| 1. | will double |
| 2. | will decrease by half |
| 3. | will remain the same |
| 4. | will become zero and the reaction will stop |
| Assertion (A): | Enzyme-catalyzed reactions proceed at rates vastly higher than that of uncatalyzed ones. |
| Reason: | Enzymes require an optimum temperature and an optimum pH to work efficiently. |
| 1. | (A) is True but (R) is False. |
| 2. | Both (A) and (R) are True but (R) is not the correct explanation of (A). |
| 3. | (A) is False but (R) is True. |
| 4. | Both (A) and (R) are True and (R) is the correct explanation of (A). |
| I: | the formation of an ‘ES’ complex is not obligatory. |
| II: | ES’ complex formation is a transient phenomenon. |
| 1. | Only I is correct |
| 2. | Only II is correct |
| 3. | Both I and II are correct |
| 4. | Both I and II are incorrect |
| 1. | Enzymes generally function in a narrow range of temperature and pH. |
| 2. | Each enzyme shows its highest activity at a particular temperature and a pH called the optimum temperature and the optimum pH. |
| 3. | Activity declines both below and above the optimum value. |
| 4. | Low temperatures denature the enzyme; high temperatures temporarily inactivate the enzyme. |
| 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 |
| a. | are inorganic compounds |
| b. | are permanently associated with the apoenzyme |
| c. | are organic compounds |
| d. | are transiently associated with the apoenzyme. |
| 1. | a and b are correct |
| 2. | a and d are correct |
| 3. | b and c are correct |
| 4. | c and d are correct |
| I: | form covalent bonds with side chains at the active site of the enzyme |
| II: | form one or more covalent bonds with the substrate. |
| 1. | tertiary structure of an enzyme. |
| 2. | active site of an enzyme. |
| 3. | tertiary structure of an enzyme. |
| 4. | allosteric site on an enzyme. |