauricio | |
dc.creator | Pereira, Humberto M. | |
dc.creator | Caniuguir, André S. | |
dc.creator | Garratt, Richard C. | |
dc.creator | Babul Cattán, Jorge | |
dc.date.accessioned | 2018-12-20T14:06:13Z | |
dc.date.available | 2018-12-20T14:06:13Z | |
dc.date.created | 2018-12-20T14:06:13Z | |
dc.date.issued | 2011 | |
dc.identifier | Journal of Biological Chemistry, Volumen 286, Issue 7, 2018, Pages 5774-5783 | |
dc.identifier | 00219258 | |
dc.identifier | 1083351X | |
dc.identifier | 10.1074/jbc.M110.163162 | |
dc.identifier | https://repositorio.uchile.cl/handle/2250/153857 | |
dc.description.abstract | Substrate inhibition by ATP is a regulatory feature of the phosphofructokinases isoenzymes from Escherichia coli (Pfk-1 and Pfk-2). Under gluconeogenic conditions, the loss of this regulation in Pfk-2 causes substrate cycling of fructose-6-phosphate (fructose-6-P) and futile consumption of ATP delaying growth. In the present work, we have broached the mechanism of ATP-induced inhibition of Pfk-2 from both structural and kinetic perspectives. The crystal structure of Pfk-2 in complex with fructose-6-P is reported to a resolution of 2 Å. The comparison of this structure with the previously reported inhibited form of the enzyme suggests a negative interplay between fructose-6-P binding and allosteric binding of MgATP. Initial velocity experiments show a linear increase of the apparent K0.5 for fructose-6-P and a decrease in the apparent kcat as a function of MgATP concentration. These effects occur simultaneously with the induction of a sigmoidal kinetic behavior (nH of approximately 2). | |
dc.language | en | |
dc.rights | http://creativecommons.org/licenses/by-nc-nd/3.0/cl/ | |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Chile | |
dc.source | Journal of Biological Chemistry | |
dc.subject | Biochemistry | |
dc.subject | Molecular Biology | |
dc.subject | Cell Biology | |
dc.title | The crystal complex of phosphofructokinase-2 of Escherichia coli with fructose-6-phosphate: Kinetic and structural analysis of the allosteric atp inhibition | |
dc.type | Artículos de revistas | |