How can competitive and noncompetitive inhibition be distinguished in terms of km?
a. the apparent value of km decreases with a competitive inhibitor, while it remains unchanged with a noncompetitive inhibitor.
b. the apparent value of km increases with a competitive inhibitor, while it decreases with a noncompetitive inhibitor.
c. the apparent value of km increases with a competitive inhibitor, while it remains unchanged with a noncompetitive inhibitor.
d. the apparent value of km remains unchanged with a competitive inhibitor, while it increases for a noncompetitive inhibitor.

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.

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substitution is the answer in this case