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Now you study enzyme inhibition by measuring enzyme kinetics in the presence of

ID: 70165 • 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) Inhibitor A: Inhibitor B: What effect (increase, decrease, slay 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, slay the same) docs the inhibitor depicted below have on Vmax Effect of inhibitor A on Km: Effect of inhibitor A 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.