Author | dc.contributor.author | Cabrera Paucar, Ricardo | es_CL |
Author | dc.contributor.author | Báez, Mauricio | es_CL |
Author | dc.contributor.author | Pereira, Humberto M. | es_CL |
Author | dc.contributor.author | Caniuguir, Andrés | es_CL |
Author | dc.contributor.author | Garratt, Richard C. | |
Author | dc.contributor.author | Babul Cattán, Jorge | es_CL |
Admission date | dc.date.accessioned | 2011-10-20T14:59:32Z | |
Available date | dc.date.available | 2011-10-20T14:59:32Z | |
Publication date | dc.date.issued | 2011-02-18 | |
Cita de ítem | dc.identifier.citation | THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 286, NO. 7, pp. 5774–5783, February 18, 2011 | es_CL |
Identifier | dc.identifier.issn | 0021-9258 | |
Identifier | dc.identifier.other | DOI: 10.1074/jbc.M110.163162 | |
Identifier | dc.identifier.uri | https://repositorio.uchile.cl/handle/2250/119334 | |
General note | dc.description | Artículo de publicación ISI | es_CL |
Abstract | 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 angstrom. 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 K(0.5) for fructose-6-P and a decrease in the apparent k(cat) as a function of MgATP concentration. These effects occur simultaneously with the induction of a sigmoidal kinetic behavior (n(H) of approximately 2). Differences and resemblances in the patterns of fructose-6-P binding and the mechanism of inhibition are discussed for Pfk-1 and Pfk-2, as an example of evolutionary convergence, because these enzymes do not share a common ancestor. | es_CL |
Patrocinador | dc.description.sponsorship | Comision Nacional de Investigacion Cientifica y Tecnologica, Chile FONDECYT 1090336
CEPID
FAPESP
CNPq | es_CL |
Lenguage | dc.language.iso | en | es_CL |
Publisher | dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | es_CL |
Keywords | dc.subject | SUBSTRATE-INHIBITION | es_CL |
Título | dc.title | The Crystal Complex of Phosphofructokinase-2 of Escherichia coli with Fructose-6-phosphate. Kinetic and structural analysis of the allosteric atp inhibition | es_CL |
Document type | dc.type | Artículo de revista | |