- 1(current)
Q. No.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 |
91%
Level 1: 80%+
Hints
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 |
84%
Level 1: 80%+
Please attempt this question first.
Hints
Please attempt this question first.
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 |
78%
Level 2: 60%+
Please attempt this question first.
Hints
Please attempt this question first.
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 |
64%
Level 2: 60%+
Please attempt this question first.
Hints
Please attempt this question first.
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 |
Level 3: 35%-60%
Please attempt this question first.
Hints
Please attempt this question first.
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 |
Level 3: 35%-60%
Please attempt this question first.
Hints
Please attempt this question first.
- 1(current)
Q. No.
© 2025 GoodEd Technologies Pvt. Ltd.