The enzyme phosphofructokinase (PFK) from E. coli is a tetrameric enzyme that ph
ID: 149611 • Letter: T
Question
The enzyme phosphofructokinase (PFK) from E. coli is a tetrameric enzyme that phosphorylates fructose-6-phosphate (F6P) to fructose-1,6-bisphosphate (F1,6BP) during gfycolysis. PFK activity is regulated by a number of metabolically relevant molecules, including AMP. The binding of AMP to PFK increases the affinity of the PFK active site for substrate(s). (Ipt) What are the substrate(s) of PFK? How could you use information in the paragraph above to answer this question? 8. (1pt) Which of the following is true concerning this system? a. AMP is an allosteric inhibitor and will stabilize PFK in a conformation that will 9. require more substrate to achieve 1/2 Vmax AMP is an allosteric activator and will stabilize PFK in a conformation that will require less substrate to achieve 1/2 Vmax. AMP is a competitive inhibitor AMP is a cofactor/coenzyme for PFK and is absolutely required for PFK activity. b. c. d.Explanation / Answer
8. The substate of PFK activity are Fructose-6-phosphate(F6P) and ATP(Adenosine tri phosphate).As in the above paragraph it is mentioned that the enzyme phosphofructokinase(PFK) phosphorylates fructose-6-phosphate(F6P) to Fructose-1,6-biphosphate(F1,6BP) during glycolysis.
9. AMP is an allosteric activator and will stabilize PFK in a conformation that will require less substrate to achieve 1/2 Vmax.(AMP reverse the inhibitory act of ATP in the PFK activity.In turn the activity of the enzyme increases when the ratio of ATP/AMP decreases.Thus,glycolysis is stimulated in the low energy state.
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