XI – BIOLOGY 1 Chapter: 3

CHAPTER # 3
ENZYMES
Short Question and Answers
Q. Define enzymes and describe their characteristics.

The term enzyme was first used by a scientist named Friedrich Wilhelm Kuhune in 1878 he defined
as:
“Enzymes are the organic substances capable of catalyzing specific chemical
reactions in the living system”.

CHARACTERISTICS OF ENZYME

 These are produced in the cell and act inside or outside the cell as organic biocatalyst.
 Enzymes are large molecules of proteins but may contain non protein molecules.
 They can react with both acidic and alkaline substances.
 They act in a small quantity to bring about change in large amount of substrate.
 Enzymes are specific in their action and react with particular substrate in particular pH.
 Their activities can be accelerated by certain ions like Mg, Ni, and Mn etc. called activators.
 Enzymes are heat sensitive and are called ‘Thermo labile’.

Q. What are ribozymes?

During 1980’s Thomas Czech and Sidney Altman discovered that certain molecules of
ribonucleic acid also function as enzymes. These are called “ribozymes” which catalyze reactions
involved in processing genetic information to be used by the cell. Generally enzymes are
protienecios in nature.

Q. Write a note on energy of Activation.

ENERGY OF ACTIVATION
Definition: “It is the energy required for the formation of chemical complex by the reactants”.

The enzymes react with the energy rich and energy poor molecules which form an intermediate
complex which break into product and enzyme. If activation energy of formation of this complex is
low many molecules can react and participate in reaction. In this way activation energy is lowered
by the enzyme but in this action equilibrium (ratio of concentration of reactant and product) is
remains same.

Q. Describe the theories of enzyme action.

In order to explain the mode of action of enzymes two theories has been given importance which are as
follows.

KEY-LOCK THEORY

Fischer (1898) proposed this theory and later improved by Paul filder and D.D. Woods. They said;
“An enzyme act on a particular substrate like particular lock can be unlocked by a particular key”.

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XI – BIOLOGY 2 Chapter: 3

This theory depends upon physical contact between substrate and enzyme and the groove of
specific shape of enzyme is called ‘active site’.

INDUCE FIT MODEL

Koshland (1959) proposed this theory and stated that;

“When a substrate combined with an enzyme it induces changes in the enzyme structure and
performs its catalytic activity more effectively”.

Q. Describe the types of enzymes.

SIMPLE ENZYME: Enzyme contains only protein.

CONJUGATED ENZYME: Enzyme contains another group other then protein. Euler (1932) also
named conjugated enzyme as ‘Holoenzyme’.
HOLOENZYME: It contains two parts, the protein part called ‘apoenzyme’ and non
protein part called ‘prosthetic group’.

TYPES OF HOLOENZYME: On the basis of the nature of prosthetic group, conjugated enzymes or
holoenzymes are of two types;

1. Co-factors: The holoenzymes in which prosthetic group is inorganic ion. These inorganic
ions are known as Co-factors like Mg, Ca, and K etc.
2. Co-enzymes; The holoenzymes in which prosthetic group is an organic ion.
These organic prosthetic groups are called Co-enzymes like NAD,
NADPH, FMN, ATP etc.

Q. How the concentration of substrate effect enzyme action.

The rate of reaction increases with an increase of amount of substrate until the available enzyme
becomes saturated with the substrate. Very high concentration of substrate exerts a retarding
effect upon enzyme action and further increase of substrate has no effect on the rate of reaction.

Q. What is the effect of temperature on enzyme activity?

Enzymes are heat sensitive and lost their activity at high temperature and destroyed. The optimum
temperature for most of the enzyme is 30 to 37 degree centigrade at 100 degree they destroyed
and at 0 degree they become inactive but not destroyed.

Q. What are co-enzymes, activators and inhibitors?

Co-factors have been divided into three categories.

Co-Enzymes: If the co-factor is an organic molecule , its is called co-enzyme without coenzyme
certain enzyme are unable to function e.g. NAD,FAD etc.
Activators: Enzyme activity enhance in the presence of inorganic substances which are called
activators e.g. Mg, Zn etc.
Inhibitors: Substances which decreases the activity of an enzyme are called inhibitors e.g. DDT
and parathion are inhibitors of key enzymes in nervous system.

Q. Write a note on competitive and Non-Competitive inhibitors.

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XI – BIOLOGY 3 Chapter: 3

Competitive Inhibitors
These resemble with the substrate molecule and block the active site of enzyme for the entrance of
substrate molecule.

Non-Competitive Inhibitors
These bind with the enzyme away from the active site which is called ‘allosteric site’ this cause the
change in enzyme shape and active site hence causing the active site unreceptive to substrate.

Q. What do we mean by Feed-back inhibition?

Feed-back Inhibition
When end product in abundance it attached with the enzyme active site it is called feed back
inhibition. This reduces the inhibition and as a result more products is formed but if it is bind with
the allosteric site no more product is formed.

Descriptive questions
Q. Describe the factors affecting enzyme activities.

Following factors affect the enzyme activity:

 CONCENTRATION OF SUBSTRATE

The rate of reaction increases with an increase of amount of substrate until the available enzyme
becomes saturated with the substrate. Very high concentration of substrate exerts a retarding
effect upon enzyme action and further increase of substrate has no effect on the rate of reaction.

 TEMPERATURE

Enzymes are heat sensitive and lost their activity at high temperature and destroyed. The optimum
temperature for most of the enzyme is 30 to 37 degree centigrade at 100 degree they destroyed
and at 0 degree they become inactive but not destroyed.

 WATER

Water is essential for the rate of enzymatic activity. In germinating seeds amount of water increase
the activity of enzyme to precede germination.

 RADIATION

Enzymes are generally inactivated rapidly by exposure to ultraviolet light and also to Beta, Gamma
and X rays.

 Co-ENZYMES, ACTIVATORS AND INHIBITORS

Co-factors have been divided into three categories.

1. Co-Enzymes: If the co-factor is an organic molecule , its is called co-enzyme without enzyme
certain enzyme are unable to function e.g. NAD,FAD etc.

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XI – BIOLOGY 4 Chapter: 3

2. Activators: Enzyme activity enhance in the presence of inorganic substances which are
called activators e.g. Mg, Zn etc.
3. Inhibitors: Substances which decreases the activity of an enzyme are called inhibitors
e.g. DDT and parathion are inhibitors of key enzymes in nervous system.

(a) Competitive Inhibitors

These resemble with the substrate molecule and block the active site of enzyme for
the entrance of substrate molecule.

(b) Non-Competitive Inhibitors

These bind with the enzyme away from the active site which is called ‘allosteric site’
this cause the change in enzyme shape and active site hence causing the active site
unreceptive to substrate.

(c) Feed-back Inhibition

When end product in abundance it attached with the enzyme active site it is called
feed back inhibition. This reduces the inhibition and as a result more products is
formed but if it is bind with the allosteric site no more product is formed.

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