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first graph (a) activation of PfK by fructose2,6bisphosphate second (b) how atp

ID: 1036344 • Letter: F

Question

first graph (a) activation of PfK by fructose2,6bisphosphate second (b) how atp increases the apparent Km for substrate fructose6phosphate, inhibiting PFK. Can you include what is Km and how it is involved with it. And what I should know about this graphs.. thanks you 100 +0.13 mM fructose-2,6- bisphosphate C3 50 O 5 No fructose-2,6- bisphosphate [Fructose-6-phosphate] (a) Activation of PFK by fructose-2,6-bisphosphate. 100 Low [ATP] High [ATP] [Fructose-6-phosphate] (b) How ATP increases the apparent Kwfor substrate fructose-6-phosphate, inhibiting PFK.

Explanation / Answer

Km is referred to as '''michaelis constant" which is mathematically equal to the half if the maximum velocity. The point at which the maximum of the enzyme is converted to the ES complex is referred to as Vmax.

High valva of Km indicates that the substrate need high amounts of substrate to reach saturation and vice versa.

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From graph we know that fructose-6-phasphate has high Km value so shows a Vmax in the first graph