Pineapple contains bromelain, which can digest

collagen protein.
What are enzymes?
• Enzymes are protein molecules which combine selectively
with and acts specifically upon another molecule called a
substrate.
 Enzyme Composition
■ Almost all enzymes are composed of
proteins

■ Exception: ribozyme

▪ RNA that catalyze reactions on other

RNA
What are some characteristics
of enzymes?
 CHARACTERISTICS
Enzymes speed up a reaction.

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.
What do enzymes look like?
STRUCTURE
OF ENZYMES ▪ The active site of an enzyme is the
region that binds substrates, co-factors
and prosthetic groups and contains
residue that helps to hold the substrate.

▪ Active sites generally occupy less than

5% of the total surface area of enzyme.

▪ Active site has a specific shape due to

tertiary structure of protein.
 SUBSTRATE
� The reactant in biochemical reactions is termed as substrate.

� When a substrate binds to an enzyme it forms an enzyme-substrate

complex.
ACTIVE SITE

o Active site can be further divided into:

Active Site

Binding Site Catalytic Site

It chooses the substrate It performs the catalytic

and binds it to active site. action of enzyme.

Enzyme Types
■ Simple enzyme: composed only of protein component
■ Complex enzyme: an enzyme that requires a cofactor to
function in addition to its protein component
▪ Apoenzyme: Inactive form of the enzyme because it is
missing the cofactor
▪ Holoenzyme: Active form of the enzyme; with cofactor
 Types of Cofactors
■ Inorganic: metal ions
▪ Most common: Zn+, Fe+, Cu+

■ Organic: usually from vitamins or their derivatives

▪ Prosthetic group: covalently / permanently bonded to an
apoenzyme (heme)
▪ Coenzyme: non-covalently / reversibly bound to an apoenzyme
(e.g. NADH)
Where are enzymes synthesized?
 SITES OF ENZYME SYNTHESIS

▪ Enzymes are synthesized by ribosomes

which are attached to the rough
endoplasmic reticulum.

▪ Information for the synthesis of enzymes

are carried by DNA.

▪ Amino acids are bonded together to form

specific enzymes according to the
DNA's codes.
 INTRACELLULAR AND EXTRACELLULAR ENZYMES

Intracellular enzymes are synthesized and retained in the cell for the use of cell itself.
They are found in the cytoplasm, nucleus, mitochondria and chloroplast.

Example :
▪ Oxydoreductase catalyzes biological oxidation.
▪ Enzymes involved in reduction in the mitochondria.

Extracellular enzymes are synthesized in the cell but are

secreted from the cell to work externally.

Example :
⮚ Digestive enzymes produced by the pancreas, are not used
by the cells in the pancreas but are transported to the
duodenum.
How are enzymes named?
 NOMENCLATURE OF ENZYMES

o An enzyme is named according to the name of the substrate it catalyses.

o Some enzymes were named before a systematic way of naming
enzymes was formed.
Example: pepsin, trypsin and rennin

o By adding suffix -ase at the end of the name of the substrate, enzymes are
named.
o Enzyme for catalyzing the hydrolysis is termed as hydrolase.

Example :
maltose + water glucose + glucose
maltase
EXAMPLES:
Substrate Enzymes Products

lactose lactase glucose + galactose

maltose maltase Glucose

cellulose cellulase Glucose

lipid lipase Glycerol + fatty acid

starch amylase Maltose

protein protease Peptides + polypeptide

CLASSIFICATION OF ENZYMES
� A systematic classification of enzymes has been
developed by the International Enzyme Commission.

� This classification is based on the type of reactions

catalyzed by enzymes.

� There are six major classes.

� Each class is further divided into sub classes, sub sub-

classes and so on, to describe the huge number of
different enzyme-catalyzed reactions.
 ENZYME CLASS REACTION TYPE EXAMPLES

Oxidoreductases Reduction-oxidation (redox) Lactate

dehydrogenase
Transferases Move chemical groups Hexokinase
Hydrolases Hydrolysis; bond cleavage with transfer of Lysozyme
functional group of water

Lysases Non-hydrolytic bond cleavage Fumarase

Isomerases Intramolecular group transfer Triose phosphate

(isomerization) isomerase

Ligases Synthesis of new covalent bond between RNA polymerase

substrates, using ATP hydrolysis
Oxidoreductases
These are enzymes that catalyze the transfer of electrons from one
molecule (the oxidant, the hydrogen or the electron donor) to another
molecule (the reductant, the hydrogen or electron acceptor).
Transferases
• Transfer of a functional group from one substance to another.
The group may be methyl-, amino- or phosphate group
AB + C → A + BC
Hydrolases
• These catalyze the hydrolysis of their substrates by adding
constituents of water across the bond they split
Lysases
Non-hydrolytic addition or removal of groups from substrates.
C-C, C-N, C-O or C-S bonds may be cleaved.
Isomerases

• Intramolecule rearrangement, i.e. isomerization changes within

a single molecule.
Ligases
• Join together two molecules by synthesis of new C-O, C-S, C-N or C-C bonds
with simultaneous breakdown of ATP.
What factors do you think affect
enzyme activity?
FACTORS AFFECTING ENZYME ACTIVITY
MECHANISM OF ENZYME ACTION
 THERMODYNAMIC CHANGES
Enzymes provide an alternate pathway for conversion
of substrate into products.

Enzymes accelerate reaction rates by forming

transitional state having low activation energy.

The reaction rate is increased many folds in the

presence of enzymes.
 COVALENT CATALYSIS

o Covalent catalysis involves the formation of a covalent bond between the

enzyme and at least one of the substrates involved in the reaction.
o Enzyme is released unaltered after completion of reaction.
 CATALYSIS BY PROXIMITY
In this catalysis, molecules must come in bond forming distance.

When enzyme binds:

⮚ A region of high substrate concentration is produced at the active site.

⮚ This will orient substrate molecules especially in a position ideal for them.
 CATALYSIS BY BOND STRAIN
● The enzyme-substrate binding causes reorientation of the structure of
site due to a strain condition.
● In this way bond between substrate is broken and converted into
products.
LOCK AND KEY MODEL

● Proposed by EMIL FISCHER in

1894.
● Lock and key hypothesis assumes
the active site of enzymes are rigid
in shape.
● There is no change in the active
site before and after a chemical
reaction.
INDUCED FIT MODEL

According to this, exposure of an enzyme

to substrate cause a change in enzyme,
which causes the active site to change its
shape to allow enzyme and substrate to
bind.
What is meant by enzyme
inhibition?
INHIBITION
• The prevention of an enzyme process as a
result of interaction of inhibitors with the
enzyme.
⮚ INHIBITORS:

Any substance that can diminish the velocity

of an enzyme catalyzed reaction is called an
inhibitor.
Types of Inhibition Inhibition

Reversible Irreversible

Competitive Uncompetitive Mixed Non-

competitive
REVERSIBLE INHIBITION
o It is an inhibition of enzyme activity in which the inhibiting molecular
entity can associate and dissociate from the protein's binding site.

TYPES OF REVERSIBLE INHIBITION

There are four types:

1. Competitive inhibition.
2. Uncompetitive inhibition.
3. Mixed inhibition.
4. Non-competitive inhibition.
 COMPETITIVE INHIBITION
� In this type of inhibition, the
inhibitors compete with the
substrate for the active site.

� Formation of E.S complex is

reduced while a new E.I
complex is formed.
UNCOMPETITIVE
INHIBITION
In this type of inhibition,
inhibitor does not compete with
the substrate for the active site
of enzyme instead it binds to
another site known as allosteric
site.
MIXED INHIBITION
o In this type of inhibition both E.I and E.S. complexes are formed.

o Both complexes are catalytically inactive.

NON COMPETITIVE INHIBITION

o An inhibitor molecule binds to the enzyme at a location other than
the active site (an allosteric site).

o The substrate can still bind to the enzyme, but the inhibitor changes
the shape of the enzyme.
IRREVERSIBLE INHIBITION

● This type of inhibition involves the covalent attachment

of the inhibitor to the enzyme.
● The catalytic activity of enzyme is completely lost.
● It can only be restored only by synthesizing molecules.
ACTIVATION
 ACTIVATION

Activation is defined as the conversion of an inactive form of an

enzyme to active form which processes the metabolic activity.

TYPES OF
ACTIVATION
� Activation
by co-factors.
� Conversion of an enzyme precursor.
ACTIVATION BY COFACTORS
� Many enzymes are activated by co-factors.

Examples:

⮚ DNA polymerase is a holoenzyme that catalyzes the

polymerization of deoxyribonucleotide into a DNA strand. It uses
Mg ion for catalytic activity.
 ENZYME SPECIFICITY
� Enzymes are highly specific in nature, interacting with one or few
substrates and catalyzing only one type of chemical reaction.
� Substrate specificity is due to complete fitting of active site and substrate .

Example:
⮚ Oxydoreductase does not catalyze hydrolase reactions and hydrolase
do not catalyze reaction involving oxidation and reduction.
 TYPES OF ENZYME SPECIFICITY
Enzymes show different degrees of specificity:

• Bond specificity.
• Group specificity.
• Absolute specificity.
• Optical or stereo-specificity.
• Dual specificity.
 BOND SPECIFICITY

� In this type, enzyme acts on substrates that are similar in

structure and contain the same type of bond.

Example :

� Amylase which acts on the glycosidic, bond in starch dextrin

and glycogen, shows bond specificity.
 GROUP SPECIFICITY
� In this type of specificity, the enzyme is specific not only to the type of bond but
also to the structure surrounding it.

� Example:

⮚ Pepsin is an enzyme, that hydrolyzes central peptide bonds in which the amino
group belongs to aromatic amino acids e. g phenyl alanine, tyrosine and
tryptophan.
SUBSTRATE SPECIFICITY
� In this type of specificity ,the enzymes acts
only on one
substrate
Example :
⮚ Uricase ,which acts only on uric acid, shows substrate
specificity.

⮚ Maltase , which acts only on maltose,

shows substrate specificity.
 DUAL SPECIFICITY
� There are two types of dual specificity.
⮚ The enzyme may act on one substrate by two
reaction types. different
Example:

� Isocitrate dehydrogenase enzyme acts on isocitrate (one substrate) by oxidation

followed by decarboxylation (two different reaction types) .
DUAL SPECIFICITY
⮚ The enzyme may act on two substrates by one reaction type

Example:

Xanthine oxidase enzyme acts on xanthine and hypoxanthine (two

substrates) by oxidation (one reaction type)