Question:
Inhibitor closely resemble the substrate in its molecular structure and inhibit the activity of the enzyme in
Inhibitor closely resemble the substrate in its molecular structure and inhibit the activity of the enzyme in
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In competitive inhibition:
The Michaelis constant (\(K_m\)) increases.
The maximum velocity (\(V_{max}\)) of the reaction remains unchanged because high substrate concentrations can outcompete the inhibitor.
The Michaelis constant (\(K_m\)) increases.
The maximum velocity (\(V_{max}\)) of the reaction remains unchanged because high substrate concentrations can outcompete the inhibitor.
Updated On: Jul 22, 2026
- Back inhibition
- Competence inhibition
- Non competence inhibition
- Homeostatic control metabolism
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The Correct Option is B
Solution and Explanation
Step 1: Understanding the Question:
The question asks to identify the type of enzyme inhibition where the chemical structure of the inhibitor closely resembles that of the normal substrate.
Step 2: Key Concepts and Approach:
Enzyme activity can be regulated or blocked by specific chemicals called inhibitors.
In competitive inhibition (referred to as "competence inhibition" in some translations), the inhibitor competes directly with the substrate for binding at the active site of the enzyme due to structural similarity.
Step 3: Detailed Explanation:
• Competitive Inhibition: Because of structural similarity with the substrate, the inhibitor fits into the active site of the enzyme, blocking substrate binding.
This reduces the rate of the enzymatic reaction.
This inhibition can be overcome by increasing the substrate concentration.
A classic example is the inhibition of succinate dehydrogenase by malonate, which structurally resembles the substrate succinate.
• Non-competitive Inhibition: The inhibitor binds to a site other than the active site (allosteric site).
This alters the enzyme conformation so the substrate can no longer bind, regardless of its concentration.
• Feedback Inhibition (Back inhibition): The end product of a metabolic pathway acts as an allosteric inhibitor of the first enzyme in the pathway.
Step 4: Final Answer:
The process where an inhibitor structurally resembles the substrate and competes for the active site is competitive ("competence") inhibition.
The question asks to identify the type of enzyme inhibition where the chemical structure of the inhibitor closely resembles that of the normal substrate.
Step 2: Key Concepts and Approach:
Enzyme activity can be regulated or blocked by specific chemicals called inhibitors.
In competitive inhibition (referred to as "competence inhibition" in some translations), the inhibitor competes directly with the substrate for binding at the active site of the enzyme due to structural similarity.
Step 3: Detailed Explanation:
• Competitive Inhibition: Because of structural similarity with the substrate, the inhibitor fits into the active site of the enzyme, blocking substrate binding.
This reduces the rate of the enzymatic reaction.
This inhibition can be overcome by increasing the substrate concentration.
A classic example is the inhibition of succinate dehydrogenase by malonate, which structurally resembles the substrate succinate.
• Non-competitive Inhibition: The inhibitor binds to a site other than the active site (allosteric site).
This alters the enzyme conformation so the substrate can no longer bind, regardless of its concentration.
• Feedback Inhibition (Back inhibition): The end product of a metabolic pathway acts as an allosteric inhibitor of the first enzyme in the pathway.
Step 4: Final Answer:
The process where an inhibitor structurally resembles the substrate and competes for the active site is competitive ("competence") inhibition.
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