dc.creator | Báez, Mauricio | |
dc.creator | Rodríguez, Patricio H. | |
dc.creator | Babul Cattán, Jorge | |
dc.creator | Guixé Leguía, Victoria Cristina | |
dc.date.accessioned | 2018-12-20T14:10:42Z | |
dc.date.available | 2018-12-20T14:10:42Z | |
dc.date.created | 2018-12-20T14:10:42Z | |
dc.date.issued | 2003 | |
dc.identifier | Biochemical Journal, Volumen 376, Issue 1, 2018, Pages 277-283 | |
dc.identifier | 02646021 | |
dc.identifier | 10.1042/BJ20030795 | |
dc.identifier | https://repositorio.uchile.cl/handle/2250/154395 | |
dc.description.abstract | Modification of Escherichia coli phosphofructokinase-2 (Pfk-2) with pyrene maleimide (PM) results in a rapid inactivation of the enzyme. The loss of enzyme activity correlates with the incorporation of 2 mol of PM/mol of subunit and the concomitant dissociation of the dimeric enzyme. The two modified residues were identified as Cys-238 and Cys-295. In the presence of the negative allosteric effector, MgATP, Cys-238 was the only modified cysteine residue. Kinetic characterization of the Cys-238-labelled Pfk-2 indicates that the enzyme is fully active, with the kinetic constants (Km, k car) being almost identical to the ones obtained for the native enzyme. The modified enzyme is a monomer in the absence of ligands and, like the native enzyme, behaves as a tetramer in the presence of the nucleotide. However, in the presence of fructose-6-phosphate (fru-6-P) and ATP -4, the enzyme behaves as a dimer, suggesting that the monomers undergo re-association in the presence of the substrates and | |
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 | Biochemical Journal | |
dc.subject | Allosteric regulation | |
dc.subject | Eosin-5-maleimide | |
dc.subject | Phospho-fructokinase-2 | |
dc.subject | Pyrene N-(1-pyrenyl) maleimide | |
dc.subject | SH group | |
dc.title | Structural and functional roles of Cys-238 and Cys-295 in Escherichia coli phosphofructokinase-2 | |
dc.type | Artículos de revistas | |