Q1: Describe the mechanism of enzymatic action with suitable examples:

MECHANISM OF ENZYMATIC TECHNOLOGY:

All enzymes are macromolecules and have numerous specific areas called active sites on their
surface. During the enzymatic activity, substrate molecules attach at these active sites and an
unstable enzyme-substrate complex is formed. This enzyme-substrate complex dissociates to set
free the product and the enzyme.
There are two ideas that explain how the enzyme-substrate complex is formed.
 The lock and key theory
 Theory of induced model fit
The rate of reaction is increased because the activation energy is lowered as a result of the
formation of the enzyme-substrate complex.

MODE OF ACTION:
The nature of the enzyme and the substrate molecule determine the method of enzyme activity,
which may be described by the following:
 Development of the ESC (enzyme substrate complex):
 A decrease in activation energy
 Development of the ESC (Enzyme Substrate Complex):

The enzyme and the substrate unite to produce an unstable complex known as the enzyme-
substrate complex in all enzyme-governed processes. (ESC). The enzyme and the product of this
complex separate. Complex of an enzyme and a substrate.
Enzyme + Product = Enzyme Substrate Complex (s).
Each enzyme's surface has a number of focused regions. They are known as active sites. At
these locations, the enzyme and the substrate molecules interact. The product is readily formed
when the substrate molecules come together at the active sites. The end product created when
new bonds are made separates from the enzyme. A new enzyme-substrate molecule complex is
created when the enzyme is free to interact with additional substrate molecules. The following
hypotheses have been used to explain the process of the enzyme-substrate complex formation
as well as the enzyme's trait of specificity.

LOCK AND KEY MODEL:

Emil Fisher proposed this hypothesis (1898). This idea proposes that a specific substrate with a
certain structure can only bind to the unique active site located on the surface of a specific
enzyme, much as a lock can only be opened by its key. After the product is discharged, the
enzyme is unaltered.

According to the "lock-and-key" concept of enzyme-substrate interaction, the enzyme and the
substrate have distinct complimentary geometric geometries that perfectly match one another.
Enzymes are extremely specialized. Before they can catalyze a chemical process, they first need
to bind to a certain substrate.

INDUCED FIT MODEL:

Daniel Koshland has offered this hypothesis (1966). The form (structure) of the active sites that
may be discovered on the surface of enzymes is flexible, not rigid, according to this notion.
Initially, these active sites are not compatible with the substrate molecule, but when a
particular substrate molecule approaches the enzyme, it causes a change in the active site's
structure and attaches to it. In other words, it may be claimed that the arrangement of active
sites is flexible and changes when a particular material comes into contact, as opposed to being
permanent or rigid as has been suggested by the lock and key idea. The substrate molecule's
complementarity with the active site is altered somewhat. So, only one unique enzyme and one
specific substrate combine to produce an enzyme-substrate complex.

Lowering of Activation Energy:

The energy required to start a chemical reaction is a need shared by all chemical substances. It
is known as activation energy.
Enzymes have the power to lower the amount of energy needed to activate the molecule.
Therefore, when an enzyme is present, the reactant substrates are transformed into a product
with a significantly lower energy input. The activation energy is typically reduced by the
enzymes by around 65%. Due to this, a process that occurs at a high temperature outside the
cell instead occurs inside it at room temperature with the aid of an enzyme.