Pasteur Phosphofructokinase

Phosphofructokinase (EC 2.7.1.30) catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate as the key regulatory enzyme of glycolysis. Inhibition of phosphofructokinase by adenosine triphosphate and its activation by adenosine monophosphate and inorganic phosphate is held responsible for the induction of the Pasteur effect (for review see Ramaiah 1974). 

Because only two molecules of ATP are produced per glucose metabolized under anaerobic conditions, the cell must utilize additional glucose at a faster rate in order to maintain the pool of intracellular ATP. This step is accomplished through activation of the enzyme phosphofructokinase (Fig. 1.10), which, in turn, increases carbon flow through glycolysis. The increase in rate of glucose breakdown under anaerobic conditions is known as the Pasteur effect. This phenomenon is only observable when glucose concentrations are low, approximately 0.9 g/L (Walker, 1998). 

Regulation of phosphofructokinase is not enough to account for the inhibition of glucose utilization in aerobiosis. An additional link was needed. And it could not be understood without the realization that there is a glucose phosphorylation pathway that involves two steps a catalysed transport and an irreversible phosphorylation. Now, control of a pathway can take place either at the level of the first step or at the first irreversible step. Of the organisms more used in studies on the Pasteur effect, in animal cells the glucose phosphorylation pathway is feedback controlled by allosteric inhibition of hexokinase by glucose- P,... 

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