Phosphofructokinase 2 the enzyme that forms fructose 2,6-bisphosphate from fructose 6-phosphate and ATP

When measured in the high-speed supernatant obtained from isolated rat hepatocytes, the apparent activity of this enzyme was decreased several fold by treatment of the cells with glucagon, and could be separated from the classical phosphofructokinase (ATP-D-fructose 6-phosphate 1-ph phosphotransferase) which is now called phosphofructureokinase 1.

Abstract

An enzyme, partially purified from rat liver, catalysed the transfer of the γ-phosphoryl group of ATP to the hydroxyl present on carbon 2 of fructose 6-phosphate. This enzyme, which has been called phosphofructokinase 2, could be separated from the classical phosphofructokinase (ATP-D-fructose 6-phosphate 1-phosphotransferase) which is now called phosphofructokinase 1. The activity of phosphofructokinase 2 was stimulated by Pi and AMP and inhibited P-enol-pyruvate and citrate. When measured in the high-speed supernatant obtained from isolated rat hepatocytes, the apparent activity of this enzyme was decreased several fold by treatment of the cells with glucagon.