Q. No.Enzymes speed up the chemical reactions by:
1. Getting used up in the reaction
2. Formation of different products
3. Converting endothermic reactions to exothermic
4. Lowering activation energy
1. Getting used up in the reaction
2. Formation of different products
3. Converting endothermic reactions to exothermic
4. Lowering activation energy
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The substrate concentration at which the enzyme catalyzed reaction achieves ½ Vmax is its ____ value.
| 1. | Km | 2. | Kcat |
| 3. | pKa | 4. | Q10 |
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In general, with every 10oC rise in the temperature [in the range 0oC to 40oC], the rate of enzyme catalyzed reaction:
1. Becomes half
2. Gets doubled
3. Remains same
4. There is no such correlation in general
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Low temperature:
1. Preserves enzyme in a temporary inactive state
2. Denatures the enzyme
3. Makes enzyme more active
4. Does not have any affect on enzyme activity
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In non competitive inhibition, an increase in substrate concentration would:
1. Increase the rate of the reaction
2. Decrease the rate of the reaction
3. Not increase the rate of the reaction
4. Nullify the effect of the inhibitor
Most common enzyme inhibition used in control of bacterial pathogens is:
| 1. Competitive | 2. Non - competitive |
| 3. Uncompetitive | 4. Mixed |
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Enzymes that catalyze removal of groups from substrates by mechanisms other than hydrolysis leaving double bonds are:
| 1. | Dehygdrogenases | 2. | Transferases |
| 3. | Lyases | 4. | Ligases |
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Transferases do not catalyze the transfer of the following group between a pair of substrates:
| 1. Glycosyl | 2. Amine |
| 3. Carboxyl | 4. Hydrogen |
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The non protein constituent present in many enzymes is called:
| 1. Co-enzyme | 2. Co-factor |
| 3. Apoenzyme | 4. Holoenzyme |
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Haem in hemoglobin:
1. is loosely bound
2. is the co-enzyme
3. is the prosthetic group
4. has no influence on activity of Hb
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