Tutorial FD Biochem (Enzymes)

TUTORIAL UniKL ID: .....................
FOUNDATION BIOCHEMISTRY (RMP00104)
1. Choose CORRECT statement regarding enzyme.

A Do not require activation energy.
B Do not change requirement of activation energy.
C Increase requirement of activation energy.
D Lowest requirement of activation energy.
2. Which of the following explains the increase in the rate of reaction at the beginning of an
enzymatic reaction when the substrate concentration is increased?
A More substrates bind to the enzyme.
B An increase in the movement of enzymes.
C The active sites of the enzymes are saturated.
D The affinity of the enzyme towards the substrate is higher.
3. Which of the following is a coenzyme?

A Magnesium.
B Vitamin B6.
C Iodine.
D Heme.
Penicillin blocks the formation of bacterial cell wall by mimicking substrate for the
4.
enzyme transpeptidase. Identify the role of penicillin.
A Non-competitive inhibitor.
B Competitive inhibitor.
C Enzyme activator.
D Coenzymes.
5. What happens to the rate of an enzyme-catalysed reaction if all its active sites are fully
saturated with substrate?
A The reaction stops.
B The rate of reaction decreases.
C The rate of reaction increases.
D The rate of reaction reaches the maximum value.
6.
The most likely result of mixing both enzymes with their substrates in a single test tube
is that
A Only gastric protease would be active if the pH of the mixture was basic.
B Intestinal protease would be more active than gastric protease at pH 4.
C Both enzymes would exhibit some activity at pH 5.
D Gastric protease would be more active than intestinal protease at pH 6.
7. Meat tenderizer contains an enzyme that interacts with meat. If meat is coated with
tenderizer and then placed in a refrigerator for a short time, how would the enzyme be
affected?
A It would be broken down.
B Its activity would slow down.
C Its shape would change.
D It would no longer act as an enzyme.
8. The graph below shows the effect of substrate concentration on the rate of enzyme
activity.
Select action that can be used to increase the rate of reaction beyond point P.
A Increase the enzyme concentration.
B Decrease the enzyme concentration.
C Increase the amount of substrate.
D Decrease the temperature.
9. In feedback inhibition, a metabolic pathway is switch off by

A A rise in temperature.
B Lack of a substrate.
C Accumulation of the end product.
D Competitive inhibition.
10. The rate of reaction of hexokinase during the phosphorylation of glucose to glucose 6-
phosphate decreases as the concentration of magnesium ions is reduced. What is the

role of the magnesium ions?
A Non-competitive inhibitor.
B Competitive inhibitor.
C Enzyme activator.
D Coenzymes.
11. Zinc is an essential trace element. It is present in the active site of the enzyme
carboxypeptidase. Which of the following is the function of zinc?
A As a coenzyme derived from a vitamin.
B As an allosteric activator of the enzyme.
C As a non-competitive inhibitor of the enzyme.
D As a cofactor necessary for enzyme activity.
12. A small non-protein organic molecule that binds tightly on a permanent basis to the
protein part of an enzyme is known as a
A Coenzyme.
B Prosthetic group.
C Non-competitive inhibitor.
D Activator.
13. One of the enzymes involved in glycolysis, aldolase, requires Zn 2+ for catalysis. Under
conditions of zinc deficiency, when the enzyme may lack zinc, it would be referred to as
the
A Holoenzyme.
B Prosthetic group.
C Apoenzyme.
D Coenzyme.
14. Zymogen is a
A Modulator
B Vitamin
C Enzyme precursor
D Hormone
15. These enzymes catalyze the transfer of atom or group between two molecules.
A transferases
B oxidoreductases
C isomerases
D ligases
1. State the differences between lock and key model and induced fit model of enzyme
mechanism.
Lock and key model Induced fit model
Active site
Mechanism
2.
pH 3 pH 8
Hyaluronidase is being extracted from Staphylococcus aureus. Then it is placed in the

solutions as above to observe the enzymatic reactions. Explain the effect of the different pH
on the rate of reactions of hyaluronidase.
3. Relate the rate of reaction with enzymes concentration.
4. The diagram below shows an enzyme and three different substrates, P, Q and R.
i. Based on the diagram above, choose the substrate that will be acted upon by the
enzyme.
ii. Explain your answer in 3 i.
5. Relate the negative allosterism in feedback inhibition.

6.
Pyruvate kinase catalyzes the last step of glycolysis which is important for

generating adenosine triphosphate (ATP). Addition of phosphate group to pyruvate kinase
decrease the rate of reaction of this enzyme. Briefly explain the regulation of this enzyme in
generating more ATP.

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TUTORIAL UniKL ID: .....................

FOUNDATION BIOCHEMISTRY (RMP00104)

1. Choose CORRECT statement regarding enzyme.

3. Which of the following is a coenzyme?

9. In feedback inhibition, a metabolic pathway is switch off by

phosphate decreases as the concentration of magnesium ions is reduced. What is the

Hyaluronidase is being extracted from Staphylococcus aureus. Then it is placed in the

3. Relate the rate of reaction with enzymes concentration.

5. Relate the negative allosterism in feedback inhibition.

Pyruvate kinase catalyzes the last step of glycolysis which is important for

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