A kinetic study of Baker's-yeast pyruvate kinase activated by fructose 1,6-diphosphate.

@article{Macfarlane1972AKS,
  title={A kinetic study of Baker's-yeast pyruvate kinase activated by fructose 1,6-diphosphate.},
  author={N. A. A. Macfarlane and Shaaron Ainsworth},
  journal={The Biochemical journal},
  year={1972},
  volume={129 5},
  pages={1035-47}
}
The paper reports a study of the kinetics of the reaction between phosphoenolpyruvate, ADP and Mg(2+) catalysed by yeast pyruvate kinase when activated by fructose 1,6-diphosphate and K(+). The experimental results indicate that the reaction mechanism is of the Ordered Tri Bi type with the substrates binding in the order phosphoenolpyruvate, ADP and Mg(2+). Direct phosphoryl transfer takes place in the quaternary complex, with pyruvate released before MgATP. A dead-end enzyme-pyruvate complex… CONTINUE READING