Abstract
Summary: The phosphofructokinase in crude extracts of Phycomyces blakesleeanus required the presence of ammonium salts, AMP or fructose 2,6-bisphosphate for its activity. The enzyme had slightly sigmoidal kinetics with respect to fructose 6-phosphate as substrate. It was slightly inhibited by high ATP concentrations and by citrate. Fructose 2,6-bisphosphate stimulated the Phycomyces blakesleeanus phosphofructokinase; the K m for fructose 6-phosphate decreased, the inhibition by ATP was completely relieved and the affinity for the activator ammonia was increased. AMP also stimulated the catalytic activity but there was poor co-operation with fructose 2,6-bisphosphate. Preliminary experiments showed that fructose 2,6-bisphosphate also stimulated the phosphofructokinase from Mucor rouxii, Neurospora tetrasperma and Agaricus bisporus.
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