PANDIT RAVISHANKAR SHUKLA UNIVERSITY ,

RAIPUR , (C.G.)

ACTIVATION
ENERGY
Submitted by-
ANJALI RAWAT
 CONTENTS
INTRODUCTION
WHAT IS ACTIVATION ENERGY
ENZYMES & ACTIVATION ENERGY
GRAPH BETWEEN FREE ENERGY AND DIRECTION OF REACTION
FUNCTION OF ENZYMES
ENZYMES SPECIFICITY
ACTIVATION ENERGY AND RATE OF REACTION
ARRHENIUS EQUATION
CONCLUSION
REFERENCE
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 INTRODUCTION

Life depends on the existence of powerful and specific catalysts ,the

enzymes. Almost every biochemical reaction is catalyzed by an enzyme.
Kinetic energy and velocity are required to initiate a reaction.
The energy required to start a reaction is activation energy.
Energy in biological system is described in terms of FREE ENERGY G.
Free energy of product is lower than the reaction , So G is negative.

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WHAT IS ACTIVATION ENERGY ?
The energy required by the reactants to undergo
the reaction is known as ACTIVATION ENERGY.

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ENZYMES & ACTIVATION
ENERGY
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 Enzymes are highly specialized proteins that act as catalyst in biological system called
as biocatalyst.
Enzymes lowers the activation energy and activation barrier between substrate and
product.
A molecule of an enzymes can act upon a 1000 or more molecules of a substrate in a
minute.
Enzyme catalyzed reactions occur 1010 - 1014 times faster than un-catalyzed reaction.
Enzyme does not undergo any chemical modification and is available only for
enhancing the rate of reaction.
Higher the activation energy lower the rate of reaction. 4
GRAPH

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 To convert into product, the substrate must attain the TRANSITION STATE.
The starting point of reaction is termed as GROUND STATE
The difference between the energy level of ground state and transition state is
known as activation energy.
The journey of a molecule from reactant or substrate to product encounters an
energy barrier called as activation barrier.
The energy derived from enzyme substrate interaction is known as the binding
energy. It is the major source of free energy used by the enzymes.
 Function of Enzyme

HALDEN {1930} and LINUS PAULING {1946} contributed to the modern

understanding of enzyme catalyst.

The substrate (S) binds to the enzyme (E) at the active site forming an enzyme
substrate complex ES.
E+S ES E+P
Catalysis occur and product P and enzymes are released . In this reaction the
substrate is converted into product, enzyme does not undergo any chemical
modification and is available again for reuse. 6
 ENZYME SPECIFICITY

Human body contains thousands of enzymes.

The enzymes are very specific for their substrate, its active site can only bind particular
substrate.
The active site is a specified conformation on an intact enzyme molecule, is largely
responsible for the ENZYME SPECIFICITY.
Some types of enzyme specificity are there:-
Stereo specificity
Substrate specificity
Reaction specificity
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STEREO SPECIFICITY -
Human enzymes are stereospecific, hence they can act only on D-carbohydrate and L-aminoacid.
D-aminoacid oxidase is an excepton.Enzymes belong to the class isomerase doesnot exhibit stereospecificity.

SUBSTRATE SPECIFICITY -
Enzymes are highly specific for their substrate, which may be absolute or relative
In absolute, an enzyme can bind with only one substrate.
Eg- glucokinase phosphorylates only glucose.
urease splits urea into ammonia and CO2
In relative, an enzyme can act upon two or more substrate which are structuraly related.
Eg- hexolinase phosphorylates glucose fructose and mannose
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REACTION SPECIFICITY

The same substrate can undergo different types of reactions, each catalyzed by a
separate enzymes.

E.g.- glucose 6-phosphate has different fates in glycolysis , gluconeogenesis and

HMP shunt catalyzed by different enzymes.
An imaginary enzyme(stickase) designed to catalyse breakage of metal stick 13
ACTIVATION ENERGY AND RATE OF REACTION

The rate of reaction reflects the activation energy.

Higher the activation energy slower the rate of reaction.
ARRHENIUS EQUATION :
K=Ze -Ea/RT
Where, Z and e are exponents
Ea- activation energy
R- the gas constant=8.314 J/mol K
T- the temperature [ kelvin]
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When we put log on both side of Arrhenius equation
ln K = ln [Z*e-Ea/RT]
ln K= [ln Z+ ln e-Ea/RT ]
ln K = ln Z - Ea/RT [ln e]
ln K = -Ea/RT ln e + ln Z [ln e = 1]
ln K = -Ea/RT + ln Z
Y = Mx + b where, y = ln K
x = 1/T And M = -Ea/R
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 CONCLUSIONS

The rate at which a molecule undergoes a particular reaction is enhanced by

ACTIVATION ENERGY.
Molecules with high activation energy are more stable.
Energy barrier or activation barrier decreases as the rate of reaction
increases.
With out such energy barrier, complex macromolecules would reverse
spontaneously to much simpler molecular forms.
Binding energy is the major source of free energy used by the enzymes to
lower the activation energy.
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References
LEHNINGER PRINCIPLE OF BIOCHEMISTRY 5 TH EDITION DAVID L. NELSON &
MICHAEL M. COX

http://www.sumanasinc.com/webcontent/animations/content/enzymes/enzymes.html
https://en.wikipedia.org/wiki/Activation_energy
https://www.khanacademy.org/test-prep/mcat/biomolecules/enzyme-structure-and-
function/v/en

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THANKS!
Any questions?

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