1. Which of the following best defines an enzyme?

A) A small molecule that increases the activation energy of reactions.

B) A type of lipid that speeds up metabolic reactions.
C) A protein that acts as a biological catalyst to lower activation energy.
D) A carbohydrate that serves as a source of energy for reactions. Answer C

2. What happens to enzymes during a catalysis reaction?

A) Enzymes are permanently altered and consumed in the reaction.

B) Enzymes remain unchanged after the reaction and can be reused.
C) Enzymes only interact with one type of substrate before breaking down.
D) Enzymes are denatured and no longer functional after catalyzing a reaction.

Answer B

3. Which of the following best describes the denaturation of enzymes?

A) The process of breaking non-covalent bonds, distorting the enzyme’s shape and active site
B) The process by which enzymes become more soluble in water, enhancing their activity.
C) The breaking of covalent bonds in enzymes, altering their active site.
D) The ability of enzymes to catalyze reactions at an optimal pH and temperature.
Answer A

4. Enzyme specificity refers to the enzyme's:

A) Ability to catalyze reactions in both forward and reverse directions.

B) Restrictiveness in choosing substrates, with some enzymes acting only on specific substrates.
C) Regulation by activators and inhibitors to control the rate of reaction.
D) Sensitivity to changes in temperature and pH.
Answer B

5. Based on the chemical properties of enzymes, which of the following statements best
describes the role of reversibility in enzymatic reactions during metabolism?

A) Enzyme reversibility enables enzymes to act exclusively on anabolic pathways, building new
molecules and inhibiting catabolic pathways.
B) Reversibility of enzymes allows them to alter the molecular structure of substrates
permanently, ensuring that the product is not reversible.
C) Enzyme reversibility limits the reactions to one direction, ensuring that metabolic processes
are more efficient and less energy-consuming.
D) The reversibility of enzymatic reactions ensures that enzymes can catalyze both anabolic and
catabolic reactions, thus maintaining metabolic balance in both directions.
Answer D

6. Which of the following best explains the molecular mechanism behind the colloidal nature of
enzymes, as described in the text?

A) The large molecular size and high molecular weight of enzymes prevent them from diffusing
through semipermeable membranes, resulting in colloidal suspension.
B) The high solubility of enzymes in solvents leads to their inability to aggregate into colloidal
particles.
C) The formation of ionic bonds between enzyme molecules causes them to form aggregates that
pass through semipermeable membranes.
D) The enzyme’s denaturation at high temperatures leads to the formation of colloidal particles
due to protein aggregation.
Answer A

7. A student is conducting an experiment to test the activity of the enzyme amylase, which
breaks down starch into sugars, under different conditions. The student conducts four tests as
described below:

Test 1: The student maintains the pH of the solution at 5, which is considered optimal for
amylase activity. The enzyme breaks down the starch rapidly, and after testing for starch, the
result shows no starch remaining.

Test 2: The student adjusts the pH to 9, which is higher than the optimal pH. The enzyme breaks
down the starch, but more slowly than in Test 1. The starch test shows that some starch is still
present.

Test 3: The student lowers the temperature to 20°C. The enzyme breaks down the starch very
slowly, and the starch test shows a moderate amount of starch still present.

Test 4: The student increases the temperature to 60°C, which is significantly higher than the
normal working temperature of the enzyme. No breakdown of starch occurs, and the starch test
shows a large amount of starch still present.

Based on the results of the student's experiment, which of the following conclusions is correct?

A) The amylase enzyme works best at high temperatures and high pH levels.
B) The enzyme is most active at 20°C and pH 9, as shown by the faster starch breakdown.
C) The enzyme is most active at pH 5, with slower activity at pH 9, and high temperatures
(60°C) denature the enzyme.
D) Temperature has no effect on enzyme activity, and pH 9 is optimal for starch breakdown in all
cases.
Answer C

8. In an experiment, a student adds lactase to a solution containing lactose. Over time, the
concentration of lactose decreases, and the solution contains glucose and galactose. Based on the
text, what can be concluded about the role of lactase in the digestion of lactose?

A) Lactase converts lactose into glucose and galactose by hydrolyzing the glycosidic bond
between them.
B) Lactase breaks down glucose and galactose into their respective monosaccharides by
dehydration synthesis.
C) Lactase directly catalyzes the conversion of lactose into fats and proteins.
D) Lactase prevents the hydrolysis of lactose and maintains it in the disaccharide form.
Answer A

9. Which of the following enzymes is involved in the breakdown of nucleic acids?

A) Helicase
B) DNA polymerase
C) Amylase
D) Lipase
Answer A

10. Which of the following enzymes is correctly matched to its function, considering its role in
both physiological processes and its interaction with specific substrates?

A) Acetylcholinesterase – Hydrolyzes the neurotransmitter acetylcholine into choline and acetic

acid, thereby terminating nerve signal transmission at synaptic junctions.
B) DNA polymerase – Catalyzes the elongation of the DNA strand by adding nucleotides to the
3' end of the growing strand, ensuring the accurate replication of DNA during cell division.
C) Trypsin – Catalyzes the breakdown of disaccharides like lactose into monosaccharides like
glucose and galactose in the small intestine.
D) Maltase – Catalyzes the hydrolysis of starch into glucose by cleaving the glycosidic bonds
between glucose units in starch molecules.
answer A
11. Which of the following best explains why a protein must maintain its three-dimensional
structure to function as an enzyme?

A) The three-dimensional structure of a protein stabilizes its primary sequence of amino acids,
which is critical for enzyme function.
B) The three-dimensional structure of a protein enables it to fold into specific shapes that allow
the active site to bind substrates efficiently.
C) A protein's tertiary structure is irrelevant to enzyme activity; it only affects the protein's
primary sequence.
D) The three-dimensional structure is only necessary for structural proteins and does not affect
the activity of enzymes.
Answer B

12. How do the structure and function of a protein relate to its role as an enzyme?

A) The function of an enzyme is determined by its tertiary structure, which dictates how the
enzyme interacts with its substrate at the active site.
B) The protein's function as an enzyme is determined solely by its primary structure, as enzymes
cannot work without a linear amino acid sequence.
C) The secondary structure of a protein determines its catalytic activity, while the quaternary
structure is irrelevant to enzymatic function.
D) The protein's function is independent of its tertiary structure, as the enzyme's active site can
form spontaneously without structural constraints.
answer A

13. Which of the following statements best describes the relationship between enzymes and
proteins?

A) All enzymes are proteins, but not all proteins are enzymes.
B) Enzymes are a type of protein that do not have a specific sequence of amino acids.
C) Enzymes are proteins that can function as catalysts only at extremely high temperatures.
D) Enzymes are proteins, but their function as catalysts is independent of their amino acid
sequence. Answer A

14. In the context of enzyme-substrate interaction, which of the following best describes the role
of the transition state theory in understanding enzyme catalysis?

A) The transition state theory suggests that enzymes stabilize the substrate, decreasing the
activation energy but does not affect the energy of the transition state.
B) The transition state theory is not relevant to enzyme catalysis, as it focuses only on the final
products of the reaction.
C) The transition state theory assumes that enzymes lower the activation energy by providing an
alternative reaction pathway with a higher energy transition state.
D) The transition state theory proposes that enzymes work by binding the transition state of the
substrate more strongly than the substrate itself, thus lowering activation energy.
Answer D

15. Which of the following statements about the induced fit model of enzyme-substrate binding
is most consistent with the observed effects of allosteric inhibitors?

A) The induced fit model predicts that allosteric inhibitors will change the shape of the active
site and reduce its ability to catalyze reactions.
B) According to the induced fit model, allosteric inhibitors bind to the active site and directly
block substrate binding.
C) The induced fit model suggests that allosteric inhibitors stabilize the transition state, thus
enhancing the enzyme's catalytic efficiency.
D) The induced fit model implies that allosteric inhibitors will bind to an alternate site on the
enzyme, causing a conformational change that affects the active site’s ability to bind the
substrate.
Answer D

16. In comparing the lock and key model to the induced fit model, which of the following is most
likely to be true when considering the specificity of enzyme-substrate interactions?

A) The lock and key model allows for higher specificity in enzyme-substrate interactions, as the
enzyme’s active site is rigid and does not change shape.
B) The induced fit model leads to less specificity in enzyme-substrate interactions because the
enzyme's active site can change shape, allowing binding to a broader range of substrates.
C) The induced fit model allows for higher specificity in enzyme-substrate interactions because
it stabilizes the transition state by promoting a precise molecular fit after substrate binding.
D) The lock and key model and the induced fit model both allow for the same level of specificity
in enzyme-substrate interactions, as both models rely on perfect shape complementarity.
Answer C

17. Which of the following would most likely cause a reduction in enzyme activity in both the
lock and key model and the induced fit model?

A) Increasing substrate concentration without affecting the enzyme’s active site.

B) The introduction of competitive inhibitors that mimic the substrate structure.
C) Increasing the temperature to above the enzyme’s optimal level, causing denaturation of the
active site.
D) Providing excess cofactor molecules, increasing the enzyme's substrate affinity.
Answer C

18. In the induced fit model of enzyme catalysis, what is the primary role of the enzyme’s active
site after substrate binding?

A) The active site changes shape to strain the substrate’s bonds, making it easier for the reaction
to proceed by lowering the transition state energy.
B) The active site remains unchanged after substrate binding, providing a stable environment for
the substrate to undergo the reaction.
C) The active site undergoes a conformational change to prevent the release of the product,
ensuring the reaction is irreversible.
D) The active site acts only as a binding platform, with no significant change in shape to
facilitate the reaction process.
Answer A

19. A research team is investigating the activity of a newly discovered enzyme involved in
breaking down a specific protein in the human body. After conducting several experiments, they
observe the following results:

When the enzyme is incubated with its substrate, it forms an enzyme-substrate complex that
immediately undergoes a conformational change, bringing the enzyme's active site closer to the
substrate's transition state.
The enzyme's active site appears to adjust its shape slightly once the substrate binds, suggesting
a flexible interaction between the enzyme and the substrate.
Inhibitors that resemble the transition state are shown to significantly decrease the enzyme's
activity, but they do not completely block the enzyme from catalyzing the reaction.
What can be concluded about the enzyme’s mechanism, and which enzyme-substrate binding
model best explains these observations?

A) The enzyme likely uses the lock and key model, where the enzyme's active site is rigid and
requires a perfect fit for the substrate to bind and form a stable transition state.
B) The enzyme appears to use the induced fit model, where the active site undergoes a
conformational change upon substrate binding, facilitating the reaction by stabilizing the
transition state.
C) The enzyme likely follows the random collision model, where enzyme-substrate interactions
occur solely due to chance without any specific binding or conformational change.
D) The enzyme uses the allosteric regulation model, where a substrate binding at one site
changes the conformation of the enzyme at another site, regulating its activity.
Answer B

20. In an experimental setup, a new enzyme is isolated from a microorganism that thrives in
extreme heat. The following observations are made during the study:

The enzyme is highly efficient at temperatures significantly higher than most other enzymes,
which are typically denatured at these levels.
The enzyme exhibits the ability to adapt its shape slightly after binding to its substrate, with its
active site transitioning to a more catalytically active form.
A specific inhibitor, which mimics the enzyme’s transition state, competes with the substrate for
binding at the enzyme's active site, reducing the enzyme’s activity but not entirely inhibiting it.
Based on these findings, which enzyme-substrate model is most likely to be operating, and what
role does the enzyme's stability at high temperatures play in its function?

A) The enzyme follows the lock and key model, where the enzyme's rigid active site prevents it
from adapting to environmental changes, allowing it to function efficiently at high temperatures.
B) The enzyme adheres to the allosteric model, where temperature shifts alter the enzyme’s
conformation to activate its catalytic function, independent of substrate binding.
C) The enzyme functions through the cooperative binding model, where multiple active sites
cooperate in substrate binding, enhancing the overall enzyme activity at higher temperatures.
D) The enzyme follows the induced fit model, with its active site adjusting to accommodate the
substrate and stabilizing the transition state, explaining its high temperature tolerance and
catalytic efficiency.
Answer D