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RJ5876 RJ5876
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Posts: 62
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11 years ago
A certain inhibitor of an enzymatic reaction was determined to act as a competitive inhibitor. Which of the following statements about the inhibitor is most likely to be true.

a. the inhibitor increases the Km (Michaelis constant) but has no effect on Vmax.
b. The inhibitor acts at a site other than the substrate binding site.
c. the inhibitor decreases the Km but has no effect on Vmax.
d. the inhibitor lowers the maximum velocity of the enzyme.
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wrote...
11 years ago
B is correct. inhibitors fit into the allosteric site, not the substrate site
wrote...
11 years ago
Actually, A is correct.

B. is true for uncompetitive inhibitors, NOT for competitive inhibitors. There are two different types. Uncompetitive inhibitors bind to an allosteric site rather than competing with the substrate for the active site, hence their name. Competitive inhibitors bind to the active site, pushing substrate out.

This also explains why competitive inhibitors alter Km but not Vmax. If you add enough substrate, eventually the substrate will out-compete the competitive inhibitor and even reach Vmax. It just takes more substrate to do that because it has competition for the active site.
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