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Life Sciences Questions and Answers –

Enzymes – 1
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This set of Life Sciences Multiple Choice Questions & Answers (MCQs) focuses on “Enzymes – 1”.

1. A __________is a biocatalyst that increases the rate of the reaction without being changed.

a) Aluminum oxide

b) Silicon dioxide

c) Enzyme

d) Hydrogen peroxide

View Answer

Answer: c

Explanation: Among these options, an enzyme is an only option which is a biocatalyst that
catalyzes the chemical reaction without being changed while all other options are of the
catalyst which increases or decrease the rate of reaction based on their concentration.

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2. Enzyme increases the rate of reaction by lowering the activation energy.

a) True

b) False

View Answer

Answer: a

Explanation: Activation energy is the difference in free energy between the reactants and
transition state. To complete a reaction, enzyme lowers the activation energy and crosses the
transition state.

3. What is the nature of an enzyme?

a) Vitamin

b) Lipid

c) Carbohydrate

d) Protein

View Answer

Answer: d

Explanation: All enzymes are protein except Catalytic RNA molecule. The native protein
conformation of an enzyme defines its catalytic activity. Once the enzyme is denatured, its
catalytic activity is also lost.

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4. What is an apoenzyme?

a) It is a protein portion of an enzyme

b) It is a non-protein group

c) It is a complete, biologically active conjugated enzyme

d) It is a prosthetic group

View Answer
Answer: a

Explanation: Removal of cofactor from a conjugated enzymes forms apoenzyme which is a


protein component. A cofactor is a non-protein group while a complete conjugated enzyme is
known as a holoenzyme.

5. Name the coenzyme of riboflavin (B2)?

a) NAD or NADP

b) FAD and FMN

c) Coenzyme A

d) Thiamine pyrophosphate

View Answer

Answer: b

Explanation: Riboflavin is a part of vitamin B complex, its coenzyme form is a FAD (Flavin
adenine dinucleotide) which involves a redox reaction. NAD is a coenzyme form of nicotinic
acid, and thiamine pyrophosphate is a coenzyme of thiamine.

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6. Which of this vitamin is associated with the coenzyme Biocytin?

a) Nicotinic acid

b) Thiamine

c) Biotin

d) Pyridoxine

View Answer

Answer: c

Explanation: Biocytin is a coenzyme of biotin which involves in carboxylation reaction while


thiamine takes part in decarboxylation reaction.
7. Name the enzyme secreted by pancreas?

a) Pepsin

b) Chymotrypsin

c) Trypsin

d) Alcohol dehydrogenase

View Answer

Answer: c

Explanation: Trypsin is a proteolytic enzyme, secreted by the pancreas. It is one of the three
digestive proteinases along with pepsin and chymotrypsin which breaks down dietary protein
molecules into simpler forms.

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8. Name the enzyme which catalyzes the oxidation-reduction reaction?

a) Transaminase
b) Glutamine synthetase

c) Phosphofructokinase

d) Oxidoreductase

View Answer

Answer: d

Explanation: Oxidoreductase is a class of enzyme which catalyze the oxidation-reduction


reaction. Some of the oxidoreductase enzymes are oxidases, dehydrogenases, peroxidases
etc.

9. What is the function of phosphorylase?

a) Transfer inorganic phosphate

b) Transfer a carboxylate group

c) Use H2O2 as the electron acceptor

d) Transfer amino group

View Answer

Answer: a

Explanation: Phosphorylase is a transferase enzyme which involves a transfer of inorganic


phosphate to a substrate while transcarboxylase transfer a carboxylate group and
transaminase transfer amino group from amino acid to the keto acid.

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10. Mark the CORRECT function of enzyme, Peptidase?

a) Cleave phosphodiester bond

b) Cleave amino bonds

c) Remove phosphate from a substrate

d) Removal of H2O

View Answer

Answer: b

Explanation: Hydrolases are the enzymes which cleave the bond by adding water. Peptidases
belong to hydrolase class and it is used to cleave amide bonds of proteins.

11. Which of the following reaction is catalyzed by Lyase?

a) Breaking of bonds

b) Formation of bonds

c) Intramolecular rearrangement of bonds

d) Transfer of group from one molecule to another

View Answer

Answer: a

Explanation: Lyase is the class of enzymes which does not involve hydrolysis or oxidation to
break the bond. It catalyzes the breaking of C-C, C-O, C-N, C-S bonds by the process of
elimination and results in the formation of a double bond.

Sanfoundry Global Education & Learning Series – Life Sciences.

To practice all areas of Life Sciences, here is complete set of 1000+ Multiple Choice Questions
and Answers.

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