ENZYME KINETICS

Submitted by: Submitted to:

Nibrasul Haque Dr. Vandana Kumari
Roll No. : 14507 Professor
B.Sc.(H) Zoology Department of Zoology
2nd Year - III Sem Hansraj College
● Contents
★ Introduction
★ Definition of the Reaction rate
★ First order and zero order kinetics
★ Graph of enzyme catalyzed and uncatalyzed reaction.
★ Factors affecting enzyme catalyzed reaction
★ Catalyst and Activation energy
★ Enzyme Kinetic Parameters
★ Inhibitors
Introduction

Enzyme kinetics is the study of the rates of

chemical reactions that are catalysed by
enzymes.

Studying enzyme kinetics provides information

about the diverse range of reactions in the
human body, which we can use to understand
and predict the metabolism of all living things.
Definition of the Reaction Rate

The rate law

Reaction rate is at any time proportional to the product of concentrations of
reactants.
k1
E.g., A+B k-1
C+D

KINETIC EQUATION
Forward reaction = v1= k1 [A] [B]

Reversal reaction = v-1= k-1[C] [D]

First order and zero order kinetics

● First order depend on reactant concentration.

● Zero order do not depend on the reactant concentration.
● Half life is constant in first order.
1 hour
E.g., 100mg 1 hour
50mg
50mg 25mg
Half life = Time to react 50% of substrate
● in zero order the reaction rate is constant. And in first order the reaction rate is
proportional to [S].
GRAPH OF ENZYME CATALYZED AND UNCATALYZED
REACTIONS
K1 K2
E+S ES E+P
K-1
Factors affecting enzyme catalyzed reaction

● Concentration of substrate. ➔ Rate of an enzymatic reaction increases

● Enzyme concentration as the substrate concentration increases
● Temperature until a limiting reagent is reached, after
● pH which further increase in the substrate
● Presence of Inhibitors or Activators concentration produces no significant
change in the reaction rate.

➔ When the concentration of the enzyme is

lower than the concentration of substrate,
the rate is directly dependent on the
enzyme concentration.
➔ Temperature working at optimum
temperature about 400C above this
temperature protein denaturation occurs.
Most enzyme exhibit about 30 to 37 0C

➔ pH working at optimum pH about 6.9 - 8 ,

exception in pepsin - optimum pH
is around 2.
Catalyst and Activation Energy

The catalyst reduce the activation

energy.
Activation energy is defined as the
minimum amount of extra energy
required by a reacting molecule to get
converted into product
Enzymes catalyse the reaction and
thereby decrease the activation energy
and rate of the reaction increase.
ENZYME KINETIC PARAMETERS
K1 K2
E+S ES E+P
K-1 K-2

(Product rarely go back to reactant since this this reactant is thermodynamically stable

K1 K2
E+S ES E+P
K-1

RATE = V = d[P]/dt

Rate1= k1[E] [S] Rate2= k2[ES]

Rate increases by increasing [S], [e] . k is constant.
● At high concentration of
substrate, The enzymes will be
saturated. Won’t able to react
further thus reaches the
maximum velocity.
● Km is Michaelis constant,
characterizes the affinity
between the substrate and the
enzyme
● Concentration of substrate at
which half of the maximum
reaction rate, Vmax/2 .
(Km concentration).
Inhibitors
Enzyme catalysed reactions need to be tightly regulated to ensure that levels of
the product do not rise to undesired levels.
2 types enzyme inhibition,
● Reversible Inhibition
● Irreversible inhibition
Enzyme kinetics is very important
Because it helps us to know,

● How enzyme work

● Helps to predict how enzymes behave in living organisms
(Vmax and Km both play a key role in understanding the metabolism of
the human body.)
THANK YOU
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