publication . Article . 2012

Effect of Hydrostatic Pressure on Allosteric Couplings in a Tryptophan-Shifted Variant of Phosphofructokinase from Bacillus Stearothermophilus

Whitaker, Amy M.; Reinhart, Gregory D.;
Open Access
  • Published: 01 Jan 2012 Journal: Biophysical Journal, volume 102, issue 3 (issn: 0006-3495, Copyright policy)
  • Publisher: Elsevier BV
Phosphofructokinase from Bacillus stearothermophilus is an allosteric, homotetrameric enzyme containing one tryptophan per subunit. Unlike its homolog from E. coli, the fluorescence of the native tryptophan is unresponsive to ligand binding. This study utilizes a tryptophan-shifted mutant (W179F/F240W) that is functionally similar to wild-type, however a decrease in fluorescence intensity of about 6.5% is associated with substrate, fructose 6-phosphate (Fru-6-P), binding and a decrease of approximately 20% is associated with inhibitor, phosphoenol pyruvate (PEP), binding. Dissociation constants equal 1.9±0.3 μM for Fru-6-P and 107±13 μM for PEP. This dissociatio...
free text keywords: Biophysics, Ligand (biochemistry), Dissociation constant, Substrate (chemistry), Allosteric regulation, Phosphofructokinase, Gibbs free energy, symbols.namesake, symbols, Hydrostatic pressure, Crystallography, Enthalpy, Biochemistry, Chemistry
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