Reversible activation and inactivation of phosphofructokinase from Ascaris suum by the action of tissue-homologous protein phosphorylating and dephosphorylating enzymes.
In the presence of ATP-Mg2+, purified phosphofructokinase from Ascaris suum muscle was effectively phosphorylated and activated in vitro by a protein kinase purified from the same tissue. Both effects were reversed by the action of a purified protein phosphatase from the same tissue. The findings suggest the presence of a highly potent interconversion mechanism for phosphofructokinase in the muscle of the parasitic nematode.
D001200:Ascaris / Q000201:enzymology*; D004789:Enzyme Activation; D010732:Phosphofructokinase-1 / Q000032:analysis / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000494:pharmacology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000494:pharmacology*
D011494:Protein Kinases; D010732:Phosphofructokinase-1; D010749:Phosphoprotein Phosphatases