This document discusses enzyme kinetics and provides details about key concepts. It introduces enzymes and their role in catalyzing reactions. It then describes enzyme kinetics as the study of reaction rates of enzyme-catalyzed reactions under varying conditions. Several key aspects of enzyme kinetics are summarized, including parametric analysis of enzyme catalysis, enzyme specificity, the lock and key model, and the Michaelis-Menten kinetics model. This model describes how reaction rates increase with substrate concentration until reaching a maximum rate Vmax as the enzyme becomes saturated.

2. ENZYME
KINETICS
Ahmed Nawaz 13ch153
Waleed Shaikh 13CH03
Talal Ashraf 13CH10
Muzamill Hussain 13CH19
Inayat Morio 13CH136

3. Contents: • Enzyme
• Enzyme Kinetics
• Parametric Analysis of enzyme
catalysis
• Enzyme specific to substrate
• Key And Lock Model
• Michaelis Menten Kinetics Model for
Enzyme

4. Enzymes
• Enzymes are usually protein molecules that manipulate other
molecules — the enzymes' substrates.
• These target molecules bind to an enzyme's active site and are
transformed into products through a series of steps known as the
enzymatic mechanism.
• These mechanisms can be divided into single-substrate and
multiple-substrate mechanisms.

6. Introduction
Enzyme
Kinetics
• Enzyme kinetics is the study of the chemical
reactions that are catalyzed by enzymes.
• In enzyme kinetics, the reaction rate is
measured and the effects of varying the
conditions of the reaction is investigated.
• Studying an enzyme's kinetics in this way can
reveal the catalytic mechanism of this
enzyme, its role in metabolism, how it activity
is controlled, and how a drug or an agonist
might inhibit the enzyme.

8. Parametric
Analysis of
Enzyme
Catalysis
• It is often asserted that enzymes are more active, i.e.,
allow reactions to go faster, than non biological
catalysts.
• At the ambient temperatures where enzymes are most
active they are able to catalyze reactions faster than
the majority of artificial catalysts.
• When the reaction temperature is increased, solid
(synthetic) catalysts may become as active as
enzymes.
• The enzyme activity does not increase continuously as
the temperature is raised. Instead, the enzyme usually
loses activity at quite a low temperature, often only
slightly above that at which it is typically found.

9. How are
enzymes
specific to
substrates?
• Enzymes are specific to substrates as they
have an active site which only allow certain
substrates to bind to the active site.This is
due to the shape of the active site and any
other substrates cannot bind to the active
site.
There is a model which is well known in the
biology field of the lock and key model.This is
because you have to have the correct key to
insert it into the lock.This goes the same as
an enzymes active site and the substrate.

10. Key And
Lock Model

12. Michaelis–
Menten
kinetics
• As enzyme-catalyzed reactions are
saturable, their rate of catalysis does
not show a linear response to
increasing substrate. If the initial
rate of the reaction is measured over
a range of substrate concentrations
(denoted as [S]), the reaction rate (v)
increases as [S] increases, as shown
on the right. However, as [S] gets
higher, the enzyme becomes
saturated with substrate and the
rate reaches Vmax, the enzyme's
maximum rate.

13. Mathematical
Model For
Enzyme Kinetics
This equation is called Michaelis–Menten equation.
Where,
Here, Vmax represents the maximum rate achieved by the system, at
maximum (saturating) substrate concentrations.
The Michaelis constant Km is the substrate concentration at which
the reaction rate is half of Vmax.