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ADP-dependent phosphofructokinases from the archaeal order Methanosarcinales display redundant glucokinase activity
(Academic Press Inc., 2017)
© 2017 Elsevier Inc. The genome of Methanosarcinales organisms presents both ADP-dependent glucokinase and phosphofructokinase genes. However, Methanococcoides burtonii has a truncate glucokinase gene with a large deletion ...
Crystallographic Structure of Phosphofructokinase-2 from Escherichia coli in Complex with Two ATP Molecules. Implications for Substrate Inhibition
(ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD, 2008-08-22)
Phosphofructokinase-1 and -2 (Pfk-1 and Pfk-2, respectively) from
Escherichia coli belong to different homologous superfamilies. However, in
spite of the lack of a common ancestor, they share the ability to catalyze ...
Specificity evolution of the ADP-dependent sugar kinase family - in silico studies of the glucokinase/phosphofructokinase bifunctional enzyme from Methanocaldococcus jannaschii
(2008)
In several archaea of the Euryarchaeota, the glycolytic flux proceeds through a modified version of the Embden-Meyerhof pathway, where the phosphofructokinase and glucokinase enzymes use ADP as the phosphoryl donor. These ...
Chemical modification of SH groups of E. coli Phosphofructokinase-2 induces subunit dissociation: Monomers are inactive but preserve ligand binding properties
(Taylor & Francis, 2000)
Modification of Escherichia coli phosphofructokinase-2 (Pfk-2) with N- (1-pyrenil)maleimide results in an enzyme form that is inactive. However, the rate of modification is drastically reduced in the presence of the ...
Structural and functional roles of Cys-238 and Cys-295 in Escherichia coli phosphofructokinase-2
(2003)
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 ...
Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: A homodimeric enzyme with a complex domain organization
(2011)
Phosphofructokinase-2 is a 66 kD homodimer whose subunits are associated by means of a bimolecular domain, the β-clasp, which is linked to the larger portion of each subunit by a reentrant chain topology. To investigate ...
Ligand-dependent structural changes and limited proteolysis of Escherichia coli phosphofructokinase-2
(2002)
Binding of MgATPto the allosteric site of phosphofructokinase-2 promotes a dimer to tetramer conversion. In the presence of
Fru-6-Pthe enzyme remains as a dimer. Limited proteolysis in the presence of MgATPcompletely ...
Bifunctional ADP-dependent phosphofructokinase/glucokinase activity in the order methanococcales - biochemical characterization of the mesophilic enzyme from methanococcus maripaludis
(Blackwell Publishing Ltd, 2014)
In some archaea, the phosphorylation of glucose and fructose 6-phosphate (fructose 6P) is carried out by enzymes that are specific for either substrate and that use ADP as phosphoryl donor. In the hyperthermophilic archaeon ...
Adp-Dependent Phosphofructokinases From The Archaeal Order Methanosarcinales Display Redundant Glucokinase Activity
(2017)
The genome of Methanosarcinales organisms presents both ADP-dependent glucokinase and phosphofructokinase genes. However, Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminal, ...
Unraveling The Catalytic Mechanism Of Phosphofructokinase-2 From E. Coli: A Qm/Mm Theoretical Study
(2016)
The ATP-dependent phosphorylation of fructose-6-phosphate, named phosphofructokinase (PFK) activity, is one of
the most important steps in the glycolytic pathway; this is why it is highly regulated in a wide variety of ...