You measure the initial velocity of an enzyme in the absence and presence of two inhibitors. In each case, the inhibitor is at 10 µM. Shown in the table below is the primary data for all three cases. Construct a Lineweaver-Burk plot for each case. Calculate the KM and Vmax for each case, both graphically and mathematically. Determine the mechanism for each inhibitor and where each will interact on the enzyme.
Initial Velocity (µmol/ml min)
Enzyme Enzyme Enzyme
[S] mM Alone + Inhibitor 1 + Inhibitor 2
0.33 1.65 1.05 0.79
0.50 2.13 1.43 1.02
1.00 2.99 2.22 1.43
2.00 3.72 3.08 1.79
5.00 4.00 3.80 2.00

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The Answer of You measure the initial velocity of an enzyme in the absence and presence of two inhibitors. In each case, the inhibitor is at 10 µM. Shown in the table below is the primary data for all three cases. Construct a Lineweaver-Burk plot for each case. Calculate the KM and Vmax for each case, both graphically and mathematically. Determine the mechanism for each inhibitor and where each will interact on the enzyme.
Initial Velocity (µmol/ml min)
Enzyme Enzyme Enzyme
[S] mM Alone + Inhibitor 1 + Inhibitor 2
0.33 1.65 1.05 0.79
0.50 2.13 1.43 1.02
1.00 2.99 2.22 1.43
2.00 3.72 3.08 1.79
5.00 4.00 3.80 2.00

You Measure the Initial Velocity of an Enzyme in the Absence