CHAPTER 4 : BIOCATALYSIS

PART A : STRUCTRED QUESTIONS

4.1 Properties of Enzymes and Mechanism of Actions

PSPM PDT SEM III 2016/2017

1. FIGURE 1 shows the curves for enzymatic reaction.

FIGURE 1

a) State the nature of inhibition for curves P,Q and R. [3 marks]

P: no/without inhibition
Q: Competitive inhibition
R: Non-competitive inhibition

b) Briefly explain the enzyme activities for curves Q and R. [4 marks]

Q: competitive inhibitor and substrate compete for the same active site of enzyme.
Maximum rate of reaction reached when more substrate added.
R: non-competitive inhibitor and substrate bind to different site on enzymes/allosteric sites Rate of
reaction decrease.

c) Which curves shows an inhibition that could not recovered by the addition of more substrate. [ 1 mark]
Curve R

d) Digestion of lipid occurs in the small intestine and is catalysed by lipase. Briefly explain the consequences of eating
oranges to the disgestion of lipid in the small intestine. [2 marks]
Lipase need alkaline medium// orange create acidic medium in the small intestine Lipase is not
active/slows down the digestion/hydrolysis of lipid.

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 PSPM PDT SEM III 2017/2018

2. FIGURE 2 shows an enzyme and a substrate action mechanism.

FIGURE 2

(a ) Name the hypothesis of the mechanism in FIGURE 2.

[1 mark]
Induced fit mechanism

(b) Describe the events that occur when the substrate bind to the active site of enzyme. [3 marks]
The binding of the substrate induces the enzyme to change its shape slightly
This leads a better fit between the active site and the substrate
There is also a slightly alteration to the shape of the substrate.

(c) How does enzymes affect the activation energy of a reaction? [1 mark]
Enzyme lowers the activation energy

(d) What happens to the rate of reaction at the highest substrate concentration. [ 1 mark]
The rate of reaction become constant

(e) State two (2) types of reversible inhibition [2marks]

Competitive
Non-competitive

(f) Give one (1) example of inhibition for each type of reversible inhibition. [2marks]
Non-competitive inhibitor: ATP/isoleucine/cyanide
Competitive inhibitor: malonic acid/malonate

PSPM PDT 3 2018/2019

3. FIGURE 3 shows the effect of two different chemicals on the activity of Enzyme A. The temperature, pH and enzyme
concentration were kept constant during this experiment.

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 FIGURE 3

(a) Explain the effect of chemical B and C on the activity of enzyme A. [4 marks]
Chemical B compete for the active site of the enzyme.
Chemical B reduce/decreasing/slow the enzymatic rate of reaction.
The enzyme’s rate of reaction reaches the maximum rate of reaction.
[ANY 2]
Chemical C binds to the allosteric site of the enzyme.
] Chemical C reduce/decrease/slow the enzymatic rate of reaction.
The enzyme’s rate of reaction does not reach the maximum rate of reaction.
[ANY 2]

(b) Based on the experiment, what is chemical B and C?. [2marks]

Chemical B : Competitive inhibitor
Chemical C : Non competitive inhibitor

(c) Give one example of each: [2marks]

Chemical B : Malonate/ATP
Chemical C : Cyanide/heavy metal ions/nerve gases/isoleusine
Does increasing the concentration of substrate overcome the effect of chemical B
(d) towards activity of enzyme A? Why?. [2marks]
Yes.
The probability of an enzyme substrate collision is higher//the subsrates have greater chance of binding to the
active site.

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PSPM SDS SB025 2019/2020

4 (a) State two (2) characteristics of enzyme. [2 marks]

- All enzymes are globular protein.
- Function is lowering the activation energy.
- Highly specific in action.
- Not altered at the end of reaction.
- Required in small amount to catalyze the reaction.
- Reaction is extremely efficient.
- May catalyze the reversible reaction.
- Enzyme can be denatured by extreme pH/high temperature.

Any two- 2 marks

(b) Illustrate the induced fit model of an enzyme. [3 marks]

Correct enzyme and substrate structure – 1 Mark

Correct enzyme substrate complex – 1 Mark
Correct label – 1 Mark

(c) Explain the mechanism of enzyme based on the induced fit model. [2 marks]
- The binding of the substrate induces the active site of an enzyme to change its shape slightly
- Allowing the substrate to fit precisely into the active site // the active site becomes fully
complementary with the substrate/reactant.
- Reaction takes place/ catalyzed the product/ products formed/ released.
- Enzyme change back to original comformation
- Enzyme can be used for next reaction/reusable
- any 2 : 2 Marks

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 PSPM 2020/2021 SDS SB015

5. FIGURE 4 shows an enzyme reaction.

FIGURE 4

a. Which graph shows the presence of enzyme? [1 mark]

● (Graph)
B

(b) (i) Name the enzyme that involved in 3(a) [1 mark]

● Maltase

(ii) Describe how the enzyme in 3(b)(i) breaks down maltose into glucose based on the induced-fit model

i. Maltose/substrate binds to activate site of maltase/enzyme

ii. The binding induces a (slight) change in the shape/conformation of the activate site//
iii. The activate site becomes (fully) complementary with maltose/substrate
iv. Forming an enzyme-substrate complex (R: E-S-C)
v. Two (a-)glucose formed/released.

PSPM 2020/2021 SDS SB015

6 (a) State the three (3) properties of enzymes.

i. (Most enzyme are globular) protein
ii. Required in small amount / quantity / low concentration
iii. Not altered at the end of reaction / reusable
iv. (Highly) specific
v. Reversible (catalyst)
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 vi. Affected by temperature and pH// Denatured at high temperature and extreme pH

b. How do enzymes speed up the rate of reactions?

● By lowering the activation energy

c. Explain the mechanism of enzyme action based on Induced Fit Model.

i. The active site of the enzyme is flexible// Active site of the enzyme are not exactly
complementary// not exactly compatible to the substrate
ii. When the substrate bind to the active site of enzyme
iii. (This induce) the slight changes of confirmation/ shape of the active site/ enzyme
iv. Allowing the substrate fit precisely/ fully complementary to the active site
of the enzyme / accurately
v. forming an enzyme - substrate complex
vi. The reaction has occurred/ Enzyme can carried out its catalytic function//
Enzyme - substrate complex broken down
vii. Product is formed / produced / released
viii. Enzyme / Active site changes back to its original conformation/ shape

7. FIGURE 7 show mechanism of enzyme action.

FIGURE 7
(a) Identify X and Y. [2 marks]
X: Enzyme
Y: Substrate

(b) Name the model of exzyme action mechanism shown in FIGURE 7. [1 mark]
Induced Fit Model

(c) Explain the mechanism of enzyme action in 3 (b). [6 marks]

i. The active site of an enzyme is flexible/not fully/exactly complementary/compatible/similar to the
shape/conformation of substrate.
ii. Enzyme collides/in contact with the substrate molecule.
iii. The substrate binds to the active site (of the enzyme)
iv. To form enzyme-substrate complex.
v. The binding (induce) a slight change in the conformation of active site of the enzyme//active site of the enzyme
changes its conformation/shape.1
vi. Active site become fully/exactly complementary to the substrate//substrate fits precisely to the active site of
enzyme
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vii. Enable the enzyme to carry out their catalytic function/catalytic reaction take place/occur
viii. Product is formed/released
ix. Active site of enzyme changes back to its original conformation/shape

4.3 Inhibitors

PSPM SDS SB015 2018/2019

7. FIGURE 3 shows two different types of inhibitors, X and Y when compared to normal enzyme

(a) Identify X and Y [2 marks]

X : Competitive (inhibitor)
Y : Non-competitive ( inhibitor)

(b) Give one (1) example of Y [1 mark]

Heavy metal/ toxins/ poisons/ lead/ DDT/ mercury/ paraquat/ cyanide/ nerve gas/ isoleucine

(c) Differentiate the structure of X and Y [2 marks]

X : Resemble / similar/ slightly same to the substrate
Y : Have different structure / shape as the substrates

(c) How can the activity of enzyme X and Y be optimized? [2 marks]

X : By increasing the concentration of substrate
Y : By removing the inhibitor // decrease the concentration of inhibitor

PART B : ESSAY QUESTIONS

4.1 Porperties of Enzymes and Mechanism of Actions

8. (a) International Union of Biochemistry (IUB) has set a standard that requires enzyme naming to consist both the
substrate acted upon and the type of reaction catalysed. Describe enzyme classification and function according
to IUB. [12 marks]

i. Oxidoreductase
ii. Catalyse redox reaction/biological oxidation and reduction
iii. By the transfer of hydrogen , oxygen or electrons from one molecule to another.
iv. Example: glucose oxidase / malate dehydrogenese/ NADH dehydrogenase/ dehydrogenase
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 v. Hydrolases
Catalyse the hydrolysis of substrate//breakdown of substrate by the addition of water
vi. Example: Lipase /amylase /sucrose/peptidase
vii. Transferases
viii. Catalyse the transfer of functional group of atoms from one molecule to another
ix. Example:Glycogen phosphorylase/ hexokinase/ phosphotransferase/ transaminase
x. Isomerases
xi. Catalyses the rearrangement of atoms within a molecule by converting one isomer to another//isomerization
xii. Example: phosphoglucoisomerase
xiii. Lyases
xiv. Catalyses the breaking of chemical bonds without the addition of water//group elimination to form double
bond
xv. Example:(pyruvate) decarboxylase
xvi. Ligases
xvii. Catalyses reactions in which new chemical bonds are formed and uses ATP as energy source xix. Example:
Aminoacyl-tRNA synthase/DNA ligase

7. a) With the aid of a diagram, explain activation energy in energy in relation to the function of enzyme.
[10M]

4.2 Co-Factor
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 ( b) Describe the characteristic for two (2) types of cofactors. State the role for each. [8 marks]

Prosthetic group
Non-protein
Bind tightly on a permanent basis
Role: involve in the catalytic function of the enzyme

Coenzyme
Non protein organic molecule
Bind loosely /temporary
Derivative of vitamin especially group B vitamins / NADH, NADPH and FADH2 Role: Detach
and help to transfer chemical group,atoms or electron

Metal ion/ enzyme activator Non

protein inorganic ions.
E.g. Mg2+ , Fe2+ , Ca2+ , Zn2+ and Cl- .
Attach temporarily to the enzyme
Role: change enzyme active site to make the shape more suitable for reaction to take place/ bind the enzyme and
substrate together