Interaction of ADP and fructose-2,6-bisphosphate with phosphofructokinase-1 from yeast.
ADP was found to activate or, depending on the experimental conditions, to inhibit yeast phosphofructokinase-1. In the absence of AMP and fructose-2,6-bisphosphate ADP increases the apparent affinity of the enzyme to fructose-6-phosphate. At low ATP concentrations the maximum activity with respect to fructose-6-phosphate decreases in the presence of ADP, while at high ATP a significant increase of the maximum activity by ADP is observed. In the presence of fructose-2,6-bisphosphate and AMP only the inhibiting effect of ADP persists. The data may be interpreted in terms of a hyperbolic inhibition mechanism.
D000244:Adenosine Diphosphate / Q000378:metabolism / Q000494:pharmacology*; D000249:Adenosine Monophosphate / Q000378:metabolism / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000378:metabolism / Q000494:pharmacology; D001667:Binding, Competitive; D005635:Fructosediphosphates / Q000378:metabolism / Q000494:pharmacology*; D006598:Hexosediphosphates / Q000494:pharmacology*; D007700:Kinetics; D010732:Phosphofructokinase-1 / Q000037:antagonists & inhibitors / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D005635:Fructosediphosphates; D006598:Hexosediphosphates; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; C027652:fructose 2,6-diphosphate; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1