Enzymes MCQs : This section focuses on the "Enzymes". These Multiple Choice Questions (MCQs) should be practiced to improve the Enzymes skills required for various interviews (campus interview, walk-in interview, company interview), placement, entrance exam and other competitive examinations.
What is the name of the substance present in leech that acts as anti blood coagulant
The proteolysis rate enhancement by chymotrypsin (~1010 folds) corresponds to a reduction in activation energy of about
A. 40 kJ/mol
B. 49 kJ/mol
C. 58 kJ/mol
D. 88 kJ/mol
In the enzyme-catalyzed reaction shown below, what will be the effect on substances A, B, C, and D of inactivating the enzyme labeled E2? A ---(E1)---> B ---(E2)---> C ---(E3)--->
A. A, B, C, and D will all still be produced
B. A, B, and C will still be produced, but not D
C. A and B will still be produced, but not C or D
D. A will still be produced, but not B, C, or D
Tryprotophan synthetase of E.coli, a typical bifunctional oligomeric enzyme consist of
A. a protein designated A
B. two proteins designated A and B
C. a protein A and one-subunit a
D. a protein designated B
The nucleophile in serine proteases is
C. both (a) and (b)
Which of the following is false statement with regard to comparison between Serine and HIV proteases?
A. Both use nucleophilic attack to hydrolyze the peptide bond
B. Both require water to complete the catalytic cycle
C. Both forms an acyl-enzyme intermediate
D. Both show specificity for certain amino acid sequences
Which of the common features are shared between serine and aspartate proteases?
A. Both require water to complete the catalytic cycle
B. Both use a base to activate the nucleophile
C. Both show specificity for certain amino acid sequences
D. All of the above
Before they can react, many molecules need to be destabilized. This state is typically achieved through
A. changing the three-dimensional shape of the molecule
B. oxidizing the molecules by removing electrons
C. changing the reaction from a biosynthetic to a catabolic pathway
D. the input of a small amount of activation energy
Common feature in all serine proteases is a
A. hydrophobic specificity pocket
B. hydrophilic specificity pocket
C. cluster of reactive serine residues
D. single reactive serine residue
Which of the following (s) is/are serine proteases?
D. all of these
Which of the following statements about enzymes or their function is true?
A. Enzymes do not alter the overall change in free energy for a reaction
B. Enzymes are proteins whose three-dimensional form is key to their function
C. Enzymes speed up reactions by lowering activation energy
D. All of the above
Enzyme-driven metabolic pathways can be made more efficient by
A. concentrating enzymes within specific cellular compartments
B. grouping enzymes into free-floating, multienzyme complexes
C. fixing enzymes into membranes so that they are adjacent to each other
D. All of the above
The role of Asp 102 and His 57 during trypsin catalysis is to
A. neutralize the charge on the other's side chain
B. keep the specificity pocket open
C. function as a proton shuttle
D. clamp the substrate into the active site
What is the specificity of the Clostripain protease?
A. It cleave after Arg residues
B. It cleave after His residues
C. It cleave after Lys residues
D. None of the above
How is the enzyme COX-1 important in human health?
A. It helps to transport carbon dioxide in the blood
B. It is critical for the biosynthesis of DNA
C. It is a chemical derivative of aspirin
D. It catalyzes the production of hormones that maintain the stomach lining
The cleavage specificity of trypsin and chymotrypsin depend in part on the
A. proximity of Ser 195 to the active site or specificity pocket
B. size, shape, and charge of the active site or specificity pocket
C. presence of a low-barrier hydrogen bond in the active site or specificity pocket
D. absence of water in the active site
The E.coli pyruvic acid dehydrogenase complex is reported to
A. decatalyze the oxidation of pyruvic acid to acetyl Co A and CO2
B. Catalyze the oxidation of pyruvic acid to acetyl Co A and CO2
C. retard the reduction of pyruvic acid to acetyl Co A and CO2
D. Catalyze the reduction of pyruvic acid to acetyl Co A and CO2
Albinism is caused by the deficiency of which enzyme?
A. Phenylalanine hydroxylase
Cellulose is not digestible by humans due to the absence of which of the following enzymes?
Enzymes are basically ______
D. pyrimidine bases
Enzymes are generally named after the ________
A. compound on which they work
B. compound which they form as product
C. medium in which they act
D. place from where they are derived
Enzymes are regarded as ______
Enzymes reduce the magnitude of activation energy for a reaction.
Identify the correct statement about enzymes.
A. Enzymes increase the activation energy of a reaction
B. Enzymes need to be used in excess compared to the reagent to catalyse the reaction
C. Enzymes work only at their optimum temperature and pH
D. The activity of enzymes cannot be affected by other compounds
The enzyme which catalyses the conversion of proteins to amino acids is ______
The hydrolysis of lactose can be catalysed only by the enzyme lactase. Also, lactase is only able to work on lactose and no other compound.
The prosthetic groups which get attached to the enzyme at the time of reaction are called _____
Which of the following best describes a particular enzyme?
A. Chemical catalyst
B. Fibrous protein
C. Highly selective
D. Can be used for various reactions
Which of the following is a substrate specific enzyme?
D. Carbonic anhydrase
A __________is a biocatalyst that increases the rate of the reaction without being changed.
A. Aluminum oxide
B. Silicon dioxide
D. Hydrogen peroxide
Enzyme increases the rate of reaction by lowering the activation energy.
Lineweaver-Burk plot is also known as______
A. Double reciprocal plot
B. Hanes-Woolf plot
C. Eadie-Hofstee plot
D. Steady-state equation
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
Name the coenzyme of riboflavin (B2)?
A. NAD or NADP
B. FAD and FMN
C. Coenzyme A
D. Thiamine pyrophosphate
Name the enzyme secreted by pancreas?
D. Alcohol dehydrogenase
Name the enzyme which catalyzes the oxidation-reduction reaction?
B. Glutamine synthetase
Name the enzyme which is found in tears, sweat, and an egg white?
The zymogen is an inactive precursor of an active enzyme.
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
What is an Isozyme?
A. Same structure, different function
B. Different structure, the same function
C. Same structure, the same function
D. Different structure, different function
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
What is the nature of an enzyme?
What is the SI unit of enzyme activity?
Which of the following function is catalyzed by Racemases?
A. Removal of water
B. Intramolecular transfer of a functional group
C. Interconversion of L and D stereoisomers
D. Inversion of asymmetric carbon atom
Which of the following is an example of ligases enzyme?
Which of the following is not a catalytic strategy for an enzyme to perform specific reaction?
A. Covalent catalysis
B. Metal ion catalysis
C. Michaelis constant
D. Acid-base catalysis
Which of the following is INCORRECT for the lock-and-key model?
A. It is used to describe the binding process
B. The active site of the enzyme is complementary to the substrate
C. It demonstrates enzyme-substrate complex
D. The binding of the substrate produces a conformational change in enzyme
Which of the following is not an example of irreversible enzyme inhibitor?
C. Diisopropyl phosphoflouridate (DIPF)
D. Statin drugs
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
Which of this vitamin is associated with the coenzyme Biocytin?
A. Nicotinic acid