The Induced Fit Model

This was introduced due to the

drawbacks of the lock and key
model. The lock and key model
assumed that the active site is
rigid, having the same
conformation as that of the
substrate. The same conformation
of the active site makes the
enzyme very specific for the
substrate.
When scientists were investigating
enzymes, they discovered that the
enzyme binds its substrate and
then converts it into an
intermediate state or a transition
state before getting converted into
the final product.
The lock and key model assumed
that the active site is rigid and has
the same shape as that of the
substrate, so the question arises,
how does an
intermediate/transition state form
when the active site is rigid?
 The lock and key model failed to
explain this phenomenon, hence, a
new model known as the induced
fit model was proposed. According
to this model, the active site of the
enzyme is not rigid but is instead
flexible and can have different
conformations.
 This model assumes that the amino acids present at the active site will
determine the specific binding of the substrate with the enzyme. Once
the substrate binds with the enzyme, the conformation of the active site
gradually changes and attains conformation as that of the substrate
molecule. Hence, it is known as the induced fit model.
The conformation of the active site
further keeps changing
Until the product is formed and released.