ASSIGNMENT ON ENZYMES

Instruction: In a one-whole sheet of yellow pad paper, copy the given question (excluding the figure/illustration) and
write your answer.

ANSWER AS DIRECTED

1. Identify the labeled parts of the illustration.

A ____________________
B ____________________
C ____________________
D ____________________

2. Suppose a reaction A + B  C + D is catalyzed with an enzyme. Refer to the illustration below and answer the
following questions:
a. Which of the lowercase letter labels (a, b, c, d or e)
represents the activation energy required for the
reaction without an enzyme?
b. Which of the lowercase letter labels (a, b, c, d or e)
represents the activation energy required for the
enzyme-catalyzed reaction? b
c. Which of the lowercase letter labels (a, b, c, d or e)
represents the G? d
d. True or False: Enzymes influence the kinetics but not the thermodynamics of a reaction?
e. True or False: affect the energetics of either the reactant/s or product/s?

3. In the first step of glycolysis, the glucose ring is phosphorylated. Phosphorylation is the  process of adding a
phosphate group to a molecule derived from ATP. The reaction is catalyzed using kinase which requires
magnesium ion. Refer to the following illustration. Assume that A is kinase and B is magnesium.
a. Magnesium ion is considered as ____.
magnesium cation, a divalent metal
cation and a monoatomic dication
b. When magnesium ion is bound to kinase as in “C”, the
enzyme is considered as ___.
c. Under the condition of magnesium deficiency, when the
enzyme may lack magnesium, it would be referred to as
the ____.

4. Classify the enzyme that catalyzes the given reactions (No need to write the reaction)

a.

b.

c.
 d.

e.

5. Differentiate the Induced Fit and Lock and Key theory of the mechanism of enzyme action.
- The lock and key model states that the active site of an enzyme precisely fits a specific substrate. The induced
fit model states that the active site of an enzyme will undergo a conformational change when binding a
substrate, to improve the fit.

6. Refer to the given illustration. Enumerate the

possible forces that draw the substrate into the
active site. Hint: The same forces maintain the
tertiary structure in the folding of peptide
chains.
-The tertiary structure is primarily due to
interactions between the R groups of the
amino acids that make up the protein.

7. What type of specificity is demonstrated by the following enzymes?

a. L-amino acid oxidase can only catalyze the oxidation of the L-form of an amino acid but not the D-form of
the same amino acid.
b. Phosphatases can hydrolyze phosphate-ester bonds in all types of phosphate esters.
c. Alcohol dehydrogenase can oxidize both ethanol and methanol to yield corresponding aldehydes
d. Aminopeptidase can only cleave amino acids, one at a time, from the amino end of a peptide chain.
e. Lactase can only hydrolyze the β-1-4 glycosidic bond of lactose to yield galactose and glucose.

8. The Michaelis-Menten model is the one of the simplest and best-known approaches to enzyme  kinetics. The
following illustration shows the Michaelis-Menten saturation curve.
a. Write the Michaelis-Menten
equation.
b. Which curve indicates that the
enzymes are saturated? (A or B)
c. What order of reaction is
demonstrated in A?

9. Enumerate the factors that affects enzyme’s activity.

Enzyme activity can be affected by a variety of factors, such as temperature, pH, and concentration. Enzymes
work best within specific temperature and pH ranges, and sub-optimal conditions can cause an enzyme to lose
its ability to bind to a substrate.
10. Which of the following illustrations demonstrates the following?

a. Competitive inhibition
b. Uncompetitive inhibition
c. Noncompetitive inhibition
11. Which of the following would NOT qualify as feedback inhibition?
A. An enzyme is inhibited by its own end product
B. The cell detects that there is too much of a substance in its cytoplasm, so it makes a chemical messenger to
inhibit the enzyme that’s making it.
C. The first enzyme in a biochemical pathway is inhibited by the end product of the last enzyme in the
pathway.