Browsing by Author "Báez, Mauricio"
Now showing items 1-7 of 7
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Miño Galaz, Germán; Báez, Mauricio; Gutiérrez Gallardo, Gonzalo (2013)The strength of key interfacial contacts that stabilize protein–protein interactions have been studied by computer simulation. Experimentally, changes in the interface are evaluated by generating specific mutations ...
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Parducci, Rafael E.; Cabrera Paucar, Ricardo; Báez, Mauricio; Guixé Leguía, Victoria Cristina (AMER CHEMICAL SOC,, 2006-04-20)Phosphofructokinase-2 (Pfk-2) from Escherichia coli belongs to the ribokinase family of sugar kinases. One of the signatures observed in amino acid sequences from the ribokinase familiy members is the NXXE motif, which ...
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Báez, Mauricio; Babul Cattán, Jorge (ELSEVIER SCIENCE BV, 2009-05-22)Escherichia coli phosphofructokinase-2 (Pfk-2) is a homodimer whose subunits consist of a large domain and an additional b-sheet that provides the interfacial contacts between the subunits, creating a b-barrel flattened-like ...
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Caniuguir, Andrés; Cabrera Paucar, Ricardo; Báez, Mauricio; Vásquez, Claudio; Babul Cattán, Jorge; Guixé Leguía, Victoria Cristina (ELSEVIER SCIENCE BV, 2005-04-25)In a previous work, chemical modification of Cys-238 of Escherichia coli Pfk-2 raised concerns on the importance of the dimeric state of Pfk-2 for enzyme activity, whereas modification of Cys-295 impaired the enzymatic ...
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Cabrera Paucar, Ricardo; Báez, Mauricio; Pereira, Humberto M.; Caniuguir, Andrés; Garratt, Richard C.; Babul Cattán, Jorge (AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2011-02-18)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 ...
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Báez, Mauricio; Merino, Felipe; Astorga, Guadalupe; Babul Cattán, Jorge (ELSEVIER, 2008-06-11)Binding of MgATP to an allosteric site of Escherichia coli phosphofructokinase-2 (Pfk-2) provoked inhibition and a dimer-tetramer (D-T) conversion of the enzyme. Successive deletions of up to 10 residues and point mutations ...
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Unfolding pathway of the dimeric and tetrameric forms of phosphofructokinase-2 from Escherichia coli Báez, Mauricio; Cabrera Paucar, Ricardo; Guixé Leguía, Victoria Cristina; Babul Cattán, Jorge (2007)Escherichia coli phosphofructokinase-2 (Pfk-2) is an oligomeric enzyme characterized by two kinds of interfaces: a monomer-monomer interface, critical for enzymatic activity, and a dimer-dimer interface formed upon ...