Q. No.
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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
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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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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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