Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, isotope exchange at equilibrium, and partial reactions.

@article{JomainBaum1978KineticMO,
  title={Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, isotope exchange at equilibrium, and partial reactions.},
  author={M Jomain-Baum and Vern L Schramm},
  journal={The Journal of biological chemistry},
  year={1978},
  volume={253 10},
  pages={3648-59}
}
Initial velocity studies of rat liver cytosolic P-enolpyruvate carboxykinase in the direction of P-enolpyruvate formation gave intersecting double reciprocal plots indicating that the reaction conforms to a sequential reaction pathway. A complete product inhibition study with MnGDP-, P-enolpyruvate, and HCO3- as product inhibitors indicated that all patterns were noncompetitive. Isotope exchange at equilibrium with exchange between the substrate/product pairs GTP/GDP oxalacetate/HCO3-, and… CONTINUE READING
9 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

Similar Papers

Loading similar papers…