BIOLOGY (NEW SYLLABUS) Class: 1st year Chapter No.

05 - ENZYMES
Click the right answer.
1. The biological active proteins are:
a) Lipoproteins b) Glycoproteins c) Enzymes d) Hormones
2. All enzymes are proteins:
a) Fibrous b) Globular c) Non-enzymatic d) None
3. The optimum pH for pancreatic amylase is:
a) 7.6-7.0 b) 7-8 c) 6.8-7.2 d) 6.8-8
4. The optimum PH for pancreatic lipase is:
a) 9.7 b) 8.0 c) 5.5 d) 9.0
5. One of the following is competitive inhibitor:
a) Succinic acid b) Formic acid c) Malonic acid d) Maleic acid
6. The bio reactions catalyzed by enzymes
a) All b) Some c) Most d) No one
7. Lock & Key model was modified by:
a) Koshland b) Fiescher c) Dr. stahl d) Beacon
8. Non-detachable cofactor is:
a) Activator b) Co-factor c) Prosthetic d) None
group
9. The temperature of most of the enzymes of our body is……….. oC:
a) 37 b) 28 c) 25 d) 40
10. Competitive inhibitors are:
a) Similar to b) Different from c) Identical to d) All are possible
substrate substrate substrate
11. Pepsinogen is:
a) Pro-enzyme b) Apo-enzyme c) Pre-enzyme d) Co-enzyme
12. Most of the enzymes are:
a) Floating in b) Attached to c) Attached to cell d) Present in
cytosol membrane membrane nucleus
13. If you add more substrate to already occurring enzymatic reaction and it has no effect on the
rate of reaction, what is the term given for this situation?
a) Saturation b) Unsaturation c) Composition d) Inhibition
14. The rate of enzyme-catalyzed reaction:
a) Is constant b) Cannot be c) Decrease at d) Can be reduced
under all measured substrate conc. by inhibitors
conditions
15. The active site of an enzyme:
a) Never changes b) Forms no c) Determines by d) None of these
chemical bond its structure,
with substrate the specificity
of enzyme
16. The detachable cofactor is called activator if it is:
a) An organic ion b) An inorganic ion c) Any vitamin d) None
17. 10.0 is the optimum pH value for the enzyme:
a) Arginase b) Sucrase c) Enterkinase d) Chymotrypsin

18. Which of the following enzyme works efficiently at alkaline PH :

a) Pepsin b) Sucrase c) Salivary d) Catalase
amylase
19. The optimum pH for enzyme Arginase is:
a) 7.60 b) 9.00 c) 9.7 d) 2.00
20. The catalytic activity of an enzyme is restricted to its small portion called:
a) Active site b) Passive site c) Intermediate d) None
site
21. The reversible inhibitors usually constitute:
a) Strong linkage b) Weak linkage c) No linkage d) Medium linkage
with enzyme with enzyme with enzyme with enzyme
22. The enzymes involved in the synthesis of proteins are integral part of:
a) Chloroplast Mitochondria b) Golgi complex c) Ribosomes
23. Non protein part of an enzyme is:
a) Cofactor b) Prosthetic group c) Metal activator d) Coenzyme
24. The substance that sometimes acts as a source of chemical energy helping to drive the reaction that
would otherwise be difficult or impossible
a) Substrate b) Coenzyme c) Cofactor d) Metal activator
25. If non protein part of enzyme is loosely attached to protein part it is known as:
a) Cofactor b) Prosthetic group c) Metal activator d) Coenzyme
26. The essential raw materials from which the coenzymes are made up are:
a) Metal ions b) Vitamins c) Proteins d) Carbohydrates
27. An activated enzyme consisting of polypeptide chain and cofactor is known as:
a) Apo-enzyme b) Holo-enzyme c) Coenzyme d) Activator
28. NAD is an example of:
a) Dinucleotide b) Coenzyme c) Used in redox d) All
reaction
29. An activated enzyme consists of polypeptide chain and a……………….:
a) Prosthetic group b) Coenzyme c) Metallic d) Cofactor
activator
30. A three-dimensional cavity bearing a specific charge:
a) Allosteric site b) Binding site c) Active site d) Catalytic site
31. How catalytic site becomes activated:
a) By a cofactor b) By formation of c) By an activator d) By ATP
ES. Complex
32. According to lock and key model active site is used only as a__________:
a) 3-dimensional b) Catalytic activity c) Charge bearing d) Template
cavity site
33. Any factor which can alter the chemistry and,,,,,,,, of an enzyme can affect its rate of
catalysis:
a) Configuration b) Amino acid c) Amino acid d) Active site
composition sequence
34. Rate of enzymatic reaction directly depends upon:
a) Amount of b) Amount of c) Temperature d) All
enzyme substrate range
35. Enzyme required during-------- are present in dissolved form in cytosol:
a) Phagocytosis b) Beta-Oxidation c) Glycolysis d) CO2 Fixation
36. Enzyme denaturation resulted due to:
a) Slight change in b) Ionization of c) Extreme d) Ionization of
PH amino acids at change in PH substrate
active site
37. The inhibitor which may destroy the globular structure of enzymes:
a) Competitive b) Non-competitive c) Reversible d) Irreversible
38. Which inhibitor is able to make an EI complex but not a product:
a) Succinic acid b) Malonic acid c) Fumaric acid d) Oxalic acid
39. Histidine decarboxylase is ……………….. type of enzymes.
a) Lyases b) Transferases c) Oxidoreductases d) Hydrolyse
 40. Which enzyme catalyzes the oxidation-reduction reaction?
a) oxygenases b) transmethylases c) lyases d) peptidases
41. Which of the following an example is of hydrolyses?
a) lipase b) glycogen c) pyruvate decarboxylase d) cytochrome oxidase
phosphorylase
42. Enzymes catalyzing rearrangement of atomic grouping without alternating molecular weight
or number of atoms is;
a) Ligase b) isomerase c) oxidoreductase d) peptidases
43. Hexokinase enzyme that catalyze the conversion of glucose into glucose 6 phosphate
is…………type of enzyme.
a) lyases b) transferases c) oxidoreducatse d) hydrolyses
44. A-B+C=A+B-C; the above reaction can be catalyzed by;
a) lyases b) transferases c) oxidoreducatse d) hydrolyses
45. The enzymes catalyze the reaction in which two molecules are joined together by synthesis of
new bond ,using energy from ATP, are placed in group;
a) hydrolyses b) ligase c) lyase d) transferase

Answers:
1. C 21. B
2. B 22. D 41. A
3. A 23. A 42. B
4. B 24. C 43. B
5. C 25. B 44. B
6. A 26. B 45. B
7. A 27. D
8. C 28. D
9. A 29. D
10. A 30. C
11. A 31. B
12. B 32. D
13. A 33. A
14. D 34. D
15. C 35. C
16. B 36. C
17. A 37. D
18. D 38. B
19. C 39. A
20. A 40. A

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