GROUP 2: Enzymes: Biological Catalysts

What are 'ENZYMES'? Once the substrate has passed through the transition
state with the help of the enzyme, it can proceed to
An Enzyme is a biomolecule that can be synthesized form the product(s).
biologically (naturally occurring) or through other processes  Activation Energy
(synthetically). Most enzymes are proteins with catalytic •Amount of energy required to reach the transition
capabilities crucial to perform different processes. Metabolic state.
processes and other chemical reactions in the cell are carried •The difference between the energy levels of ground
out by a set of enzymes that are necessary to sustain life. state (Reactants) and the transition state.

A catalyst is a chemical that speeds up chemical How does enzyme reduce activation energy?
reactions. In organisms, catalysts are called enzymes.
Essentially, enzymes are biological catalysts. Enzymes reduce activation energy by providing a pathway for
the reaction that has a lower energy barrier. They do this by
The substrate is any substance that is being converted into precisely aligning substrates, stabilizing the transition state,
products during the chemical reaction. Since substrate and facilitating chemical interactions, making reactions occur
undergoes reaction, they are also called reactants. more easily and quickly.

Mechanisms on the formation of the Enzyme-substrate Models for binding of substrate to enzyme
Complexes
1 Lock and Key Model
Substrate Specificity
• This was proposed by German chemist Emil Fischer in 1899.
• Absolute: Enzymes act only on one substrate.
•According to this theory the structure or conformations of
• Relative: Some enzymes act on structurally related enzymes are rigid
substances.
•Substrate fits to binding active site.
• Broad: Some enzymes act on closely related substances.
•Assumes that active site is rigid or preshaped where only
Active Site substrate can bind.

• The region of the enzyme surface which combines with the 2 Induced Fit Model
substrate to form the enzyme-substrate complex and at which
the transformation of the substrate to products occurs is called • It was first proposed by Koshland in 1958.
the active site of the enzyme. The active site is a pocket
formed by the folding of the protein where the substrates bind. •According to the induced fit hypothesis, the active site of an
enzyme is not rigid and pre-shaped; instead, it is flexible and
Parts of Active Site elastic so that it can be changed or modified suitably if need
arises.
1. Binding Site: This is where the substrate molecules attach
to the enzyme. It often involves specific interactions, like • It follows therefore that the active site need not have a
hydrogen bonds or van der Waals forces. configuration exactly complementary to that of the substrate.
2. Catalytic Site: This is where the actual chemical reaction
takes place. Enzymes facilitate reactions by providing a • According to the model, the contact with the substrate
suitable environment and, in some cases, actively participating induces some configurational changes in the active site of the
in the reaction.Enzyme: enzyme so that its new configuration is perfectly matching
with that of the substrate.
Mechanism of Action
State:
1 Ground State- The ground state is the initial state
where the enzyme and substrate are both at their ENZYME STRUCTURES
lowest energy levels. The substrate, in its ground
state, binds to the enzyme's active site. At this point, 1. Primary
the substrate is not yet transformed into the product.
•The Primary structure of proteins is the exact ordering of
2 Transition State- For a chemical reaction to occur, amino acids forming their chains.
the substrate needs to pass through a high-energy
transition state. This transition state represents an •The exact sequence of the proteins is very important as it
unstable, energy-rich intermediate stage where determines the final fold and therefore the function of the
chemical bonds are breaking and forming. It's the protein.
point in the reaction where the activation energy
barrier needs to be overcome.
•The number of polypeptide chains together form proteins.
These chains have amino acids arranged in a particular
Formation of the enzyme – product complex sequence which is characteristic of the specific protein. Any
change in the sequence changes the entire protein.
 Product Formation

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 GROUP 2: Enzymes: Biological Catalysts
2. Secondary- refers to the local folded structures that form
within a polypeptide due to interactions between atoms of the
backbone. Functions of Enzymes

•The proteins do not exist in just simple chains of The enzymes perform several functions in our bodies. These
polypeptides. include:

•These polypeptide chains usually fold due to the interaction 1. Enzymes help in signal transduction. The most
between the amine and carboxyl group of the peptide link. common enzyme used in the process includes protein
kinase that catalyzes the phosphorylation of proteins.
•The structure refers to the shape in which a long polypeptide
chain can exist. 2. They break down large molecules into smaller
substances that can be easily absorbed by the body.
•They are found to exist in two different types of structures α 3. They help in generating energy in the body. ATP
– helix and β – pleated sheet structures. synthase is the enzyme involved in the synthesis of
energy.
(a) α – Helix:
4. Enzymes are responsible for the movement of ions
across the plasma membrane.
α – Helix is one of the most common ways in which a
polypeptide chain forms all possible hydrogen bonds by 5. Enzymes perform a number of biochemical reactions,
twisting into a right-handed screw with the -NH group of each including oxidation, reduction, hydrolysis, etc. to
amino acid residue hydrogen-bonded to the -CO of the eliminate the non-nutritive substances from the body.
adjacent turn of the helix. The polypeptide chains twisted into
a right-handed screw. 6. They function to reorganize the internal structure of
the cell to regulate cellular activities.
b) β – pleated sheet:

In this arrangement, the polypeptide chains are stretched out

beside one another and then bonded by intermolecular H-
bonds. In this structure, all peptide chains are stretched out to
nearly maximum extension and then laid side by side which is
held together by intermolecular hydrogen bonds. The structure
resembles the pleated folds of drapery and therefore is known
as β – pleated sheet.

This structure arises due to the regular folding of the backbone

of the polypeptide chain due to hydrogen bonding between -
CO group and -NH groups of the peptide bond.
TYPES OF ENZYMES
•However, segments of the protein chain may acquire their
own local fold, which is much simpler and usually takes the
shape of a spiral an extended shape or a loop. These local 1.Oxidoreductase – are a broad group of enzymes that
folds are termed secondary elements and form the proteins catalyze electron transfer from one molecule (reductive
secondary structure. molecule, also known as electron donor) to another molecule
(oxidant molecule, also known as electron acceptor).
3. Tertiary
2.Transferase – are a class of enzymes that help transfer or
remove a specific functional groups (methyl, phosphate,
•This structure arises from further folding of the secondary
glycosyl, etc) from one molecule to another.
structure of the protein. H-bonds, electrostatic forces,
disulphide linkages, and Vander Waals forces stabilize this
structure. The tertiary structure of proteins represents overall 3.Hydrolase – are a class of enzymes that commonly function
folding of the polypeptide chains, further folding of the as biochemical catalyst that use water to break a chemical
secondary structure. bond, which typically results in dividing a larger molecule into
smaller molecules.
•It gives rise to two major molecular shapes called fibrous and
globular. 4.Lyase – are a group of enzymes that catalytically aiding in
breaking various chemical bonds by means of elimination
reaction through methods other than hydrolysis and oxidation.
•The main forces which stabilize the secondary and tertiary
structures of proteins are hydrogen bonds, disulphide linkages,
van der Waals and electrostatic forces of attraction. 5.Isomerase – are a general class of enzymes that convert
(Isomerization) a molecule from one isomer to another. It
facilitates intermolecular rearrangements in which bonds are
4. Quaternary - the interaction of two or more folded
broken and formed.
polypeptides. Many proteins require the assembly of several
polypeptide subunits before they become active. If the final
protein is made of two subunits, the protein is said to be a 6.Ligase – also called Synthetase, are a class of enzymes that
dimer. catalyzes the binding or joining of two large molecules

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 GROUP 2: Enzymes: Biological Catalysts
through the formation of a new chemical bond or linking
together of two compounds.

FACTORS AFFECTING ENZYME ACTIVITY

Enzymes are proteins that catalyze biochemical reactions in

living organisms. The activity of enzymes can be influenced
by various factors, including:

1. Temperature: Enzyme activity is highly sensitive to

temperature. As temperature increases, enzyme activity
generally increases due to faster molecular motion and more
frequent collisions between the enzyme and its substrate.
However, excessively high temperatures can denature
enzymes, causing them to lose their shape and functionality.

2. pH: Enzymes have an optimal pH range at which they

exhibit maximum activity. Deviations from this pH range can
affect the enzyme's three-dimensional structure and alter its
active site, leading to a decrease in activity. Different enzymes
have different pH optima based on their specific biological
environment.

3. Substrate concentration: The rate of an enzymatic reaction

typically increases with increasing substrate concentration
until a saturation point is reached. At this point, all active sites
of the enzyme are occupied, and further increases in substrate
concentration do not significantly increase the reaction rate.

4. Enzyme concentration: Higher enzyme concentrations

generally result in faster reaction rates, assuming substrate
concentration is not limiting. This is because a higher
concentration of enzymes provides more available active sites
for substrate binding.

5. Inhibitors: Inhibitors are molecules that bind to enzymes

and reduce their activity. They can be classified as reversible
or irreversible inhibitors. Reversible inhibitors can bind to the
enzyme temporarily and can be displaced, while irreversible
inhibitors form strong covalent bonds with the enzyme,
permanently inactivating it.

6. Activators: Activators are molecules that enhance enzyme

activity. They can bind to the enzyme and induce
conformational changes that increase the enzyme's catalytic
efficiency.

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