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PUC 1st Year Semester-2
Unit 10: Chemical constituents of living cells

Module 14: Enzymes- Classification, properties and action

One of the most important functions of proteins in living cells is to act as

enzymes.

“An enzyme may be defined as a complex biological catalyst that is

produced by a living organism in its cells to regulate the various physiological
processes of the body.”

The substance on which an enzyme acts is called the “substrate”. A catalyst

is any organic or inorganic substance that accelerates a chemical reaction without
affecting the end products of the reaction and without being destroyed in the
course of the reaction.

Enzymes are produced by living cells but can act independently of living
cells. Enzymes are biological catalysts which accelerate the rate of biochemical
reactions. They are effective in very small concentrations. They are unchanged by
the reaction. They exert their physiological effects by changing the rate at which
equilibrium is reached, not by changing the equilibrium of the reaction. Enzymes
only change the rate of the chemical reaction. In the absence of enzymes, the
chemical reaction proceeds very slowly. These, infact, lower the energy of
activation. Enzymes are highly specific because each enzyme usually catalyzes one
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particular kind of reaction. Each enzyme can combine with a specific substrate to
form enzyme -substrate complex. This is called substrate specificity. All enzymes
are proteins with large molecular weights having one or more active sites for the
binding of the substrate molecules. The enzyme proteins undergo denaturation
when the natural conditions are altered. This results in the loss of enzyme activity.

Classification:

According to International union of Biochemistry (IUB) , the present system

of classification of enzymes is based on their reaction specificity. Six classes have
been recognized.

1. Oxido reductases: These are the enzymes which catalyze biological

oxidations and reductions
The important subclasses are:
a. Dehydrogenases
b. Oxidases
c. Peroxidases
d. Oxygenases

2. Hydrolases: These enzymes are instrumental in the cleavage of complex

molecules in the presence of water. These fall into 3 categories.
a. Proteases: They attack the peptide bonds of proteins and peptides
b. Esterases: They catalyze hydrolysis of ester linkages
c. Carbohydrases: They hydrolyze the glycosidic linkages
3. Transferases: These are the enzymes that catalyze the transfer of a chemical
group from one molecule to another.
Ex. Transaminases, transphosphorylases etc
4. Lyases: These are a group of enzymes that reversibly catalyze the removal
of groups from substrates non hydrolytically. These enzymes act on C-C,
C-O,C-N,C-S and C-halide bonds. This group includes.
a. Hydrases (carbon-oxygen lyases)
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b. Aldehyde –lyases
c. Decarboxylases (remove Co2 from carboxylic acids)
5. Isomerases (or mutases): These include enzymes that catalyze reactions to
bring about intramolecular rearrangement of atoms in susbstrates. Ex. The
inter conversion of aldose and ketose sugars.

6. Ligases or synthetases:
These are the enzymes that catalyze the linking together of two
separate molecules in which pyrophosphate bond of ATP is broken down.
These enzymes catalyze reactions forming C-O,C-S,C-N and C-C bonds.
Thus X+Y+ATP X-Y+AMP+P-P (pyrophosphate)

Mechanism of enzyme action:

The enzyme promotes a given reaction, but, itself remains unchanged
at the end of the reaction. In 1913 Michaelis and Menten proposed that an
intermediate enzyme-substrate complex is formed during enzymatic
activity.
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Enzyme (E)+Substrate(S) Enzyme substrate complex (ES)

Enzyme +Products (P)

The enzyme itself remains almost passive. It merely provides a “platform”

on which certain molecules could react with each other. Such an enzyme –
platform brings reacting molecules into contact much faster than chance
collisions at that temperature. The result is that the reactions are
accelerated.
Enzymes being proteins molecules, have a definite surface
geometry. These have substrate specificity i.e, there is close structural
similarity between the molecular surface of enzyme and its substrates. In
other words, the functional groups of the enzyme and the substrate are
complementary. Therefore, only specific enzyme can combine with the
specific substrate to form the enzyme –substrate complex. Every enzyme is
supposed to have a definite sites in which specific substrate molecule with
complementary functional groups can fit in. This site is called the active site
or catalytic site of the enzyme.
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The mechanism of enzyme action has been explained by two

theories.
1. Lock and key theory of Emil Fischer and
2. Induced fit theory of Koshland.
1. Lock and key Theory (Rigid model of the catalytic site)
According to this model, the catalytic site of enzyme has a definite
shape where only specific shaped substrate molecules can fit in. just as
only particular shaped keys fit into particularly shaped locks. This
concept was developed to explain the great specificity of enzymes.
According to this concept, a structurally well defined catalytic site will

accept only those substrate molecules which have a matching shape and
will repel others that differ structurally. In other words, the catalytic site
of the enzymes by it self is complementary in shape to that of the
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substrate. This fitting results in the formation of enzyme substrate

complex which breaks down to give rise to products of the chemical
reaction and the enzyme is released for its subsequent use.
2. Induced Fit Theory (Flexible model of the catalytic site )
According to this model , the substrate induces a conformational
change in the enzyme. According to this model , the catalytic sites of
some enzymes are not rigid. In these enzymes, the shape of the catalytic
site is modified by the binding of substrate. The catalytic site has a shape
complementary to that of the substrate only after the substrate is
bound. This process of dynamic recognition is called induced fit. It brings
amino acid residues or other groups on the enzyme in the correct spatial
orientation for substrate binding, catalysis or both.

Co enzymes and co-factors:

Coenzymes are small molecules which enhances the action of
an enzyme. They cannot by themselves catalyze a reaction but they can
help enzymes to do so.
Some enzymes like pepsin and trypsin are made up entirely of
protein (simple enzymes), but many others have two parts –a protein
part called the apoenzyme and a non protein part, called the cofactor
(conjugated enzymes). The combination of the two can be referred to as
the holoenzyme.
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Apoenzym+cofactor Holoenzyme (Active enzyme)

Thus, only when apoenzyme and cofactor are present together, catalysis
will occur. Neither of the two can produce catalytic action by it self. The
cofactor may be either a metal ion (ex. Ca,Mg,Zn, Co etc) or some times
a non protein organic compound.
If the cofactor is firmly bound to the apoenzyme, it is called
prosthetic group. If, instead of being more or less permanently bound to
the apoenzyme the cofactor attaches itself to the apoenzyme only at the
time of reaction, it is called a coenzyme.
Based on the above finding “co enzyme may be defined as a
particular kind of co-factor ,i.e a non protein organic compound or a
carrier molecule functioning in conjunction with a particular enzyme”
Coenzymes geberally act as acceptors or donors of a functional
group. Types of reactions that frequently require the participation of
co- enzymes are oxido reductions, group transfer, isomerization
reactions and reactions resulting in the formation of covalent bonds.
The majority of co enzymes are chemical derivatives of the
nucleotides. In most co enzymes, the nitrogen base portion of
nucleotides is replaced by another chemical unit. This unit is usually a
derivative of a B-vitamin
Isozymes: An enzyme which has multiple molecular forms in the
same organism catalyzing the same reaction is ca``lled isozymes or iso
enzymes. For instance, lactic dehydrogenase (LDH) exists in five different
forms (isozymes) in the tissues of rat. These different forms have been
found to catalyze the same overall reaction. The enzyme lactic
dehydrogenase has two different types of polypeptide chains designated
as M and H chains. The lactate dihydrogenase present in muscles has M
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polypeptide chains where as the one predominating in heart has H

polypeptide chains. The total four polypeptide chain present in lactate
dehydrogenase in different combinations form five different molecular
forms of it. Generally, isozymes of closeby related species show greater
similarity than those of distant species. Thus isozymes provide a basic
clue to the genetic inter relationships of organisms.

Questions
1. What are enzymes? Describe the classification of enzymes
2. Discuss the mechanism of enzyme action
3. Write notes on –Coenzymes and Isozymes.