The table presents the rates of reaction at specific substrate concentrations for an enzyme that displays classical Michaelis-Menten kinetics. Two sets of inhibitor data are also included.
[S] (mM) |
Vo (mM/min) Without Inhibitor |
Vo (mM/min) With Inhibitor |
1.3 |
2.50 |
1.17 |
2.6 |
4.00 |
2.10 |
6.5 |
6.30 |
4.00 |
13.0 |
7.60 |
5.70 |
26.0 |
9.00 |
7.20 |
a. Draw the Michaelis-Menten and Lineweaver burk plots for both sets of data. (Put both data sets on the same graph).
b. What is the Km and Vmax for the enzyme in the presence and absence of inhibitor?
c. What type of inhibitor is this? Explain.