Answer:
d. increases PFK activity, decreases FBPase activity
Explanation:
Fructose-2,6-bisphophate is formed by the phosphorylation of fructose-6-phosphate catalyzed by phosphofructokinase-2, PFK-2.
Fructose-2,6-bisphophate functions as an allosteric effector of the enzymes phosphofructokinase-1, PFK-1 and fructose-1,6-bisphosphatase, FBPase.
Fructose-2,6-bisphophate has opposite effects on the enzymes, PFK-1 and FBPase. When it binds to the allosteric site of the enzyme, PFK-1, it increases the enzymes's activity by increasing its affinity for its substrate fructose-6-phosphate and reduces its affinity for its allosteric inhibitors ATP and citrate. However, when it binds to FBPase, it reduces its activity by reducing its affinity for glucose, its substrate
<span>It affects only one chemical reaction</span>
process by which one separates compounds from one another by passing a mixture through column that retains some compounds longer than others.
The answer is Argon (Ar).
