Phosphofructokinase, inhibition properties

This enzyme catalyses the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate (FBP) and is the key regulatory enzyme of glycolysis. The properties of phosphofructokinase (PFK) have been investigated in some detail in adult Moniezia expansa (60) and in plerocercoids of S. solidus (65), where its activity is modulated by a number of compounds, including ATP, AMP, fructose-6-phos-phate, Mg2 +, Mn2 +, K + and NH. In general, the PFKs from both species exhibit properties similar to those of the enzymes from mammalian sources and they probably regulate glycolysis in the same manner as their mammalian counterparts. The inhibitory effects of ATP on the PFK from Schistocephalus solidus and the relief of this inhibition by AMP are shown in Fig. 5.2. 

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