TOPIC : BIOCATALYSIS

PART A : MULTIPLE CHOICE QUESTIONS

1. What are the factors that affecting the enzyme activity?

I. pH
II. temperature
III. presence of inhibitor

A. I only
B. I and II only
C. II and II only
D. I,II and III

2. What is the difference between the lock and key hypothesis and the induced fit
hypothesis?
A. The configuration of the active site
B. The composition of the enzyme
C. The type of substrate
D. The type of products formed

3. A competitive inhibitor
I. Has a similar structure to the normal substrate molecule
II. Can fit into the active site of the enzyme
III. Binds to the allosteric site

A. I only
B. I and II only
C. II and III only
D. 1, II and III

4. Which of the following is true about coenzymes?

I. Most are derived from the vitamin B group
II. Do not have any prosthetic groups
III. Are tightly bound to the enzyme

A. I only
B. I and II only
C. II and III only
D. 1, II and III
 5. Enzymes which catalyse oxidation processes include
A. Lipase
B. Dehydrogenase
C. Amylase
D. Peptidase

PART B : STRUCTURED QUESTIONS

1. FIGURE 2 shows the effect of increasing substrate concentration on the rate of a

particular reaction in the present and absent of inhibitor
Without inhibitor
A

With competitive inhibitor

Rate of reaction With non-competitive inhibitor

B

Substrate concentration
FIGURE 2

i. How do graph A and B differ?

[1 mark]
The rate of reaction in graph A is higher than graph B

ii. Explain the difference that stated in 1(i)

[2 marks]
-In graph A, the active site remain active so enzyme can bind with substrate
-Whereas in the graph B, the inhibitor binds to the allosteric site and alters
the active site making the enzyme not able to bind with the substrate
anymore.

iii. On FIGURE 2,draw labeled curve to show the effect on the rate of the enzyme
catalyzed reaction of the addition of competitive inhibitor

[2 marks]
 iv. Explain the effect of a competitive inhibitor on the rate of enzyme activity
[3 marks]
-A competitive inhibitor may have a molecular structure similar to the
substrate that allows it to combine with the enzyme’s active site.
-Therefore, it competes with substrate for the active sites of enzymes by
binding itself to an active site so that it prevents the substrate from
occupying it.
-this will reduce the rate of reaction as the substrate can only bind with those
enzyme not yet bound with the inhibitor and it takes longer for the products
to be formed.

v. Explain briefly about irreversible inhibitor in relation to enzyme structure and

activity.
[2 marks]
-Irreversible inhibitor will bind permanently to the enzyme and destroy the
enzyme
-Permenantly inhibit the enzymatic activity

PART C : ESSAY QUESTION

1. a) Briefly explain the types of inhibitors

[3 marks]
No Answer scheme Mark
1. Inhibitors are divided into two types, reversible inhibitor and 1
irreversible inhibitor
2. Reversible inhibitor is the inhibitor that form weak chemical 1
bond with enzyme
3. Irreversible inhibitor is the inhibitor that permanently 1
inactivates or destroys the enzyme
b) Distinguish between competitive and non-competitive inhibition of enzymes.
[7 marks]

No. Answer scheme Mark

1. Competitive and non-competitive inhibition of enzymes are 1
both reversible.
2. The effect of these inhibitors is temporary and no permanent 1
damage occurs to the enzyme
3. Competitive inhibitors will compete for the active site of the 2
enzyme whereas the non- competitive inhibitors do not
compete with the substrate for the active site
4. Competitive inhibitors bind to the active site of the enzyme 2
whereas the non-competitive inhibitors bind to the allosteric
site of the enzyme
5. The structure of the competitive inhibitor similar to the 2
structure of the substrate whereas the structure of the non-
competitive inhibitor is not similar to the substrate
6. If the substrate concentration is increased, it can reduce the 1
effect of competitive inhibitor because there will be greater
chance for the substrate to find the actives sites
7. whereas for non-competitive inhibitor, if the substrate 1
concentration is increased it will not reduce the effect o the
inhibitor because inhibitor attach to the allosteric parts of the
enzyme
TOTAL 10
MAX 7