Now you study enzyme inhibition by measuring enzyme kinetics in the presence of
ID: 70148 • Letter: N
Question
Now you study enzyme inhibition by measuring enzyme kinetics in the presence of 10 mM of inhibitor A or inhibitor B (separately). The Lineweaver-Burk plots in the presence of these inhibitors are indicated by "+A" or "+B" in the Figure below. What Type of inhibitor of A and B is shown in the figure above (Competitive, pure noncompetitive, mixed non-competitive or uncompetitive) What effect (increase, decrease, stay the same) docs the inhibitor depicted below have on Vmax Effect of inhibitor A on Vmax: Effect of inhibitor B on Vmax: What effect (increase, decrease, stay the same) docs the inhibitor depicted below have on Vmax Effect of inhibitor A on Km: Effect of inhibitor B on Km: Using the data you have (depicted in the Figure above). Determine the Km and Vmax for the uninhibited enzyme (E) and the inhibitors (A and B).Explanation / Answer
1)
Inhibitor A: competitive
Inhibitor B: mixed non-competitive
2)
Competitive inhibitor binds to the enzyme’s actives site. It affects the Km, but will not affect Vmax.
Non-competitive inhibitor lowers the Vmax.
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