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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What is the co-factor for the proteolytic enzyme, carboxypeptidase?
1. Molybdenum | 2. Manganese |
3. Zinc | 4. Copper |
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Most of the coenzymes contain:
1. Metal ions | 2. FMN and FAD |
3. Ribonucleoproteins | 4. Vitamins |
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Most common element present in human body is:
1. | Oxygen | 2. | Carbon |
3. | Hydrogen | 4. | Sulfur |
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Which of the following is not an aromatic amino acid?
1. Phenylalanine | 2. Threonine |
3. Tyrosine | 4. Tryptophan |
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