Binding kinetics of glucose and allosteric activators to human glucokinase reveal multiple conformational states.

@article{Antoine2009BindingKO,
  title={Binding kinetics of glucose and allosteric activators to human glucokinase reveal multiple conformational states.},
  author={Mathias Antoine and Jean A. Boutin and Gilles Ferry},
  journal={Biochemistry},
  year={2009},
  volume={48 23},
  pages={5466-82}
}
Slow conformational changes have been proposed to be responsible for the kinetic positive cooperativity of glucokinase (GK) with glucose. Induced-fit and preexisting equilibrium kinetic models have been previously suggested. In the present study, equilibrium and pre-steady-state fluorescence spectroscopy has been used to resolve those conflicting reports. Multiphasic transients were observed after rapid mixing of apo-GK with glucose. Progress curve analysis revealed inconsistencies with the… CONTINUE READING

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