Sort the phrases below as describing a competitive inhibitor,uncompetitive inhibitor or a pure noncompetitive inhibitor:

A. Structurally similar to substrate

B. When present, Vmax of enzyme is unaffected

C. When present, Km of enzyme will decrease

D. Binds enzyme-substrate complex only

E. Binds either enzyme or enzyme-substrate complex

F. Km is unchanged in the presence of this type of inhibitor

G. Prevents substrate from binding enzyme

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1. (3%) You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data are obtained: [S] V0 âInhibitor +Inhibitor 0.0001 33 17 0.0002 50 29 0.0005 71 50 0.001 83 67 0.002 91 80 0.005 96 91 0.01 98 95 0.02 99 98 0.05 100 99 0.1 100 100 0.2 100 100

a) What is the Vmax in the absence of inhibitor?

b) What is the Km in the absence of inhibitor?

c) When [S] = 0.0004, what will V0 be in the absence of inhibitor?

d) When [S] = 0.0004, what will V0 be in the presence of inhibitor?

e) What kind of inhibitor is it likely to be?

2. (2%) An enzyme is inhibited by two distinct competitive inhibitors, IA and IB. IA is shown to bind with a Ki of 13 Î¼M while IB binds with a Ki of 150 Î¼M.

a) Which is the more potent of the two inhibitors?

b) The natural substrate for the enzyme has a Km value of 0.1 mM. How does the substrate binding affinity compare to each of the two competitive inhibitors?

3. (2%) Assuming they have equal affinity for the enzyme, why would a noncompetitive inhibitor be a more effective drug than a competitive inhibitor?

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