Pyruvate Kinase Reaction Research Articles

Kinetic and Magnetic Resonance Studies of the Pyruvate Kinase Reaction: I. DIVALENT METAL COMPLEXES OF PYRUVATE KINASE

Kinetic and Magnetic Resonance Studies of the Pyruvate Kinase Reaction: I. DIVALENT METAL COMPLEXES OF PYRUVATE KINASE

MECHANISM OF THE PASTEUR EFFECT.

THE Pasteur effect was early attributed to the influence on the rate of glycolysis of changes in the balance of inorganic phosphate and of adenosine diphosphate and triphosphate following a transition from air to nitrogen1–3. The changes in content of several phosphate compounds during various experimental treatments of yeast suggested that ‘mitochondria’ adenosine triphosphate might not be freely available for phosphorylating fructose-6-phosphate4,5. An increase in fructose diphosphate was observed in muscle under anaerobic conditions6, and this was attributed to the activation of phosphofructokinase caused by the increased contents of adenosine monophosphate and inorganic phosphate and to a decreased content of adenosine triphosphate7. Moreover, an increase in the permeability of the mitochondrial membrane to adenosino diphosphate under anaerobic conditions has been postulated8. Finally, an acceleration in the turn-over rate of phosphoenolpyruvate followed by an increase of fructose diphosphate and of pyruvate were observed during the large increase in output of carbon dioxide in bananas ripening in air; an increase in the rate of glycolysis was postulated and this increase was attributed mainly to the localization of ‘glycolytic’ adenosine triphosphate (initially produced in the pyruvate kinase reaction) near to the sugar phosphorylating and glycolytic enzymes9.

Phosphorylation of Pyruvate by the Pyruvate Kinase Reaction and Reversal of Glycolysis in a Reconstructed System

Phosphorylation of Pyruvate by the Pyruvate Kinase Reaction and Reversal of Glycolysis in a Reconstructed System