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From the data in the table, determine the following. Also determine if hydroxyme

ID: 59319 • Letter: F

Question


From the data in the table, determine the following. Also determine if hydroxymethlyaspartate is a competitive or noncompetitive inhibitor of the reaction.


Km for the uninhibited enzyme = uM


apparent Km for the inhibited enzyme = uM


the Vmax for the uninhibited enzyme = arbitrary units


the Vmax for the inhibited enzyme = arbitrary units


based on the above information the inhibitor is competitivenoncompetitive .

An aspartase-mediate deamination of -methylaspartate is carried out in the absence and presence of the inhibitor hydroxymethlyaspartate. Data for the reaction under these two conditions is shown in the table.


From the data in the table, determine the following. Also determine if hydroxymethlyaspartate is a competitive or noncompetitive inhibitor of the reaction.


Km for the uninhibited enzyme = uM


apparent Km for the inhibited enzyme = uM


the Vmax for the uninhibited enzyme = arbitrary units


the Vmax for the inhibited enzyme = arbitrary units


based on the above information the inhibitor is competitivenoncompetitive .







[S](uM) V, no inhibitor
(arbitrary units)
V, with inhibitor
(arbitrary units)
9 2.11E-2 7.59E-3 45 7.74E-2 3.36E-2 136 0.140 7.86E-2 227 0.167 0.107 454 0.195 0.147

Explanation / Answer

** It would be better to make a graph and answer the question. Anyways, I will calculate it theoritically.

1/Vo= 1/vmax +Km/Vmax * 1/S (without inhibitor)

Now, Vmax for inhibited enzyme is 0.147 ; Km will come greater than 136 micromole graphically

and Vmax for un-inhibited enzyme is 0.195. Km will come to be greater than 45 and less than 136 micromole graphically.

For unihibited enzyme,

1/.02 = 1/0.195 +Km / 0.195 * (1/9)

44.87 = Km/ 1.75

Km= 78.74 micromole

For inhibited enzyme, 1/0.007 = 1/0.147 + Km / 0.147 *(1/9)

142.85- 6.80 = Km/ 1.32 = 179.5 micromole

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