What effect does a competitive inhibitor have on enzyme activity?

₹0.0

Question: What effect does a competitive inhibitor have on enzyme activity?

Options:

Correct Answer: Increases Km

Solution:

A competitive inhibitor increases the Km of the enzyme, indicating a higher substrate concentration is needed to reach half-maximal velocity.

What effect does a competitive inhibitor have on enzyme activity?

What effect does a competitive inhibitor have on enzyme activity?

Step 1: Understand what an enzyme is. An enzyme is a protein that helps speed up chemical reactions in the body.
Step 2: Know what a substrate is. A substrate is the molecule that an enzyme acts on.
Step 3: Learn about competitive inhibitors. A competitive inhibitor is a substance that competes with the substrate for the enzyme's active site.
Step 4: Recognize the effect of a competitive inhibitor. When a competitive inhibitor is present, it makes it harder for the substrate to bind to the enzyme.
Step 5: Understand Km. Km is a measure of how much substrate is needed for the enzyme to work at half of its maximum speed.
Step 6: Realize that a competitive inhibitor increases Km. This means that more substrate is needed to reach half of the enzyme's maximum activity.
Step 7: Conclude that the presence of a competitive inhibitor decreases the efficiency of the enzyme because it requires more substrate to achieve the same level of activity.

Competitive Inhibition – A competitive inhibitor binds to the active site of an enzyme, competing with the substrate and affecting the enzyme's ability to catalyze reactions.
Km (Michaelis constant) – Km is the substrate concentration at which the reaction rate is half of its maximum velocity (Vmax), indicating the affinity of the enzyme for the substrate.
Vmax (Maximum Velocity) – Vmax is the maximum rate of an enzyme-catalyzed reaction when the enzyme is saturated with substrate.