ENZYMES-MOLECULAR

DEVICES THAT
DETERMINES THE
COURSE OF CHEMICAL
REACTIONS

C.NAVEEN PRABAKARAN,
ASSISTANT PROFESSOR, DEPARTMENT OF BIOCHEMISTRY,
INTERNATIONAL EDUCATION COLLEGE,
JIANGXI UNIVERSITY OF TCM,
WANLI, NANCHANG,
PEOPLES REPUBLIC OF CHINA
 INTRODUCTION
BIOCATALYST
SYNTHESISED BY THE LIVING
CELL
CARRIES OUT CHEMICAL
TRANSFORMATIONS IN LIVING
ORGANISMS
POSSESS VERY HIGH CATLYTIC
EFFICIENCY AND SPECIFICITY
 CHEMICAL NATURE OF
ENZYMES
Most of the Enzymes are Proteins.
There are few exceptions such as
Ribozymes (RNAs that acts as enzymes)
They may be of Simple proteins and
Conjugated Proteins
Some may contain a single polypeptide
chain-Monomeric Enzymes
Some may contain more than one
polypeptide-Oligomeric Enzymes
Few enzymes exists as complexes-
Multienzyme Complex
SOME TERMINOLOGIES
SUBSTRATE: Substances on which enzyme
acts to convert them into products.
APO-ENZYME: Protein part of the enzyme.
CO-ENZYME: Low molecular weight, heat
stable organic compounds required for
enzyme activity.
HOLO-ENZYME = APO-ENZYME +
CO-ENZYME
 CO-ENZYMES
Low molecular weight, heat stable, non-
protein organic compounds
Binds covalently or non-covalently to apo
enzyme
They are derived from Physiologically
active forms from the constituents of
Vitamin B-Complex
Ex: Pantothenic Acid: CoASH, Vit B12:
Cobamide, Folic Acid: THF, Niacin: NAD,
NADP, Riboflavin: FMN,FAD etc
 CO-FACTORS (OR) METAL
IONS
Apart from Co-enzymes some enzymes may
require metal ions for their activation
Such enzymes are called metal activated
Enzymes
Ex: K+, Mg++, Ca++, Zn++, Cu++
There is another group of enzymes is present
and it is called metallo -enzymes
The difference between metal activated enzyme
and metallo enzyme is in the former the metal
ions can be removed from the enzymes whereas
in the later, the metal ions got tightly bound to
the enzyme
CATALYTIC EFFICIENCY
Unlike Chemical Catalyst Enzymes
are highly efficient in carrying out
chemical transformations.
It can able to accelerate the
reactions by many folds
It carries out such transformations
by reducing the activation energy.
 Contd..
Before a chemical reaction can occur,
the reacting molecules are required to
gain a minimum amount of energy, this
is called the Energy of Activation or
Activation Energy.
In normal chemical reaction this can be
achieved by increasing the temperature
But in human body which maintains a
normal temperature fairly constant, it
is achieved by enzymes.
 SPECIFICITY
They are of three types

Stereochemical Specificity

Reaction Specificity and

Substrate Specificity
 Contd..
Stereochemical Specificity: There can be many optical
isomers for a substrate but enzymes can only one
particular isomer

Reaction Specificity: A substrate can undergo many

reaction but all the reactions cannot be catalysed by
single enzyme

Bond Specificity: Enzymes that can act on specific

bonds such as glycosidic, peptide bonds follows bond
specificity

Substrate Specificity: There are two types

A) Absolute Specificity and
B) Relative Specificity
 NOMENCLATURE AND
CLASSIFICATION
ENZYMES ARE GENERALLY
NAMED BY ADDING THE SUFFIX
ASE TO THE NAME OF THE
SUBSTRATE
EXAMPLE: Enzymes that acts on
nucleic acids are called as Nucleases
There are exceptions such as
trypsin, chymotrypsin and pepsin
 Contd..
The IUB classified enzyme based on their
specific function.
Enzyme are classified in mainly into 6 main
classes.
They are
1.Oxidoreductase
2.Transferase
3.Hydrolase
4.Lyases
5.Isomerase
6.Ligases
 OXIDOREDUCTASES
These are enzyme which catalyse oxidation and
Reduction reaction between two substrate.
These are further classified into three types.
Dehydrogenases.
Oxidases.
Oxygenases.
 Contd..
DEHYDROGENASE
Removal of hydrogen from one substrate
OXIDASES
Removal of hydrogen from substrate and
pass it directly to oxygen.
OXYGENASES
Incorporation of oxygen directly into
substrate
 Contd..
TRANSFERASES
These are enzymes that can transfer a
group from one substrate to another
substrate.
HYDROLASES
These are enzymes which catalyses the
hydrolysis of groups by the direct
addition of H2O molecules, which is to
be cleaved.
 Contd..
LYASES
These are enzyme which catalyses the removal
of groups from substrate cleaving double band.
ISOMERASES
Interconversions of optical and geometrical
isomers by intramolecular rearrangement of
atoms.
LIGASES
These are enzyme which catalyses the linking
of two compounds.
 EC CODE
Each Enzyme possess a specific code number
assigned by the Enzyme Commission and the IUB
It comprises of four numbers separated by points,
Eg. 1.1.1.1
The first number indicates the main class
The second number indicates the type of group
involved in the reaction
The third number denotes the reaction more
precisely indicating the substrate on which it acts
The fourth digit is the serial number of the
enzyme
 MECHANISM OF ENZYME
ACTION
Usually, an enzyme catalyzes just
one type of reaction for one specific
substance known as a substrate.
An enzyme recognizes and binds to a
substrate because the tertiary (or
quaternary) structure of the enzyme
complements the structure of the
substrate.
 Contd..
E + S= ES
enzyme substrate enzyme-substrate
complex

active site is the part of the enzyme

that binds the substrate and where
catalysis occurs.
The reaction of the substrate is
catalyzed within the enzyme-substrate
complex.
 At the active site, bonds of the
substrate are broken and new bonds
are formed to yield a product.

Because the shape of the product is

different than that of the substrate,
the molecules of the product detach
from the enzyme.

The active site on the enzyme is

available again to bind and catalyze
the reaction of another substrate
molecule.
 The overall enzyme-catalyzed
reaction can be written as:

E + S E-S E
+ P
 PROPOSED MODELS FOR
ENZYME ACTION
LOCK AND KEY MODEL

The enzyme has a pocket that fits the

shape of a specific substrate formed by
the side groups of a few of the amino
acids in the protein.
Because the substrate fits into the active
site like a key fits into a particular lock it
is known as the lock-and-key model.
The lock-and-key model assumes the
active site is a rigid geometric structure.
 Contd..
INDUCED- FIT MODEL

In the induced-fit model of an

enzyme the active site is flexible.

This allows it to accommodate the

shapes of several different
substrates.