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7. Enzyme Inhibition and Regulation - Part 2 of 5
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7. Enzyme Inhibition and Regulation - Part 2 of 5
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7. Enzyme Inhibition and Regulation / Apparent Km and Vmax / Problem 3
Problem 3
Why does the apparent Km increase in the presence of a competitive inhibitor?
A
Because the inhibitor binds to the enzyme-substrate complex, increasing substrate binding.
B
Because the inhibitor decreases the enzyme's affinity for the substrate.
C
Because the inhibitor increases the enzyme's affinity for the substrate.
D
Because the inhibitor competes with the substrate for the active site, reducing substrate binding.
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