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Natalie Pemberton-Parris 00027917

20th November 2014

CHEM 121 Enzymes Worksheet (37 marks)


1. State the function of an enzyme.
Enzymes speed up reactions or increase the rate of reactions.

(1 mark)

2. Most enzymes are proteins, but some enzymes are RNA ribozymes

(1 mark)

3. The names of enzymes normally end in the suffix ase

(1 mark)

4. Transferase are enzymes that catalyze reactions that involve transfer of C, N or P-containing groups. (1
mark)
5. Lyases are enzymes that catalyze reactions that involve cleavage of C-C, C-S and C-N bonds. (1 mark)
6. Describe the active site of an enzyme.
(2 marks)
The active site is the portion of enzyme on which the substrate attaches and the catalyzed reaction occurs.
Its a special cleft containing amino acid side chains which are complementary to a specific substrate.
When an enzyme interacts with its substrate, an enzyme-substrate (ES) complex is formed. ES is converted
to EP (enzyme-product complex) which then dissociates to enzyme (E) and product (P).
7. Write an equation to illustrate the enzyme-catalyzed conversion of a substrate to a product. (1 mark)
E + S ES -> EP -> E + P

8. Briefly explain the difference between the lock and key mechanism and the induced fit mechanism.
(2marks)
In the lock-and-key model, the enzyme is assumed to be the lock and the substrate the key
The enzyme and substrate are made to fit exactly. In the induced-fit model, the enzyme action assumes that
the enzyme active site is more a flexible pocket whose conformation changes to accommodate the substrate
molecule.
9. Briefly explain what is meant by the transition state.
(2marks)
The transition state favors the conversion of substrate product. Before Glucose-6-phosphate (the
reactant) can be converted into Glucose-1-phosphate (the product), Glucose-6-phosphate is converted into
an intermediate form where bonds are in the process of being broken and rearranged and reformed.
10. What is the activation energy (in terms of the substrate and the transition state)?
(2 marks)
Activation energy is when the reactants gain sufficient energy to reach the transition state in order to be
changed into products.
11. How is activation energy different between catalyzed and un-catalyzed reactions?
(1marks)
The uncatalyzed reaction has a large activation energy. In the catalyzed reaction, the activation energy has
been lowered significantly increasing the rate of the reaction. Catalyzed reactions have a lower activation
energy (rate-limiting free energy of activation) than the corresponding uncatalyzed reaction, resulting in a
higher reaction rate at the same temperature.

SECTION B. (22 marks)


12. State two ways in which the rate of an enzyme catalyzed reaction can be measured.

(2 marks)

1. Measure the number of product molecules formed per unit time (e.g. moles product formed per
minute).
2. Measure the number of substrate molecules converted to product per unit time (e.g. moles of substrate
used per minute.
13. Describe how and why substrate concentration affects rate of an enzyme-catalyzed reaction. (4 marks)
As the concentration of substrate increases, the rate of reaction also increases until the point saturation
occurs. It means as you increase the concentration, rate keeps increasing and then one point comes when
the maximum rate is achieved and there is no free enzyme to bind with substrate and all the active sites of
enzyme are bound to the substrate. So after that point, increasing the concentration wont have any effect.
14. Describe how and why temperature affects rate of an enzyme-catalyzed reaction.
(4 marks)
Increasing in temperature increases the rate of reaction. As you increase the rate of temperature the rate of
reaction also increase until a maximum rate is obtained because more molecules have sufficient energy to
reach the transition state. If the reaction is increased above 37 degrees the rate will decrease as the protein
denatures.
15. Describe how and why pH affects rate of an enzyme-catalyzed reaction.
(4 marks)
Each enzyme works best at an optimum pH. (For most enzymes that pH is 7.4) A change of pH away from
the optimum pH results in the rate of the reaction decreasing. This is because enzymes and substrate have
specific chemical groups in an ionized or unionized state in order to interact; it may prevent the substrate
from binding properly to the enzymes active site. It causes denaturation of the enzyme because of changes
in the ionic state of the amino acid side chains.
16. Explain the principle by which enzymes can be used to detect diseases and disorders.
(2 marks)
Damaged tissues can be detected by abnormally elevated plasma levels of enzymes which are normally
present in the cells of those tissues and are specific to those tissues.
17. What are Isoenzymes?
(2 marks)
Isoenzymes are enzymes that catalyze identical chemical reactions but are composed of different amino
acid sequences. They are sometimes referred to as isozymes. Isoenzymes are produced by different genes
and are not redundant despite their similar functions. They occur in many tissues throughout the body and
are important for different developmental and metabolic processes.
18. List two factors which can denature a protein.
(2 marks)
1. Heating, which disrupts the secondary and tertiary structure of the protein.
2. Changes in pH that interfere with ionic bonding between amino-acid side chains.
3. Detergents, which make nonpolar amino-acid side chains soluble and thereby destroy the hydrophobic
interactions that give rise to the tertiary and quaternary structure of the protein.
19. Explain why prolonged high fever in the body can be fatal.
(2 marks)
At extreme temperatures proteins in the body unfold or "denature. Our normal bodily temperature is
perfect for chemical reactions to occur. Enzymes are chemical catalysts which speed up reactions and are
made of proteins-- so excessively high body temperatures could denature these and cause them to no longer
function properly. As a result, it prohibits your proteins from functioning normal and vital chemical
reactions can no longer work in your body.

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