In competitive enzyme inhibition, how do the Michaelis constant () and the maximum velocity () change in the presence of the inhibitor?
Answer and explanation
Correct answer: C. increases while remains unchanged
- Step 1: A competitive inhibitor closely resembles the natural substrate in chemical structure and competes directly for the active site.
- Step 2: At sufficiently high substrate concentrations, the substrate displaces the inhibitor, allowing the enzyme to achieve its original maximum velocity ( unchanged).
- Step 3: Because more substrate is required to achieve half-maximal velocity, the apparent substrate affinity decreases, causing an increase in the numerical value of .
Answer
increases while remains unchanged.
Why not the others: unchanged while decreases is the characteristic pattern of non-competitive inhibition; Both and decrease describes uncompetitive inhibition; Both increasing does not occur in standard reversible inhibition.
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