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For an enzyme in the absence of inhibitor Vmax is 10 μM.s-1 and its Km is 2 mM. In the presence of a 3 mM inhibitor the apparent Vmax is 6.67 μM.s-1 and the apparent Km is 4 mM.Select the correct statementGroup of answer choicesalpha and alpha' = 3alpha' = 3alpha' = 2alpha = 1.5 and alpha' = 3alpha = 1.5alpha = 3 and alpha' = 1.5

Question

For an enzyme in the absence of inhibitor Vmax is 10 μM.s-1 and its Km is 2 mM. In the presence of a 3 mM inhibitor the apparent Vmax is 6.67 μM.s-1 and the apparent Km is 4 mM.Select the correct statementGroup of answer choicesalpha and alpha' = 3alpha' = 3alpha' = 2alpha = 1.5 and alpha' = 3alpha = 1.5alpha = 3 and alpha' = 1.5

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Solution 1

The correct statement is: "alpha = 1.5 and alpha' = 3"

Explanation: In enzyme kinetics, alpha (α) and alpha prime (α') are used to describe the effects of inhibitors on the maximum rate of reaction (Vmax) and the

Solution 2

The alpha (α) and alpha prime (α') values are used to determine the type of inhibition an enzyme is experiencing.

α is the ratio of the apparent Km in the presence of inhibitor to the Km in the absence of inhibitor (Km(app)/Km).

α' is the ratio of the apparent Vmax in the absence of inhibitor to the Vmax in the presence of inhibitor (Vmax/Vmax(app)).

Given the values in the question:

α = Km(app)/Km = 4 mM / 2 mM = 2

α' = Vmax/Vmax(app) = 10 μM.s-1 / 6.67 μM.s-1 = 1.5

So, the correct statement is "alpha = 2 and alpha' = 1.5". However, this option is not given in your list of answer choices.

If we consider the closest match from the given options, then "alpha = 1.5 and alpha' = 3" would be the closest, but it's not the accurate calculation based on the given data.

This problem has been solved

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