Question

Inhibitor closely resemble the substrate in its molecular structure and inhibit the activity of the enzyme in

• A. Back inhibition
• B. Competence inhibition
• C. Non competence inhibition
• D. Homeostatic control metabolism

Hint:

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.

Answer 1

The Correct Option is B

Step 1: Picture the enzyme's active site as a lock.
Only a key of the right shape fits.
Step 2: Compare the two kinds of blockers.
A molecule that looks almost like the real substrate can slide into that same lock and sit there, physically stopping the substrate from binding. A molecule that binds somewhere else on the enzyme instead changes its shape rather than fighting for the same site.
Step 3: Match this to the question.
Since the inhibitor here closely resembles the substrate's structure, it is fighting for the same active site, which is exactly what happens in competitive (called competence in the question) inhibition.
Final answer: Option 2, Competence (competitive) inhibition.