Michaelis Menten

Equation
Group # 3
Tashif Suhair Yasma Shezal
Huraira Hanif Tehreem Farooq
Esha Edrees Esha Zubair
Maryam Zia Koseen Maryam
 01 HISTORY

CONTENTS 02 MICHAELIS MENTEN EQUATION

03 ASSUMPTIONS

04 LINE WEAVER BURK PLOT

• Infographic Style
HISTORY
In the early stages of this work
Michaelis was joined by Maud
Menten during the period of its
operation, from 1905 to 1921.

 Michaelis and Menten were able to

express mathematically the relationship
which demonstrated that each enzyme
not only has its own substrate but also
that at sufficient concentrations of
substrate it has its own rate of causing
that substrate to change chemically.

 One of the constants used in expressing

this rate is now called the Michaelis-
Menten constant.
 Michaelis Menten Equation
The Michaelis-Menten equation arises from the general equation for
an enzymatic reaction:

K1 K1 is the rate of the formation (forward reaction) of ES

from E + S.

K1 K2
E+S ES E+P K-1 K-1 is the rate of breakdown (reverse reaction)
of ES into E + S.
K- 1

K2 is the rate of formation (forward reaction) of E + P

K2 from ES.
 [S]
V =V o max
K +[s] m

It represents the maximum

It represents the initial velocity, when all active sites Vmax
velocity of enzymatic
reaction.
Vo are occupied.

Km is the Michaelis-Menten

It represents the
constant which shows the
concentration of the substrate.
Km
concentration of
[S] K-1 + K2
substrate
Km =
K1
 Graph for Understanding

Vmax

Velocity (Rate)

Vo

Substrate Concentration
 Conclusion of Km

Large Km
Large value of Km indicates that there is large concentration
of substrate in enzymatic reaction due to less affinity.
01

Small Km
Small value of Km indicates small concentration of substrate 02
in enzymatic reaction due to high affinity.
ASSUMPTIONS / CHARACTERS

01 Substrate Concentration
There should be high
concentrations of substrate so that
all active sites of enzyme can be
easily occupied.

02 Steady State
It is the state in which rate of
formation of ES and rate of
03 Initial Velocity
Initial velocity of enzymatic reaction
can be calculated by Michaelis Menten
breakdown ES are equal. Equation.
Need of Line weaver Burk plot

The need of Line weaver Burk plot arises when

affinity of substrate is very low to the enzyme.

Due to low affinity and large concentration of

substrate normal graph occupies large space.

Line weaver Burk plot is proved very convenient for

saving space.
 Review

MICHAELIS
MENTEN ASSUMPTIONS
EQUATION

HISTORY CONCLUSIONS LINE WEAVER

BURK PLOT
THANK
YOU