WHOLE XI BIOLOGY 5000+ MCQS WORKSHEET BY MATS

WITH 100+ DIFFERENT FORMATES OF MCQS

Sno. CHAPTERS MCQS
1 BIOLOGICAL MOLECULES 500
2 ENZYMES 500
3 CELL STRUCTURE & FUCTION 500
4 BIO-ENERGETICS 500
5 ACELLULAR LIFE 500
6 PROKARYOTES 500
7 NUTRITION 500
8 CIRCULATION 500
9 IMMUNITY 500
10 GASEOUS EXCHANGE 500
TOTAL 5000+

WORKSHEET
MEDICAL ASSESMENT TESTING SERVICE
02 ENZYMES
STRICKTLY FOLLOW NEW SINDH TEXT 2024-25
 MATS 500 MCQS WORKSHEET  ONLY FOR REGISTERED ASPIRANTS
Q01. Which of the following are characteristics
of enzymes?
A) They are proteins.
B) They are sensitive to temperature.
C) They are consumed in the reaction.
D) They are specific in nature.
A) A, B, C
B) B, C, D
C) A, B, D
D) A, B, C, D

Q02. Which of the following statements about

enzymes are correct?
I. Enzymes are biocatalysts produced in the In the diagram showing energy changes during
protoplasm. an enzyme-catalyzed reaction, which of the
II. All enzymes are proteins. following labels corresponds to the activation
III. Enzymes remain chemically unchanged energy without enzyme?
during the reaction. A) The energy barrier from reactants to the peak
IV. Enzymes are not specific in function. B) The energy barrier from reactants to the peak
A) I, II minus the energy with enzyme
B) II, III C) The difference in free energy between reactants
C) I, IV and products
D) II, IV D) The energy of the enzyme-substrate complex

Q03. [Refer to Fig 2.3: Energy of activation Q04. Which of the following statements about
diagram] enzymes is INCORRECT?
A) Enzymes are sensitive to pH.
B) Enzymes increase the activation energy of a
reaction.
C) Enzymes are not consumed in the reaction.

MATS NEW STB BOOK LINE WORKSHEETS 2025-26 (MATS OWNERS 03252257223) Page 1
D) Enzymes are specific in nature. D) Enzyme: Amylase - Substrate: Starch

Q05. What is the primary role of enzymes in Q10. The following are functions of different
biological systems? classes of enzymes:
A) To provide energy for metabolic reactions 1. Catalyze oxidation-reduction reactions.
B) To increase the temperature of the reaction 2. Transfer functional groups.
C) To lower the activation energy of reactions 3. Catalyze hydrolysis.
D) To change the equilibrium of the reaction 4. Break covalent bonds without hydrolysis.
5. Rearrange atoms within a molecule.
Q06. The following are locations where certain 6. Join molecules with covalent bonds.
enzymes act: These functions are related to which
1. Within the cell classification of enzymes?
2. Outside the cell A) Based on substrate
3. In the stomach B) Based on reaction type (as per IUBMB)
4. In the small intestine C) Based on cofactors
5. In the lysosomes D) Based on location
6. In the mitochondria
These locations are associated with which type of Q11. Match the following enzyme inhibition
enzymes? types with their characteristics:
A) Endoenzymes and exoenzymes Inhabition type Characteristics
B) Hydrolases 1. Competitive a. Binds to allosteric
C) Oxidoreductases inhibition site
D) Transferases 2. Non-competitive b. Binds to enzyme-
inhibition substrate complex
Q07. Match the following: 3. Uncompetitive c. Binds to active site
Column I (Enzyme) Column II (Function) inhibition
1. Pepsin a. Breakdown of fats A) 1-c, 2-a, 3-b
2. Amylase b. Hydrolysis of B) 1-a, 2-b, 3-c
proteins C) 1-b, 2-c, 3-a
3. Lipase c. Breakdown of starch D) 1-c, 2-b, 3-a
4. DNA polymerase d. Synthesis of DNA
A) 1-b, 2-c, 3-a, 4-d Q12. In feedback inhibition, the end product of a
B) 1-c, 2-b, 3-a, 4-d metabolic pathway binds to:
C) 1-b, 2-a, 3-c, 4-d A) The substrate of the first enzyme
D) 1-d, 2-c, 3-b, 4-a B) The active site of the first enzyme
C) An allosteric site on the first enzyme
Q08. Which of the following correctly matches D) The product of the last enzyme
the enzyme with its cofactor?
A) Chlorophyll: Magnesium Q13. An enzyme is found to have a higher
B) Carbonic anhydrase: Zinc optimal temperature than most human enzymes.
C) Cytochrome oxidase: Copper Which of the following is most likely true about
D) All of the above this enzyme?
A) It is derived from a thermophilic bacterium.
Q09. Which of the following is a mismatched B) It is a ribozyme.
pair? C) It has a lower molecular weight.
A) Enzyme: Pepsin - Substrate: Proteins D) It is denatured at 37°C.
B) Enzyme: Lipase - Substrate: Lipids
C) Enzyme: Sucrase - Substrate: Lactose

MATS NEW STB BOOK LINE WORKSHEETS 2025-26 (MATS OWNERS 03252257223) Page 2
Q14. Which of the following statements about 2. Catalyze specific reactions
enzyme kinetics is correct? 3. Mostly proteinaceous
A) At very high substrate concentrations, the rate of 4. Sensitive to temperature and pH
reaction is inversely proportional to enzyme 5. Lower activation energy
concentration. 6. Remain unchanged after reaction
B) The Michaelis constant (Km) is the substrate A) Hormones
concentration at which the reaction rate is half of B) Enzymes
Vmax. C) Antibodies
C) Competitive inhibition does not affect the Vmax D) Vitamins
of the reaction.
D) Non-competitive inhibition increases the Km of Q20. What would happen if the active site of an
the reaction. enzyme was made rigid and unable to change
shape?
Q15. Consider the reaction: X → Y → Z → A. If A) It would only catalyze reactions by the lock and
product A inhibits the enzyme that converts X to key mechanism.
Y, what is this mechanism called? B) It would be able to catalyze a wider range of
A) Competitive inhibition substrates.
B) Non-competitive inhibition C) It would lose its specificity for the substrate.
C) Feedback inhibition D) It would become a ribozyme.
D) Uncompetitive inhibition
Q21. Which of the following are functions of
Q16. Why do enzymes not alter the equilibrium cofactors in conjugated enzymes?
of a reaction? A) They are required for the attachment of the
A) They lower the activation energy for both substrate at the active site.
forward and reverse reactions equally. B) They perform catalytic activity.
B) They are consumed in the reaction. C) They are always proteins.
C) They only catalyze the forward reaction. D) They are permanently attached to the enzyme.
D) They increase the free energy change.
Q22. Which of the following are true about the
Q17. Arrange the following steps of enzyme induced fit model?
action in the correct sequence: I. The active site is rigid.
I. Formation of enzyme-substrate complex II. The substrate induces a change in the enzyme's
II. Release of product shape.
III. Binding of substrate to active site III. The enzyme is complementary to the substrate
IV. Conversion of substrate to product only after binding.
A) I, II, III, IV IV. It was proposed by Emil Fischer.
B) III, I, IV, II A) I and II
C) IV, I, III, II B) II and III
D) II, I, IV, III C) III and IV
D) I and IV
Q18. The active site of an enzyme is formed by:
A) The entire enzyme molecule Q23. [Refer to Fig 2.4: Effect of temperature on
B) Only the cofactor enzymes]
C) Specific amino acids in the polypeptide chain In the graph, the point where the enzyme activity
D) The prosthetic group is maximum is labeled as:
A) Denaturation point
Q19. The following are features of: B) Optimal rate
1. Organic substances C) Minimum temperature

MATS NEW STB BOOK LINE WORKSHEETS 2025-26 (MATS OWNERS 03252257223) Page 3
D) Activation energy B) Maltase: Sucrose
C) Sucrase: Maltose
Q24. Which of the following is an INCORRECT D) Amylase: Cellulose
statement about enzyme inhibitors?
A) Competitive inhibitors bind to the active site. Q29. Which of the following is a mismatched
B) Non-competitive inhibitors bind to a site other pair of enzyme and its cofactor?
than the active site. A) Carboxypeptidase: Zinc
C) Uncompetitive inhibitors bind only to the B) Catalase: Iron
enzyme-substrate complex. C) Cytochrome c: Copper
D) Feedback inhibition is a type of competitive D) Hexokinase: Magnesium
inhibition.
Q30. The following are functions:
Q25. Which of the following is a coenzyme? 1. Transfer of hydrogen atoms
A) Magnesium ion 2. Group transfer
B) NAD+ 3. Hydrolytic cleavage
C) Heme 4. Non-hydrolytic bond cleavage
D) Zinc ion 5. Intramolecular rearrangement
6. Joining of two molecules with covalent bonds
Q26. The following are locations where certain These are the functions of which group of
cofactors are found: enzymes?
1. Bound to the active site A) Transferases
2. Covalently attached to the enzyme B) Hydrolases
3. Loosely attached and detachable C) Lyases
4. Derived from vitamins D) Classes of enzymes based on reaction type
5. Inorganic ions
6. Organic molecules Q31. Match the following:
These are characteristics of which component of Model Scientist
enzymes? 1. Lock and key model a. Koshland
A) Apoenzyme 2. Induced fit model b. Emil Fischer
B) Cofactor 3. Ribozyme discovery c. Thomas Cech and
C) Holoenzyme Sidney Altman
D) Substrate 4. Feedback inhibition d. End product
inhibition
Q27. Match the enzyme class with the reaction A) 1-b, 2-a, 3-c, 4-d
type: B) 1-a, 2-b, 3-c, 4-d
Column I (Class) Column II (Reaction) C) 1-b, 2-a, 3-d, 4-c
1. Oxidoreductase a. Transfer of groups D) 1-c, 2-d, 3-a, 4-b
2. Transferase b. Hydrolysis
3. Hydrolase c. Isomerization Q32. In a reaction catalyzed by an enzyme, if the
4. Isomerase d. Redox reaction substrate concentration is increased beyond a
A) 1-d, 2-a, 3-b, 4-c certain point, the rate of reaction does not
B) 1-a, 2-b, 3-c, 4-d increase. Why?
C) 1-b, 2-c, 3-d, 4-a A) The enzyme becomes denatured.
D) 1-d, 2-b, 3-a, 4-c B) The enzyme is inhibited by the product.
C) The enzyme is saturated with substrate.
Q28. Which of the following correctly matches D) The enzyme is consumed in the reaction.
the enzyme with its substrate?
A) Lactase: Lactose

MATS NEW STB BOOK LINE WORKSHEETS 2025-26 (MATS OWNERS 03252257223) Page 4
Q33. If an enzyme has a prosthetic group, what B) Performing the chemical transformation
can be inferred? C) Releasing the product
A) The prosthetic group is loosely bound and acts D) All of the above
as a coenzyme.
B) The prosthetic group is covalently bound and an Q39. The following are features of:
integral part of the enzyme. 1. Non-protein part
C) The enzyme can function without the prosthetic 2. May be organic or inorganic
group. 3. Required for catalytic activity
D) The prosthetic group is always inorganic. 4. May be loosely or tightly bound
5. Activators are examples
Q34. Which type of inhibition can be overcome 6. Includes coenzymes and prosthetic groups
by increasing the substrate concentration? A) Substrate
A) Non-competitive inhibition B) Inhibitor
B) Uncompetitive inhibition C) Cofactor
C) Competitive inhibition D) Apoenzyme
D) Allosteric inhibition
Q40. What would be the effect on an enzyme-
Q35. Which of the following is true about catalyzed reaction if an allosteric activator binds
uncompetitive inhibition? to the enzyme?
A) The inhibitor binds only to the enzyme-substrate A) The enzyme's active site would become blocked.
complex. B) The enzyme would denature.
B) The inhibitor binds to the active site. C) The enzyme's affinity for the substrate might
C) The inhibitor binds to an allosteric site. increase.
D) The inhibitor is a substrate analog. D) The enzyme would become inhibited.

Q36. Why are enzymes not destroyed at low Q41. Which of the following are true about
temperatures? endoenzymes and exoenzymes?
A) Because they are denatured at low temperatures. A) Endoenzymes act within the cell.
B) Because the low temperature only reduces B) Exoenzymes act outside the cell.
molecular motion without breaking bonds. C) Pepsin is an exoenzyme.
C) Because enzymes become more active at low D) Intracellular enzymes are exoenzymes.
temperatures.
D) Because enzymes are stable at all temperatures. Q42. Which of the following are characteristics
of ribozymes?
Q37. Arrange the following in the sequence of I. They are made of RNA.
enzyme action: II. They are protein in nature.
I. Product formation III. They catalyze reactions in genetic information
II. Substrate binding processing.
III. Product release IV. They were discovered in the 1980s.
IV. Enzyme-substrate complex formation A) I, II, III
A) II, IV, I, III B) I, III, IV
B) IV, II, I, III C) II, III, IV
C) II, I, IV, III D) I, II, IV
D) IV, I, II, III

Q38. The catalytic site of an enzyme is

responsible for:
A) Binding the substrate

MATS NEW STB BOOK LINE WORKSHEETS 2025-26 (MATS OWNERS 03252257223) Page 5
Q43. [Refer to Fig 2.2: Induced fit model] 4. Phosphoglucomutase d. Isomerase
A) 1-a, 2-b, 3-c, 4-d
B) 1-b, 2-c, 3-d, 4-a
C) 1-c, 2-d, 3-a, 4-b
D) 1-d, 2-a, 3-b, 4-c

Q48. Which of the following correctly matches

Which step shows the enzyme changing shape the enzyme with its function?
upon substrate binding? A) Lipase: Breaks down proteins
A) Substrate entering active site B) Protease: Breaks down fats
B) Enzyme/Substrate complex C) Amylase: Breaks down starch
C) Enzyme/Products complex D) Lactase: Breaks down sucrose
D) Products leaving active site
Q49. Which of the following is a mismatched
Q44. Which of the following is INCORRECT pair of enzyme and its class?
about enzyme classification? A) Catalase: Oxidoreductase
A) Transferases transfer groups. B) Hexokinase: Transferase
B) Hydrolases break bonds by hydrolysis. C) Enolase: Lyase
C) Lyases break bonds without hydrolysis. D) Pepsin: Isomerase
D) Ligases break down molecules.
Q50. The following are features of enzyme
Q45. Which enzyme class catalyzes the inhibition:
conversion of glucose-6-phosphate to fructose-6- 1. Reversible
phosphate? 2. Binds to allosteric site
A) Transferase 3. Inhibited by its own product
B) Isomerase 4. Shuts down the pathway
C) Lyase 5. Occurs in metabolic pathways
D) Hydrolase 6. Binds to the first enzyme of the pathway
These features are related to:
Q46. The following are components of A) Competitive inhibition
conjugated enzymes: B) Non-competitive inhibition
1. Protein part C) Feedback inhibition
2. Non-protein part D) Uncompetitive inhibition
3. Holoenzyme
4. Apoenzyme Q51. Match the term with its definition:
5. Coenzyme Term Definition
6. Prosthetic group 1. Apoenzyme a. Enzyme with
These are associated with: cofactor
A) Simple enzymes 2. Holoenzyme b. Protein part of
B) Conjugated enzymes enzyme
C) Ribozymes 3. Coenzyme c. Organic cofactor,
D) Inhibitors loosely bound
4. Prosthetic group d. Organic cofactor,
Q47. Match the enzyme with its class: tightly bound
Enzymes Class A) 1-b, 2-a, 3-c, 4-d
1. DNA polymerase a. Ligase B) 1-a, 2-b, 3-d, 4-c
2. Alanine transaminase b. Transferase C) 1-c, 2-d, 3-b, 4-a
3. Trypsin c. Hydrolase D) 1-d, 2-c, 3-a, 4-b

MATS NEW STB BOOK LINE WORKSHEETS 2025-26 (MATS OWNERS 03252257223) Page 6
 D) II, III, I, IV
Q52. Which of the following is true about the
active site of an enzyme? Q58. The binding site of an enzyme is
A) It is the same for all enzymes. responsible for:
B) It is where the allosteric inhibitor binds. A) Catalyzing the reaction
C) It is complementary to the substrate in shape and B) Holding the substrate in place
charge. C) Releasing the product
D) It is destroyed after the reaction. D) Changing the shape of the enzyme

Q53. If an enzyme is denatured, what is the most

likely change in its structure?
A) The primary structure is altered. Q59. The following are characteristics of:
B) The secondary and tertiary structures are altered. 1. Lower the activation energy
C) The cofactor is removed. 2. Are specific
D) The active site becomes more flexible. 3. Remain unchanged
4. Are sensitive to pH and temperature
Q54. In the presence of a non-competitive 5. Are biocatalysts
inhibitor, what happens to the Vmax and Km of 6. Are mostly proteins
the enzyme? A) Vitamins
A) Vmax decreases, Km unchanged B) Hormones
B) Vmax unchanged, Km increases C) Enzymes
C) Vmax increases, Km decreases D) Antibodies
D) Vmax unchanged, Km decreases
Q60. If the substrate concentration is very low,
Q55. What is the role of HCl in the activation of what is the relationship between the rate of
pepsinogen to pepsin? reaction and substrate concentration?
A) It denatures the enzyme. A) The rate is independent of substrate
B) It removes an inhibitory polypeptide. concentration.
C) It acts as a cofactor. B) The rate is directly proportional to substrate
D) It changes the pH to optimal for activity. concentration.
C) The rate is inversely proportional to substrate
Q56. Why do enzymes have an optimal pH? concentration.
A) Because they are denatured at all other pH D) The rate is proportional to the square of substrate
values. concentration.
B) Because the ionization state of the active site
residues is optimal for catalysis. Q61. Which statements are true about enzyme
C) Because the substrate is only stable at that pH. inhibition?
D) Because the product is only formed at that pH. A. Competitive inhibition is reversible.
B. Non-competitive inhibition changes the enzyme's
Q57. Arrange the following in the sequence of shape.
events in feedback inhibition: C. Uncompetitive inhibition binds only to the ES
I. Accumulation of end product complex.
II. Binding of end product to the first enzyme D. Feedback inhibition is a type of competitive
III. Inhibition of the first enzyme inhibition.
IV. Shutdown of the pathway
A) I, II, III, IV Q62. Which are characteristics of coenzymes?
B) II, I, III, IV I. Organic molecules
C) I, III, II, IV II. Derived from vitamins
III. Permanently bound
MATS NEW STB BOOK LINE WORKSHEETS 2025-26 (MATS OWNERS 03252257223) Page 7
IV. Act as activators These are sites for which of the following?
A) I, II A. Enzyme synthesis
B) I, III B. Enzyme activity
C) II, IV C. Enzyme inhibition
D) I, II, IV D. Enzyme denaturation

Q63. [Refer to Fig 2.1: Lock and key model] In Q67. Match:
the diagram, what does the "Active site" Column I Column II
represent? 1. Oxidoreductase a. Transfer of
phosphate group
2. Transferase b. Conversion of
glucose-6-P to
fructose-6-P
3. Hydrolase c. Reduction of
ferredoxin
A) 1c, 2a, 3b
B) 1a, 2b, 3c
C) 1c, 2b, 3a
D) 1b, 2a, 3c

Q68. Which enzyme-class pair is correct?

A. Lyase: Breaks bonds without water
A. A rigid cavity B. Isomerase: Hydrolyzes peptides
B. A flexible pocket C. Ligase: Transfers electrons
C. A cofactor D. Hydrolase: Joins DNA strands
D. An inhibitor
Q69. Which enzyme-substrate pair is
Q64. Which statement about enzymes is MISMATCHED?
INCORRECT? A. Lactase: Lactose
A. Enzymes are not consumed in reactions. B. RNase: RNA
B. All enzymes have an optimal pH. C. ATPase: Proteins
C. Enzymes can catalyze both forward and reverse D. Maltase: Maltose
reactions.
D. Enzymes increase the free energy change of a Q70. Functions:
reaction. - Catalyzes condensation reactions
- Involved in DNA and RNA synthesis
Q65. What is the role of a cofactor in conjugated - Requires energy (ATP)
enzymes? - Forms covalent bonds
A. It provides structural stability. These describe which enzyme class?
B. It assists in substrate binding and catalysis. A. Ligase
C. It denatures the enzyme. B. Transferase
D. It acts as an inhibitor. C. Lyase
D. Oxidoreductase
Q66. Locations:
- Inside the cell Q71. Match:
- On the ribosomes Col I Col II
- In the mitochondrial matrix 1. Temperature effect a. Rate doubles per
- Bound to DNA 10°C rise

MATS NEW STB BOOK LINE WORKSHEETS 2025-26 (MATS OWNERS 03252257223) Page 8
2. pH effect b. Bell-shaped curve A. To bind any molecule in the cell.
3. Substrate c. Michaelis-Menten B. To ensure catalysis of only specific reactions.
concentration kinetics C. To increase the temperature of the reaction.
A) 1a, 2b, 3c D. To act as a storage site for products.
B) 1b, 2a, 3c
C) 1c, 2b, 3a Q77. Sequence in feedback inhibition:
D) 1a, 2c, 3b I. End product accumulates
II. Binds to allosteric site
Q72. In the induced fit model, what happens III. Conformational change in enzyme
after substrate binding? IV. Pathway shuts down
A. The enzyme becomes denatured. A) I, II, III, IV
B. The active site becomes rigid. B) II, I, IV, III
C. The enzyme changes shape for catalysis. C) III, II, I, IV
D. The product is immediately released. D) IV, I, II, III

Q73. Why is the lock and key model considered Q78. The binding site in the active site is
too simplistic? responsible for:
A. Enzymes can catalyze multiple substrates. A. Chemical transformation
B. Enzymes change conformation upon substrate B. Holding the substrate
binding. C. Releasing the product
C. Enzymes work only at optimal pH. D. Denaturing the enzyme
D. Enzymes require cofactors.
Q79. Features:
Q74. Which factor does NOT affect enzyme 1. Protein part
activity? 2. Inactive without cofactor
A. Light intensity 3. Can be activated
B. pH 4. E.g., Pepsinogen
C. Temperature 5. Converted to active form
D. Substrate concentration 6. Secreted in stomach
Describe:
Q75. An enzyme has maximum activity at pH 7. A. Apoenzyme
If the pH drops to 3, what occurs? B. Holoenzyme
A. Denaturation and permanent loss of function. C. Zymogen
B. Reversible inhibition. D. Coenzyme
C. Increased activation energy.
D. The enzyme becomes an allosteric activator. Q80. If an enzyme is saturated with substrate,
what limits the reaction rate?
Q76. Why do enzymes have a specific active site? A. Substrate concentration
B. Enzyme concentration
C. Product accumulation
D. Cofactor availability

Q81. Which are true about allosteric regulation?

A. Involves binding away from active site.
B. Can be activation or inhibition.
C. Causes conformational change.
D. Is irreversible.

MATS NEW STB BOOK LINE WORKSHEETS 2025-26 (MATS OWNERS 03252257223) Page 9
Q82. Which statements apply to ribozymes? C. Enzyme denaturation
I. Made of protein D. Enzyme storage
II. Catalyze genetic information processing
III. Discovered by Cech and Altman Q87. Match:
IV. Function only in bacteria Column I Column II
A) I, II 1. Competitive inhibition a. Binds ES complex
B) II, III 2. Non-competitive b. Binds active site
C) III, IV inhibition
D) I, IV 3. Uncompetitive c. Binds allosteric
inhibition site
Q83. [Fig 2.2: Induced fit model] What does the A) 1b, 2c, 3a
change in enzyme shape indicate? B) 1a, 2b, 3c
C) 1c, 2a, 3b
D) 1b, 2a, 3c

Q88. Correct match for enzyme and its function:

A. DNA polymerase: Breaks DNA
B. Amylase: Hydrolyzes starch
C. ATP synthase: Hydrolyzes ATP
D. Pepsin: Synthesizes proteins

Q89. MISMATCHED enzyme-class pair:

A. Denaturation A. Lactase: Hydrolase
B. Adaptation to substrate B. DNA ligase: Ligase
C. Inhibition C. Hexokinase: Oxidoreductase
D. Loss of function D. Phosphohexose isomerase: Isomerase

Q84. Which is INCORRECT about enzyme Q90. Functions:

classification? - Removes hydrogen
A. Hydrolases use water to break bonds. - Adds phosphate
B. Lyases remove groups without hydrolysis. - Rearranges atoms
C. Isomerases change molecular formulas. - Joins molecules with covalent bonds
D. Ligases break down macromolecules. These are functions of which enzyme classes?
A. Oxidoreductase, Transferase, Isomerase, Ligase
Q85. What best describes an enzyme? B. Hydrolase, Lyase, Isomerase, Transferase
A. A reactant in biochemical reactions. C. Ligase, Transferase, Lyase, Oxidoreductase
B. A biological catalyst that speeds up reactions. D. Transferase, Hydrolase, Ligase, Isomerase
C. A molecule that stores genetic information.
D. A structural component of cell membranes. Q91. Match:
1. Prosthetic group → a. Covalently bound
Q86. Locations: 2. Coenzyme → b. Vitamin-derived, detachable
- Cytoplasm 3. Activator → c. Metallic ion
- Nucleus A) 1a, 2b, 3c
- Endoplasmic reticulum B) 1b, 2a, 3c
- Golgi apparatus C) 1c, 2b, 3a
These are sites for which of the following? D) 1a, 2c, 3b
A. Enzyme synthesis
B. Enzyme inhibition

MATS NEW STB BOOK LINE WORKSHEETS 2025-26 (MATS OWNERS 03252257223) Page 10
Q92. What is the significance of enzyme A. Holds the substrate in place.
inhibition in drug discovery? B. Directly participates in bond breaking/forming.
A. Inhibitors can act as drugs to block pathogenic C. Releases the product.
enzymes. D. Binds allosteric inhibitors.
B. Inhibitors increase enzyme activity.
C. Drugs are always enzyme activators. Q99. Features:
D. Inhibition is irreversible in drugs. 1. Lowers activation energy
2. Does not change equilibrium
Q93. Why can't enzymes catalyze 3. Highly specific
thermodynamically unfavorable reactions? 4. Sensitive to temperature
A. They only lower activation energy. 5. Sensitive to pH
B. They alter the equilibrium constant. 6. Not consumed in reaction
C. They require cofactors. Describe:
D. They are denatured. A. Enzymes
B. Cofactors
Q94. In uncompetitive inhibition, increasing C. Substrates
substrate concentration: D. Inhibitors
A. Increases inhibition
B. Decreases inhibition Q100. Why is the induced fit model more
C. Has no effect accurate than lock and key for some enzymes?
D. Denatures enzyme A. Substrates are flexible.
B. Enzymes undergo conformational changes to
Q95. An enzyme shows maximum activity at catalyze reactions.
37°C and pH 7.4. What happens at 60°C and pH C. Active sites are rigid.
7.4? D. Inhibitors bind covalently.
A. Activity increases due to higher temperature.
B. Activity decreases due to denaturation.
C. Activity remains unchanged.
D. pH becomes optimal.

Q96. How do enzymes stabilize the transition

state?
A. By increasing activation energy.
B. By binding tightly to the transition state.
C. By releasing more energy.
D. By altering the reaction equilibrium.

Q97. Steps in enzyme action:

I. Formation of enzyme-substrate complex
II. Product formation
III. Substrate binding
IV. Product release
A) III, I, II, IV
B) I, III, II, IV
C) IV, II, I, III
D) II, I, IV, III

Q98. The catalytic site in an enzyme:

MATS NEW STB BOOK LINE WORKSHEETS 2025-26 (MATS OWNERS 03252257223) Page 11