Enzyme Kinetics

1. ENZYME KINETICS
By-
Manish Sahu
M.Sc. Chemistry (Final)
Sp.- Physical Chemistry

2. SYNOPSIS
• Introduction
• History
• Derivation
• Graphical Representation
• Application
• References

3. INTRODUCTION
Michaelis-Menten kinetics is one of the best
known model of enzyme kinetics.
The model takes the form of an
equation describing the rate of enzymatic
reactions by relating reaction rate.

4. HISTORY
• The modern relationship between substrate
and enzyme concentration was propose by in
1903 by VICTOR HENRI.
• A microscopic interpretation was thereafter
proposed in 1913 by LEONOR MICHAELIS and
MAUD MENTEN.

5. DEFINITION
Michaelis-menten constant which show
the concentration of the substrate when
the reaction velocity equal to one heavy
of the maximum velocity for the reaction

6. DERIVATION
Let us consider a single substrate , single
binding site reaction
We have,

7. • Rate of formation of ES at any time t =
Rate of deformation of ES at any time t =
So, from steady state approximation

8. • Separating the constant from variables
Km

9. • This is known as Michaelis –Menten
equation
Special cases

10. GRAPHICAL REPRESENTATION

11. APPLICATION
• In this equation the constant is a measure of
how efficiently an enzyme converts a substrate
into product.
• It helps in variety of biochemical reactions
including alveolar clearance of dusts.
• The richness of species pools
• Clearance of blood alcohol
• The photosynthesis irradiance relationship
• Bacterial phage infection

12. REFERENCES
• Bio Physical Chemistry By
-J.N GURTU & A.GURTU
• Enzymatic Reaction Mechanism By
-A. FERSHT W.H.FREEMAN