The inhibition of succinic dehydrogenase by malonate is an example of:
1. Non-competitive reversible inhibition
2. Non-competitive irreversible inhibition
3. Competitive inhibition
4. Allosteric inhibition

Subtopic:  Enzyme Inhibition |
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The use of sulpha drugs used to slow down the growth of bacterial colonies is based on the principle of:
1. antigen-antibody interaction
2. competitive inhibition
3. allosteric feedback inhibition
4. mutagenesis
Subtopic:  Enzyme Inhibition |
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Consider the given statements regarding competitive enzyme inhibition:
Statement I: Competitive inhibitor closely resembles the substrate in its molecular structure
Statement II: In spite of its close structural similarity with the substrate, the inhibitor does not compete with the substrate for the substrate-binding site of the enzyme.
Statement III: Inhibition of succinic dehydrogenase by succinate which closely resembles the substrate malonate in structure is an example of competitive inhibition.
 
1. Statement I is correct; Statement II is correct;  Statement III is correct
2. Statement I is incorrect; Statement II is correct;  Statement III is incorrect
3. Statement I is correct; Statement II is incorrect;  Statement III is incorrect
4. Statement I is correct; Statement II is correct;  Statement III is incorrect
Subtopic:  Enzyme Inhibition: Introduction | Enzyme Inhibition |
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Consider the given two statements:
Assertion (A):  In competitive enzyme inhibition, the inhibitor binds to the active site of the enzyme, preventing the substrate from binding.
Reason (R):  Competitive inhibitors structurally resemble the substrate, allowing them to bind reversibly to the active site and reduce the enzyme's activity without affecting the maximal velocity (Vmax) of the reaction.
  
1. Both (A) and (R) are True and (R) correctly explains (A)
2. Both (A) and (R) are True and (R) does not correctly explain (A)
3. (A) is True, (R) is False
4. (A) is False, (R) is True
Subtopic:  Enzyme Inhibition |
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Consider the given two statements:
Assertion (A): The effect of competitive inhibition can be overcome by increasing
the substrate of the enzyme.
Reason (R): The presence of a competitive inhibitor can decrease the rate of
enzyme-catalyzed reaction by blocking the substrate from binding to the enzyme.
 
1. Both (A) and (R) are True and (R) correctly explains (A)
2. Both (A) and (R) are True but (R) does not correctly explain (A)
3. (A) is True but (R) is False
4. (A) is False but (R) is True
Subtopic:  Enzyme Inhibition: Introduction | Enzyme Inhibition |
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Consider the given two statements:

I:  In competitive enzyme inhibition, the substrate and inhibitor cannot bind to the enzyme at the same time.
II: The inhibitor always has a much higher affinity for the active site than the normal substrate.
 
1. Both I and II are correct and II explains I
2. Both I and II are correct but II does not explain I
3. I is correct but II is incorrect
4. I is incorrect but II is correct
Subtopic:  Enzyme Inhibition |
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