Similarity of activation of yeast phosphofructokinase by AMP and fructose-2,6-bisphosphate.
Phosphofructokinase from yeast is effectively activated by AMP and fructose-2,6-bisphosphate by increasing the affinity of the enzyme to fructose-6-phosphate and the maximum activity toward this substrate. The enzyme is activated by AMP and fructose-2, 6-bisphosphate both at high and at low concentrations of ATP. The half maximum stimulation concentrations of AMP and fructose-2, 6-bisphosphate are about 200 microM and 2 microM, respectively. At saturating concentrations of AMP and fructose-2, 6-bisphosphate similar maximum activities were observed in the dependence of enzyme activity on the concentrations of fructose-6-phosphate. The fructose-6-phosphate affinity is more enhanced by fructose-2, 6-bisphosphate than by AMP.
D000249:Adenosine Monophosphate / Q000494:pharmacology*; D000255:Adenosine Triphosphate / Q000378:metabolism; D004789:Enzyme Activation; D005635:Fructosediphosphates / Q000494:pharmacology*; D005636:Fructosephosphates / Q000378:metabolism; D006598:Hexosediphosphates / Q000494:pharmacology*; D008433:Mathematics; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D005635:Fructosediphosphates; D005636:Fructosephosphates; D006598:Hexosediphosphates; D000249:Adenosine Monophosphate; C027618:fructose-6-phosphate; C027652:fructose 2,6-diphosphate; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1