UNIVERSITI TUNKU ABDUL RAHMAN

CENTRE FOR FOUNDATION STUDIES

FOUNDATION IN SCIENCE
MAY 2016
FHSC1214
FUNDAMENTALS OF CELL BIOLOGY
TUTORIAL 5
ENZYME II

Students Guide for Tutorial:

At university level, the tutor facilitates student learning without spoon-feeding. Therefore,
you are expected to:
Read your textbook, attempt the questions before the tutorial
You may enter the class and sign your attendance after showing your tutor that all

tutorial questions have been completed; even if you dont know how to do, write
something - youre not advised to leave answers blank in the finals.
Write answers on board if you wish to receive tutor feedback
(no answer, no feedback)
Be independent: consult textbooks or dictionaries on your own first before asking the
tutor
All questions are compulsory. 1 mark may reflect 1 answer point.
(No half mark is awarded in the finals marks)

[Source: Final Examination for April 2016]

Q1. (a)
Figure 1 shows the effects of increasing substrate concentration on the rate of
an enzyme-catalyzed reaction at a temperature of 35C at a constant pH.

Figure 1
Answer the following questions based on Figure 1.
(i)

Describe the effects of varying substrate concentration on the rate of

the enzyme-catalyzed reaction.
(2 marks)

(ii)

Explain the following scenarios.

(iii)

(A)

An increase in substrate concentration at low substrate

concentration increases the rate of reaction
(2 marks)

(B)

An increase in substrate concentration at high substrate

concentration does not increase the rate of reaction (2 marks)

State ONE (1) way to increase the rate of reaction at high substrate
concentration.
(1 mark)

(iv)

Explain the following observations.

(A)

At a substrate concentration of 0.7 mol dm-3, an equal volume of

competitive inhibitor at a concentration of 0.05 mol dm-3 is
added. The rate of reaction remains the same.
(2 marks)

(B)

At a substrate concentration of 0.7 mol dm-3, an equal volume of

non-competitive inhibitor at a concentration of 0.05 mol dm-3 is
added. The rate of reaction is decreased dramatically.
(2 marks)

[Source: Final Examination for December 2015]

Q2. (a)
Figure 2 shows the binding of substrate (S) to enzyme (E) under the influence
of two inibitors (I).

Figure 2
Answer the following questions based on Figure 2.
(i)

Specify the type of inhibitors for reaction P, Q, R and S, respectively.

Give reasons for your answers.
(4 marks)

(ii)

Describe the effects of inhibitors toward the enzyme.

3

(2 marks)

(iii)

(b)

Suggest a way to overcome the inhibition in reaction Q.

(1 mark)

Hydrogen peroxide is not a stable compound and it decomposed into water

and oxygen as shown in the equation below:
2H2O2

2H2O + O2

If a catalyst is added, the decomposition can be sped up. A student investigated

the activity of enzyme catalase by counting the numbers of bubbles formed.
The apparatus is shown in Figure 3.

Figure 3
Answer the following questions based on Figure 3.
(i)

Explain the result you would obtain if catalase was first incubated in a
water bath at 80C for an hour before added into hydrogen peroxide.
(5 marks)

(ii)

Apart from counting the bubbles, suggest another method to measure

the activity of the enzyme.
(1 mark)

(iii)

Suggest ONE (1) possible source of catalase.

(1 mark)

(c)

Based on Figure 4, explain feedback inhibition. State the importance of

feedback inhibition in a cell.
(6 marks)

Figure 4

[Source: Final Examination for April 2015]

Q3.
(a)
Angiotensin-converting enzyme (ACE) increases blood pressure by converting
angiotensin I to angiotensin II which constricts the blood vessels. Enalapril is
a drug that functions as ACE inhibitor and is used to treat high blood pressure
patients. Figure 5 shows the effect of enalapril on the rate of ACE-catalysed
reaction with different concentration of angiotension I.

Figure 5

Based on Figure 5, answer the following questions.

(i)

Identify the type of inhibitor for enalapril. Justify your answer.

(3 marks)

(ii)

Explain how enalapril reduces high blood pressure.

(iii)

The optimum pH for ACE enzyme is 8.3. Describe the effects of acidic
condition on ACE-catalysed reaction without the presence of enalapril.
(5 marks)

(2 marks)

[Source: Final Examination for September 2014]

Q4.
(a)
The enzyme tyrosine kinase (TK) in found in human cells. TK can exist in a
non-functional and a functional form. The functional form of TK is only
produced when a phosphate group is added to TK, as shown in Figure 6.

Figure 6

Based on Figure 6, answer the following questions.

(i)

Phosphorylation of non-functional form of TK enzyme would produce

the functional form of TK. Explain how.
(2 marks)

(ii)

Binding of the functional form of TK enzyme to its substrate leads to

cell division. Chronic myeloid leukemia is a cancer that involves
uncontrolled cell division caused by a faulty form of TK. Figure 7
illustrates the faulty form of TK.

Figure 7
Suggest how faulty TK leads to chronic myeloid leukemia.

(iii)

(2 marks)

Imatinib is a drug used to treat chronic myeloid leukemia. Figure 8

shows how imatinib inhibits faulty TK enzyme.

Figure 8
Based on Figure 8, describe how imatinib stops the development of
chronic myeloid leukemia.
(2 marks)