Answer:
The correct answer is option c. "The apparent value of KM increases with a competitive inhibitor, while it remains unchanged with a noncompetitive inhibitor".
Explanation:
The KM value in an enzymatic reaction is defined as the substrate concentration at which the half of the enzyme molecules are binding with the substrate. A way to distinguish between a competitive and noncompetitive inhibition is that the apparent value of KM increases with a competitive inhibitor, while it remains unchanged with a noncompetitive inhibitor. A competitive inhibitor would make that a higher concentration of substrate is needed, while a noncompetitive inhibitor does not change KM since the inhibitor binds to a site of the enzyme different from the active site.
