ENZYMES

GROUP 3
 OBJECTIVES
What Are Enzymes and its structure
Functions of Enzymes
To know the enzymes classification and
examples
Learn the Mechanism of Enzyme Reaction
Learn the Enzyme-Substrate Interactions
To know the 4 possible major mechanisms of
catalysis
What is the action and nature of Enzymes
Know the Factors Affecting Enzyme Activity
 WHAT ARE
ENZYMES?
 ENZYMES
Enzymes may be defined as
biocatalysts, “the catalyst of
life”, synthesized by living
cells. They are protein in
nature (exception – RNA
acting as ribozyme), colloidal A catalyst is defined as a
substance that increases the
and thermolabile in character, velocity or rate of a chemical

and specific in their action.

reaction without itself undergoing
any change in the overall process.
 ENZYMES AND CHEMICAL REACTIONS

Chemical reactions must occur continuously in living things!

Examples:
-Photosynthesis
-Breaking down food

Can occur with the help of

macromolecules called
STRUCTURE
OF
ENZYMES
ENZYMES STRUCTURE
FUNCTIONS
OF
ENZYMES
FUNCTIONS OF ENZYMES
It help speed up chemical reactions in
the human body

They help in generating energy in the

body.
FUNCTIONS OF ENZYMES
Enzymes are responsible for the
movement of ions across the plasma
membrane.

Breaks down large molecules into

smaller substances.
CLASSIFICATIONS
OF
ENZYMES
ENZYMES
C
L
A Oxidoreductases
S
S
Catalyze oxidation-
I
reduction reactions
F
I
Example: Conversion of
C alcohol to aldehyde
A
T
I
O
N
ENZYMES
C
L
A
S
Transferase
S Transfer functional groups
I between molecules.
F
I Example: Transfer of a
C phosphate group from ATP to
A glucose.
T
I
O
N
ENZYMES
C
L
A
S
Ligases
S join two molecules,
I typically using ATP.
F
I Example: Joining of DNA
C fragments during
A replication.
T
I
O
N
ENZYMES
C
L
A
S Isomerase
S Rearrange atoms within a
I molecule.
F
I
Example: Conversion of
C
glucose-6-phosphate into
A fructose-6-phosphate.
T
I
O
N
ENZYMES
C
L
A
S Hydrolase
S
Break bonds using water.
I
F
I Example: Breakdown of
C starch into smaller
A carbohydrates.
T
I
O
N
ENZYMES
C
L
A
S Lyase
S
Remove groups of atoms,
I
forming double bonds or
F
rings
I
C Example: Conversion of
A fumarate to malate.
T
I
O
N
EXAMPLES
OF
ENZYMES
 EXAMPLES OF ENZYMES
BEVERAGES DRUG ACTION
FOOD
For example, grapes, honey, hops, PRODUCTS Enzyme action can be
wheat, cassava roots, and potatoes inhibited or promoted by
depending upon the materials Bread can be the use of drugs which
available. Beer, wines and other considered as the finest tend to work around the
drinks are produced from plant
example of active sites of enzymes.
fermentation.
fermentation
in our everyday life.
MECHANISM OF
ENZYME
REACTION
Mechanism of Enzyme Reaction

An enzyme attracts substrates to its active site,

catalyzes the chemical reaction by which products
are formed, and then allows the products to
dissociate. The combination formed by an enzyme
and its substrates is called the enzyme–substrate
complex.
 ENZYME-
SUBSTRATE
INTERACTIONS
Enzyme-Substrate Interactions
When enzymes connect with their substrates, they
create an enzyme-substrate complex. This complex
reduces the energy needed to start the reaction,
making it happen faster. It does this by supplying
specific ions or chemical groups that help molecules
bond together during the reaction.
FOUR POSSIBLE
MAJOR
MECHANISMS OF
CATALYSIS
 FOUR POSSIBLE MAJOR
MECHANISMS OF CATALYSIS
1 2
Catalysis by Covalent
Bond Strain Catalysis
Structural rearrangements in catalysis The substrate is positioned on enzymes,
cause strained substrate bonds, forming a covalent intermediate between the
enzyme and substrate. This occurs through
enabling easier transition to the
covalent mechanisms, such as proteolysis by
transition state, by forcing substrate
serine proteases, which have digestive and
atoms and catalytic groups like
blood clotting enzymes. Their active site,
aspartate into conformations that serine, generates a covalent bond with a
strain substrate bonds. peptide bond, resulting in its hydrolysis.
 FOUR POSSIBLE MAJOR
MECHANISMS OF CATALYSIS
3 Catalysis 4 Catalysis by
Involving Acids Orientation and
and Bases Proximity

Other mechanisms add to the Enzyme-substrate interactions induce

completion of catalytic events reactive groups into proximity with
which are launched by strain one another. Also, groups like
aspartate are chemically reactive, and
mechanisms such as the usage of
their proximity towards the substrate
glutamate as a general acid
favours their involvement in catalysis.
catalyst.
 ACTION
AND NATURE OF
ENZYMES
ACTION AND NATURE OF
ENZYMES
Substrates bind to enzyme, forming an
intermediate complex that produces
products. Enzymes lower activation
energy, catalyzing reactions in a
continuous cycle until completion.
ACTION AND NATURE OF ENZYMES
The enzyme action basically happens in two steps:
Step1: Combining of enzyme and the
reactant/substrate.
→
E+S [ES]
Step 2: Disintegration of the complex molecule to
give the product.
→
[ES] E+P
Thus, the whole catalyst action of enzymes is
summarized as:
E+S→ →
[ES] →
[EP] E+P
MODELS OF ENZYMES ACTIVITY
•Lock and Key Model
This model portrayed
the enzyme as
conformationally rigid
and able to bond only
to substrates that
exactly fit the active
site. The Lock-and-Key Model of Enzyme Action. (a)
Because the substrate and the active site of the
enzyme have complementary structures and
bonding groups, they fit together as a key fits a
lock. (b) The catalytic reaction occurs while the two
 MODELS OF ENZYMES ACTIVITY
•Induced-fit Model
The current theory, known as the
induced-fit model, says that
enzymes can undergo a change in
conformation when they bind
substrate molecules, and the
The Induced-Fit Model of Enzyme
active site has a shape Action. (a) The enzyme
complementary to that of the hexokinase without its substrate
substrate only after the (glucose, shown in red) is bound to
substrate is bound, as shown for the active site. (b) The enzyme
hexokinasa. After catalysis, the conformation changes
dramatically when the substrate
enzyme resumes its original
 BIOLOGICAL CATALYSTS

Enzymes, as biological catalysts, accelerate specific

reactions in living organisms by reducing activation
energy. Their unique structures and active sites
make them highly specific, while allosteric
regulation helps cells respond to internal changes.
 FACTORS
AFFECTING
ENZYME ACTIVITY
FACTORS AFFECTING ENZYME
ACTIVITY
The conditions of the reaction have a great
impact on the activity of the enzymes.
Enzymes are particular about the optimum
conditions provided for the reactions such as
temperature, pH, alteration in substrate
concentration, etc.
FACTORS AFFECTING ENZYME
ACTIVITY
The Enzymes work faster with higher
temperatures, but too much heat can
damage them. Purified enzymes break
down faster in weak solutions and when
left for a long time.
 ACTIVE SITE
Enzymatic catalysis relies on specific amino acids in a
folded active center, forming a pocket. Common amino
acids involved include aspartate, cysteine, glutamate,
histidine, serine, and lysine. Typically, 2-3 essential
amino acids directly contribute to bond formation,
with residues like glutamate, aspartate, and histidine
also acting as proton acceptors or donors.
TEMPERATURE AND PH
Enzymes need the right temperature and pH
(optimum) for maximum activity. Deviating
from the optimum can alter enzyme
structure. For enzymes, the ideal pH is
typically between 5 and 7.
CONCENTRATION AND TYPE OF
SUBSTRATE
Enzyme activity increases with substrate
addition until reaching saturation, where further
substrate doesn't affect velocity. Different
substrates, including competitive inhibitors, can
impact enzyme activity by binding to the active
site, a concept applied in treating bacterial
infections.
 SALT CONCENTRATION
Changes in salinity: Adds or removes cations (+) & anions (–)
• Disrupts bonds, disrupts the 3D shape
• Disrupts attractions between charged amino acids
• Affect 2° & 3° structure
• Denatures protein
• Enzymes intolerant of extreme salinity
• The Dead Sea is called dead for a reason
 Conclusion
In conclusion, enzymes are crucial biological polymers
that catalyze biochemical reactions, playing a vital role in
various metabolic processes essential for sustaining life.
Their structure, classification, mechanism, and factors
affecting their activity are all key aspects to understand
their functions in living organisms.
THAT'S ALL
THANK YOU!!