UNIVERSITY INSTITUTE OF

SCIENCES
Academic Unit V
Bachelor of Engineering
(Computer Science & Engineering)
Biology For Engineers

Enzymes
 Enzymes
• Enzymes are biological catalysts that speed up
the rate of the biochemical reaction by lowering
activation energy.
• Catalyst are substances that increases the
velocity or rate of a chemical reaction without
itself undergoing any change in the overall
process.
• Macromolecular components composed of
proteins.
• Most enzymes are three dimensional globular
proteins (tertiary and quaternary structure)
Structure of enzyme
Banana: Amylases Cow, cattle's etc.: Trypsin, chymotrypsin
and Glucosidases
Pineapple: Bromelain

 Enzymes are pivotal in all living

entities which govern all the biological
processes.
Diastases; Amylases; Invertases;
 Enzymes are found in all tissues and Protease

fluids of the body, plant tissues and in

microorganism's.

 Enzymes have a high degree of

specificity for types of reaction
catalyzed and for their substrate. Bacteria and fungi
 Enzymes

• A large protein enzyme molecule is composed

of one or more amino acid chains called
polypeptide (polymer of amino acids) chains.
• The amino acid sequence determines the
characteristic folding patterns of the protein’s
structure, which is essential to enzyme
specificity.
 Enzymes as protein
Enzymes are a linear chain of amino acids, which give
rise to a three-dimensional structure.
 A Brief History of Enzymes..
• The term “Enzyme” was coined by
Friedrich Wilhelm Kuhne in 1878 to
designate biological catalysts.
• In 1897, Eduard Buchner named the
enzyme that brought the fermentation of
sucrose as ‘zymase’.
• He was awarded with noble prize (1907)
for his contribution towards biochemical
research and cell free fermentation.
• In 1926, James Summer established the
true nature of enzyme as protein.
• He crystallized urease from Jack-Bean In 1878, German
extracts, and in the next few years many Physiologist Wilhelm
Kuhne, first used the term
other enzymes were purified.
enzymes
• Therefore, enzyme are still a major
subject of academic research.
 Structure of enzyme
• All enzymes are globular proteins with the
exception of recently discovered RNA enzymes.
Some enzymes may additionally contain a non-
protein group.
• Accordingly there are two types of enzymes on
the basis of composition, simple and conjugate.
Simple Enzyme:
It is an enzyme which is wholly made up of protein.
Active site is formed by specific grouping of its own
amino acids. Additional substance or group is
absent, e.g., pepsin, trypsin, urease.
 Conjugate Enzyme:
• It is an enzyme which is formed of two parts— a
protein part called apoenzyme (e.g., flavoprotein)
and a nonprotein part named cofactor.
• The complete conjugate enzyme, consisting of an
apoenzyme and a cofactor, is called holoenzyme.
Active site is formed jointly by apoenzyme and
cofactor.
 Cofactor
• Co-factor -non protein molecule which carries
out chemical reactions that cannot be
performed by standard 20 amino acids
Cofactor is small, heat stable part of conjugate
enzyme.
• Co-factors are of two types:
Inorganic Cofactors
 Organic Cofactors
Inorganic Co-factors: These are the inorganic
molecules required for the proper activity of
enzymes.
Examples:
Carbonic anhydrase requires Zn2+ for its activity.
Hexokinase has co-factor Mg 2+
 Organic Co-factors: These are the organic molecules
required for the proper activity of enzymes.
Types of Organic Co-factors:
 Prosthetic Group: A prosthetic group is a tightly
bound organic cofactor.
Examples: Flavins, heme groups and biotin.
 Coenzyme: A coenzyme is loosely bound organic co-
factor. Example: NAD+
 Active site of enzymes
• Only a certain region of the enzyme, called
the active site, binds to the substrate.
• The reactant in biochemical reaction is termed as
substrate.
• Enzymes bind substrates to their active site and
stabilize the transition state of the reaction.
• The active site of the enzyme is the place where
the substrate binds and at which catalysis occurs.
• The active site binds the substrate, substrate,
forming an enzyme-substrate (ES) complex.
 The active site of the enzyme

• Active site can be further divided into:

 Binding site: It chooses the substrate and binds it to
active site.
 Catalytic site: It perform the catalytic action of the
enzyme.
Mechanism of enzyme action
 How enzyme lowers activation energy
• Activation energy is the minimum energy required
for the activation of atoms or molecules to
undergo a chemical transformation/reaction.
• The substrate binds to the active site of an enzyme
by multiple weak non-covalent interactions like
hydrophobic interactions, H-bonds, ionic
interactions or reversible covalent bonds.
• The free energy released in the formation of a
large number of weak interactions between the
enzyme and the substrate is termed binding
energy.
• The 'binding energy' released due to the
interactions between the enzyme and the
substrate lowers the activation energy.
 IUB Classification and Nomenclature of
enzymes
• According to the International Union of
Biochemists (I U B), each enzyme is preceded by
Enzyme commission (EC) number. The first
number in the series classifies this enzyme on
the basis of its mechanism.
•There are six groups of enzymes as per the
reaction that is being catalyzed. Therefore, all
enzymes are designated as “EC numbers”.
 Enzyme commission Numbers
• EC number is a 4 digit number for instance –
a.b.c.d. Here “a” is class, “b” is subclass, “c” is
sub-subclass and “d” is the sub-sub-subclass. The
“b” and “c” part of the EC number describes the
reaction, “d” differentiates between different
enzymes with similar function on the basis of the
actual substrate in the reaction.
• Example – EC number of Alcohol: NAD+
oxidoreductase is 1.1.1.1
 IUB Classification and Nomenclature
of enzymes
•Enzymes are generally named according to the
reaction they catalyze or by suffixing “ase”
after the name of substrate.
– (as in urease, which catalyzes the
breakdown of urea)
Classification/Types of enzymes on the
basis of reaction they catalyze
The six kinds of enzymes are:
• EC 1. Oxidoreductases
• EC 2. Transferases
• EC 3. Hydrolases
• EC 4. Lyases
• EC 5. Isomerases
• EC 6. Ligases
 EC 1. Oxidoreductases:
• Enzymes belonging to this class catalyzes biological
oxidation-reduction reaction in which one compound is
oxidized and another is reduced. In other words, they
take part in oxidation and reduction reactions or
transfer of electrons.
Examples are:
 Dehydrogenases
 Oxidases
 Oxygenases
 Oxidative deaminases
 Hydroxylases
 Peroxidases
 EC 2. Transferases

• These are enzymes that catalyze the transfer

of chemical groups such as alkyl, methyl,
carboxyl, aminoacyl, sulfate, aldehyde
ketone, glycosyl, phosphate group, etc. from
donor to acceptor. Examples are as follows
Aminotransferase
Kinases
Acetyl transferases
Glycosyl transferases
 EC 3. Hydrolases

• These include hydrolytic enzymes that split C-

O, C-N, C-C, and other bonds by the addition
of water. These includes
Esterases
Lipases
Glycosidases
 Peptidases
Phosphatases
 EC 4. Lyases
• These are the group of enzymes that catalyzes
the removal of specific groups from their
substrate and introduce double bonds.
• The same enzymes can add groups to the
double bonds. Important examples are
aldoses, decarboxylases, dehydratases,
aconitases, etc.
 EC 5. Isomerases
• The enzymes cause rearrangement of
molecular structure to effect isomeric
changes. They are of three types,
• isomerases
• Epimerases
• mutases
 EC 6. Ligases
They are also called synthetases which catalyze
the joining together of two molecules coupled
with the breakdown of phosphate bonds in ATP
or any nucleoside triphosphates. Examples
include synthetases, and carboxylase. etc.
 Enzyme Characteristics and Properties
• Enzymes speed up the reaction by lowering the
activation energy of the reaction.
• Their presence does not effect the nature and
properties of end product.
• They are highly specific in their action that is each
enzyme can catalyze one kind of substrate.
• Small amount of enzymes can accelerate chemical
reactions.
• Enzymes are sensitive to change in pH, temperature
and substrate concentration.
 APPLICATIONS OF ENZYMES
They are used in the chemical industry and
other industrial applications when extremely
specific catalysts are required. However,
enzymes in general are limited in the number of
reactions they have evolved to catalyze, and by
their lack of stability in organic solvents and at
high temperatures.
• In food processing, the enzymes used include
amylases from fungi and plants. These
enzymes are used in the production of sugars
from starch, such as in making high-fructose
corn syrup.
• In baking, they catalyze the breakdown of
starch in the flour to sugar. Yeast fermentation
of sugar produces the carbon dioxide that
raises the dough. Proteases are used by biscuit
manufacturers to lower the protein level of
flour.
• Trypsin is used to predigest baby foods.
• For the processing of fruit juices, cellulases
and pectinases are used to clarify fruit juices.
• Papain is used to tenderize meat for cooking.
• In the dairy industry, rennin, derived from the
stomachs of young ruminant animals (like
calves and lambs) is used to manufacture of
cheese, used to hydrolyze protein. Lipases are
implemented during the production of
Roquefort cheese to enhance the ripening of
the blue-mold cheese.
• Lactases are used to break down lactose to
glucose and galactose.
• In the production of biological detergents,
proteases, produced in an extracellular form from
bacteria, are used in pre-soak conditions and
direct liquid applications, helping with the
removal of protein stains from clothes. Other
enzymes are amylases, lipases, cellulase,
mannanases, pectinase etc.
• In molecular biology, restriction enzymes, DNA
ligase, and polymerases are used to manipulate
DNA in genetic engineering, important in
pharmacology, agriculture and medicine, and are
essential for restriction digestion and the
polymerase chain reaction. Molecular biology is
also important in forensic science.
• Submerged fermentation, a type of fermentation
is used for large scale manufacturing of enzymes
 Important topics
• Enzyme definition with structure
• Types of enzyme-on the basis of reaction they
catalyse(Classification) and on the basis of
Composition.
• Application of enzyme –Specially detergent
industry
Thanks
 References
• Tymoczko, Lubert Stryer, and Lubert Stryer; Biochemistry. New
York: W.H. Freeman, 2002. Print
• Nelson, D., and Cox, M.; Lehninger Principles of Biochemistry
(4th Ed.). W.H. Freeman and Company, New York, 2005.
• Rodwell. Harper's Illustrated Biochemistry. 27th ed. New York:
Lange Medical Books/McGraw-Hill, 2006.
• Harvey, Richard A., Ph. D. Lippincott's Illustrated Reviews:
Biochemistry. Philadelphia :Wolters Kluwer Health, 2011.
• Wikipedia