# (1) Vo(uM.S(2) Vo(3) Vo(mM)0.7712.51.1724.02.101.2556.34.002.002.50107.65.7209.07.22.86

Question
Asked Nov 27, 2019
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The following table indicates the rates at which a substrate reacts as catalyzed by an enzyme that follows the Michaelis-Menten mechanism: (1) in the absence of inhibitor; (2) and (3) in the presence of 10 mM concentration, respectively, of either of two inhibitors. Assume [E]T is the same for all reactions.

(a) Determine KM and Vmax for the enzyme. For each inhibitor determine the type of inhibition and KI and/or K’I. What additional information would be required to calculate the turnover number of the enzyme? (b) For [S] = 5 mM, what fraction of the enzyme molecules have a bound substrate in the absence of inhibitor, in the presence of 10 mM inhibitor of type (2), and in the presence of 10 mM inhibitor of type (3)?

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Step 1

In order to obtain a linear graph between th

In order to obtain a linear graph between the rate and substrate concentration, a Lineweaver -Burk graph is made in which the inverse of rate is plotted against inverse of substrate concentration. The Lineweaver-Burk relation is shown below. In the given relation, V is the reaction rate, VM is the maximum reaction velocity and KM is the Michaelis-Menten constant.

e rate and substrate concentration, a Lineweaver -Burk graph is made in which the inverse of rate is plotted against inverse of substrate concentration. The Lineweaver-Burk relation is shown below. In the given relation, V is the reaction rate, VM is the maximum reaction velocity and KM is the Michaelis-Menten constant.

Step 2

The graphs between substrate concentration and rate of reaction with and without inhibitors are shown below:

Step 3

According to the Lineweaver-Burk plot, the intercept is equal to 1/Vmax and slope is KM/Vmax. Therefore, from the equation on graph, the value of K...

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