University Of Kota , Kota

Department Of Microbiology
Guided By: Submitted By:
Shweta Gupta Pari Jaiswal
 Introduction to Enzymes
 Types of Enzymes
 Introduction to Enzyme Kinetics
 Lock and Key Theory
 Comparison of Fischer and Koshland
Mechanism
 Michaelis Menton Model
 Graph
 Km
 Vmax
 Pharmaceutical Importance
 References
 Anselme Payen was the first to discover
and enzyme , “Diastase” in 1833.
 Enzymes are those macromolecular
biological catalyst that accelerate chemical
reactions.
1. Oxidoreductases – catalyse
oxidation/reduction reactions. Eg.Glucose-6-
Phosphate Dehydrogenase
2. Transferases – transfer of atom or group
between two molecules. Eg.Hexokinase
3. Hydrolases – catalyze the hydrolysis reaction.
Eg.Pepsin , Trypsin
4. Lyases – removal of group from substrate.
Eg.Fumarase
5. Isomerases – catalyze isomerization changes
within a single molecule. Eg.Epimerase
6. Ligases – join two molecules with covalent
bonds. Eg.DNA Ligases
 Temperature
 pH
 Enzyme Specificity
 Active Site
 Enzyme Concentration
 Substrate Concentration
 Presence of Any Inhibitors or Activators
 It is the study of the chemical reaction that
are catalysed by enzymes.
 In enzyme kinetics, the reaction rate is
measured and the effects of varying the
conditions of the reactions are investigated.
 Enzyme kinetics reveals the catalytic
mechanism of that enzyme, its role in
metabolism, how its activity is controlled, and
how a drug or an agonist might inhibit the
enzyme.
 Michaelis – Menten kinetics is one of the
simplest and best-known models of enzyme
kinetics. •
 This model explain how an enzyme can
cause kinetic rate enhancement of a reaction
and why the rate of a reaction depends on
the concentration of enzyme present.
 According to this model the enzyme
reversibly bind with substrate to form an ES
complex that subsequently yields product.
• The mechanism of enzyme catalyzed
reactions is studied by making kinetic
measurements on enzyme-substrate
reaction systems.
• The simple kinetic model is obtained, when
plotting the rate of catalysis, V (reaction
velocity), v/s the substrate concentration, [S]
(fixed enzyme concentration)
From this equation, reaction velocity, V
can be expressed as:

V = V max [S]
Km + [S]

Km = K-1 + K2
K1
 It is the substrate concentration, [S] at which
half maximum velocity of reaction is
observed.
 Km implies that half of the active sites on the
enzymes are filled.
 It is the measure of the binding strength
between substrate and the enzyme.
 where lower Km value indicates a strong
affinity between the substrate and enzymes.
 It is the maximum velocity of reaction or rate
at which the enzyme catalyzed a reaction
under given conditions.
 Vmax is reached when all enzyme sites are
saturated with the substrate. This will
happen when substrate concentration [S] is
greater than Km.
 Enzymes are involved in all physiological
processes which makes them the targets of
choice for drugs that cure human disease.
 Enzyme kinetics represents the important
tool by which scientist identify and
characterize therapeutic agents that
selectively inhibit the rates of specific
enzymes catalyzed processes.
 19,78 ,Introduction to Enzymes , Enzyme
Kinetics , Understanding Enzymes By
Palmer
 121,Chemistry of Enzymes , Biochemistry By
M N Chatterjee