Enzymology (Biochemistry) BSc MCQs Set-1

Biochemistry Mcqs

1. The compound which has the lowest density is 

(A) Chylomicron 
(B) β-Lipoprotein 
(C) α-Lipoprotein 
(D) pre β-Lipoprotein 

Answer:(A) Chylomicron 

2. Non-steroidal anti-inflammatory drugs, such as aspirin act by inhibiting the activity of the enzyme: 

(A) Lipoxygenase 
(B) Cyclooxygenase
(C) Phospholipase A2 
(D) Lipoprotein lipase 

Answer:(B) Cyclooxygenase

3. From arachidonate, synthesis of prostaglandins is catalysed by 

(A) Cyclooxygenase 
(B) Lipoxygenase 
(C) Thromboxane synthase 
(D) Isomerase 

Answer:(A) Cyclooxygenase

4. A Holoenzyme is 

(A) Functional unit
(B) Apo enzyme 
(C) Coenzyme 
(D) All of these 

Answer:(D) All of these 

5. Gaucher’s disease is due to the deficiency of the enzyme: 

(A) α-Fucosidase 
(B) β-Galactosidase 
(C) β-Glucosidase 
(D) Sphingomyelinase 

Answer:(C) β-Glucosidase 

6. Niemann-Pick disease is due to the deficiency of the enzyme: 

(A) Hexosaminidase A and B 
(B) Ceramidase 
(C) Ceramide lactoside 
(D) Sphingomyelinase 

Answer:(D) Sphingomyelinase

7.Krabbe’s disease is due to the deficiency of the enzyme: 

(A) Ceramide lactoside
(B) Ceramidase 
(C) β-Galactosidase 
(D) GM1 β-Galactosidase

Answer: (C) β-Galactosidase 

8. Fabry’s disease is due to the deficiency of the enzyme: 

(A) Ceramide trihexosidase 
(B) Galactocerebrosidase 
(C) Phytanic acid oxidase 
(D) Sphingomyelinase 

Answer:(A) Ceramide trihexosidase

9. Farber’s disease is due to the deficiency of the enzyme: 

(A) α-Galactosidase 
(B) Ceramidase 
(C) β-Glucocerebrosidase 
(D) Arylsulfatase A. 

Answer:(B) Ceramidase

10. A synthetic nucleotide analogue, used in organ transplantation as a suppressor of immunologic rejection of grafts is 

(A) Theophylline 
(B) Cytarabine 
(C) 4-Hydroxy Pyrazolopyrimidine 
(D) 6-Mercaptopurine

Answer:(D) 6-Mercaptopurine

11. Example of an extracellular enzyme is 

(A) Lactate dehydrogenase 
(B) Cytochrome oxidase 
(C) Pancreatic lipase 
(D) Hexokinase 

Answer:(C) Pancreatic lipase

12. Enzymes, which are produced in inactive form in the living cells, are called

(A) Papain 
(B) Lysozymes
(C) Apoenzymes 
(D) Proenzymes 

Answer:(D) Proenzymes 

13. An example of ligases is 

(A) Succinate thiokinase 
(B) Alanine racemase 
(C) Fumarase 
(D) Aldolase 

Answer:(A) Succinate thiokinase

14. An example of lyases is 

(A) Glutamine synthetase 
(B) Fumarase 
(C) Cholinesterase 
(D) Amylase 

Answer:(B) Fumarase 

15. Activation or inactivation of certain key regulatory enzymes is accomplished by covalent modification of the amino acid: 

(A) Tyrosine 
(B) Phenylalanine 
(C) Lysine 
(D) Serine

Answer: (D) Serine

16. The enzyme which can add water to a carbon-carbon double bond or remove water to create a double bond without breaking the bond is 

(A) Hydratase 
(B) Hydroxylase 
(C) Hydrolase 
(D) Esterase 

Answer:(A) Hydratase

17. Fischer’s ‘lock and key’ model of the enzyme action implies that 

(A) The active site is complementary in shape to that of substance only after interaction. 
(B) The active site is complementary in shape to that of substance 
(C) Substrates change conformation prior to active site interaction 
(D) The active site is flexible and adjusts to substrate 

Answer:(B) The active site is complementary in shape to that of substance

18. From the Lineweaver-Burk plot of Michaelis-Menten equation, Km and Vmax can be determined when V is the reaction velocity at substrate concentration S, the X-axis experimental data are expressed as 

(A) 1/V 
(B) V
(C) 1/S 
(D) S 

Answer:(C) 1/S 

19. A sigmoidal plot of substrate concentration ([S]) verses reaction velocity (V) may indicate 

(A) Michaelis-Menten kinetics 
(B) Co-operative binding 
(C) Competitive inhibition 
(D) Non-competitive inhibition 

Answer:(B) Co-operative binding

20. The Km of the enzyme giving the kinetic data as below is 

(A) –0.50 
(B) –0.25 
(C) +0.25 
(D) +0.33

Answer: (D) +0.33

21. The kinetic effect of purely competitive inhibitor of an enzyme 

(A) Increases Km without affecting Vmax 
(B) Decreases Km without affecting Vmax 
(C) Increases Vmax without affecting Km 
(D) Decreases Vmax without affecting Km

Answer: (A) Increases Km without affecting Vmax

22. If curve X in the graph (below) represents no inhibition for the reaction of the enzyme with its substrates, the curve representing the competitive inhibition, of the same reaction is 

(A) A 
(B) B 
(C) C
(D) D 

Answer:(A) A 

23. An inducer is absent in the type of enzyme: 

(A) Allosteric enzyme 
(B) Constitutive enzyme 
(C) Co-operative enzyme 
(D) Isoenzymes enzyme 

Answer:(B) Constitutive enzyme 

24. A demonstrable inducer is absent in 

(A) Allosteric enzyme
(B) Constitutive enzyme 
(C) Inhibited enzyme 
(D) Co-operative enzyme

Answer:(B) Constitutive enzyme

25. In reversible non-competitive enzyme activity inhibition 

(A) Vmax is increased 
(B) Km is increased 
(C) Km is decreased 
(D) Concentration of active enzyme is reduced 

Answer:(D) Concentration of active enzyme is reduced 

26. In reversible non-competitive enzyme activity inhibition 

(A) Inhibitor bears structural resemblance to substrate 
(B) Inhibitor lowers the maximum velocity attainable with a given amount of enzyme 
(C) Km is increased 
(D) Km is decreased

Answer: (B) Inhibitor lowers the maximum velocity attainable with a given amount of enzyme

27. In competitive enzyme activity inhibition 

(A) The structure of inhibitor generally resembles that of the substrate 
(B) Inhibitor decreases apparent Km 
(C) Km remains ineffective 
(D) Inhibitor decreases Vmax without affecting Km 

Answer:(A) The structure of inhibitor generally resembles that of the substrate

28. In enzyme kinetics Vmax reflects 

(A) The amount of an active enzyme 
(B) Substrate concentration 
(C) Half the substrate concentration 
(D) Enzyme substrate complex 

Answer:(A) The amount of an active enzyme

29. In enzyme kinetics Km implies 

(A) The substrate concentration that gives one half Vmax 
(B) The dissocation constant for the enzyme substrate complex 
(C) Concentration of enzyme 
(D) Half of the substrate concentration required to achieve Vmax 

Answer:(A) The substrate concentration that gives one half Vmax

30. In competitive enzyme activity inhibition 

(A) Apparent Km is decreased 
(B) Apparent Km is increased 
(C) Vmax is increased 
(D) Vmax is decreased

Answer:(B) Apparent Km is increased