- 1(current)
Q. No.Inhibition of succinate dehydrogenase by malonate is an example of:
1. Non-competitive inhibition
2. Competitive inhibition
3. Antagonism
4. Synergism
The Km value of an enzyme denotes the substrate concentration at which the enzyme catalyzed reaction:
| 1. | Reaches Vmax |
| 2. | Shows a decline in the rate of reaction |
| 3. | Attains ½ Vmax |
| 4. | Finally stops |
The Km value of an enzyme denotes the substrate concentration at which the enzyme catalyzed reaction:
1. Reaches Vmax
2. Shows decline in the rate of reaction
3. Attains ½ Vmax
4. Finally stops
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 |
Which of the following does not affect the activity of simple enzyme?
| 1. | Temperature |
| 2. | Presence of coenzymes |
| 3. | pH |
| 4. | Substarate concentration |
The following graphs show enzymatic activity for certain factors on x-axis and y-axis. Which of the following is correct in such regard?
1. Figure (1) ; x-axis - Potential energy , y-axis- Progress of reaction
2. Figure (2) ; x-axis - Enzymatic activity, y-axis- Temperature
3. Figure (3) ; x-axis- Velocity of reaction, y-axis-Substrate concentration
4. Figure (2) ; x-axis- pH, y-axis- Enzymatic activity
1. increasing the amount of substrate
2. adding more water
3. increasing the temperature
4. decreasing enzyme concentration
How many statements are false from given information?
| (a) | Ribozymes are enzyme made up of protein. |
| (b) | In every chemical reaction transition state energy is always greater than activation energy. |
| (c) | Co-factors are always proteinous in nature |
| (d) | Enzyme inhibition can not be removed. |
| (e) | Enzyme action can be stopped at low temp. |
| (f) | Km value (Michaelis constant) is the specific concentration of substrate molecule. |
1. 2
2. 3
3. 4
4. 5
- 1(current)
Q. No.
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