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Response To Questions PartA To C A. Make a general graph the reaction velocity of PFK at low ATP levels and high ATP levels B. How does ATP specifically inhibit PFK (what does it do to the active site?) C. What happen s at this allosteric site when AMP levdls are high?

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Answer #1

A. The general graph for the reaction velocity of PFK at low and high levels of ATP is as follows:

B. PFK exist in two conformational states, both R and T states. ATP binds both active and allosteric sites in both conformations. While ATP binds the active site equally well, it preferentially binds the allosteric site of the T state . High levels of ATP leads to inhibitory effect to PFK by specifically binding to an allosteric site on PFK and lowering its affinity fructose 6-phosphate. High levels of ATP forms sigmoidal binding curve from hyperbolic binding curve.

C. AMP reverses the inhibitory action of ATP. It bind to the allosteric site and facilitates the formation of the R state by inducing structural changes in the enzyme. Activity of the enzyme increases when the cellular ATP/AMP ratio is lowered.

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