Q. No.
In the following graph, the X-axis will show:
1.
substrate concentration
2.
enzyme concentration
3.
pH
4.
enzyme concentration or substrate concentration
The rate of enzyme action decreases at higher temperature [after a certain value] because the increased heat
| 1. | changes the pH of the system |
| 2. | alters the active site of the enzyme |
| 3. | neutralizes the acids and bases in the system |
| 4. | increases the concentration of the enzyme |
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The "lock and key hypothesis", given be Emil Fischer, attempts to explain the mechanism of:
1. denaturation of enzyme proteins
2. the formation of peptide binds
3. sharing of electrons
4. enzyme specificity
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If an active-site directed inhibitor is present in the medium, the curve that will represent the progress of the chemical reaction will be shown by the letter:
| 1. D | 2. C |
| 3. A | 4. B |
If an non active-site directed inhibitor is present in the medium, the curve that will represent the progress of the chemical reaction will be shown by the letter:
1. D
2. C
3. B
4. A
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Which of the following will fit in the description of a competitive enzyme inhibitor?
| 1. | a highly reactive compound. |
| 2. | a metal ion such as Hg2+ or Pb2+. |
| 3. | structurally similar to the substrate. |
| 4. | water insoluble. |
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A non-competitive inhibitor of an enzyme catalyzed reaction
| 1. | binds to the Michaelis complex (ES). |
| 2. | increases Vmax. |
| 3. | is without effect at saturating substrate concentrations. |
| 4. | can actually increase reaction velocity in rare cases. |
The measurement of which of the following would be indicator of the degree of inhibition by a competitive enzyme inhibitor?
1. Vmax
2. The y-intercept on a Limeweaver-Burke Plot
3. Km
4. ¼ Vmax
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An allosteric inhibitor of an enzyme usually
| 1. | binds to the active site. |
| 2. | participates in feedback regulation. |
| 3. | denatures the enzyme. |
| 4. | causes the enzyme to work faster. |
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