Enzymes
Enzymes
Enzymes
CONTENTS
Chemistry
Classification
Mechanism of Enzyme Action
Enzyme Kinetics
Inhibition
Activation
Specificity
CHEMISTRY
INTRODUCTION
Enzymes are biological catalysts
that speed up the rate of the
biochemical reaction.
Hammerhead Enzyme
STRUCTURE OF ENZYMES
The active site of an enzyme is the region that binds substrates,
co-factors / prosthetic groups and contains residue that helps to
hold the substrate.
Co-factors is the non protein molecule which carries out chemical reactions that can
not be performed by standard 20 amino acids.
These are the inorganic molecules required for the proper activity of
enzymes.
Examples:
Enzyme carbonic anhydrase requires Zn for it’s activity.
Hexokinase has co-factor Mg
ORGANIC CO-FACTORS
These are the organic molecules required for the proper activity of
enzymes.
Example:
Glycogen phosphorylase requires the small organic molecule
pyridoxal phosphate.
TYPES OF ORGANIC CO-FACTORS
Prosthetic Group A prosthetic Coenzyme
group is a tightly bound organic A coenzyme is loosely bound
co- factor e.g. Flavins, heme organic co-factor. E.g. NAD+ +
groups and biotin.
TYPES OF ORGANIC CO-FACTORS continuation…
Extracellular enzymes are synthesized in the cell but secreted from the cell to
work externally.
Example :
Digestive enzyme produced by the pancreas, are not used by the cells
in the pancreas but are transported to the duodenum.
CHARACTERISTICS
Enzymes speed up the reaction by lowering the activation energy of the reaction.
Their presence does not effect the nature and properties of end product.
They are highly specific in their action that is each enzyme can catalyze one kind of
substrate.
Small amount of enzymes can accelerate chemical reactions.
Enzymes are sensitive to change in pH, temperature and substrate concentration.
Turnover number is defined as the number of substrate molecules transformed per
minute by one enzyme molecule.
NOMENCLATURE OF ENZYMES
An enzyme is named according to the name of the substrate it catalyses.
Some enzymes were named before a systematic way of naming enzyme was
formed.
Example:
pepsin, trypsin and rennin
By adding suffix -ase at the end of the name of the substrate, enzymes are named.
Example:
CLASSIFICATION
CLASSIFICATION OF ENZYMES
A systematic classification of enzymes has been developed by International
Enzyme Commission.
Each class is further divided into sub classes, sub sub-classes and so on, to
describe the huge number of different enzyme- catalyzed reactions.
CLASSIFICATION OF ENZYMES
MECHANISM OF
ENZYME ACTION
MECHANISM OF ENZYME ACTION
Hence, the reaction rate is increased many folds in the presence of enzymes.
The total energy of the system remains the same and equilibrium state is not
disturbed.
LOCK AND KEY MODEL
Lock and key hypothesis assumes the active site of an enzymes are rigid in
its shape.
There is no change in the active site before and after a chemical reaction.
INDUCED FIT MODEL
More recent studies have revealed that the process is much more
likely to involve an induced fit model(proposed by DANIAL KOSH
LAND in 1958).
According to this exposure of an enzyme to substrate cause a change
in enzyme, which causes the active site to change it’s shape to allow
enzyme and substrate to bind.
INDUCED FIT MODEL
ENZYMES KINETICS
INTRODUCTION
Kinetic analysis reveals the number and order of the individual steps by which
enzymes transform substrate into products.
Studying an enzyme's kinetics in this way can reveal 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
RATES OF REACTION AND THEIR DEPENDENCE ON
ACTIVATION ENERGY
Activation Energy (Ea): “The least amount of energy needed for a chemical
reaction to take place.”
Enzyme (as a catalyst) acts on substrate in such a way that they lower the
activation energy by changing the route of the reaction.
The reduction of activation energy (Ea) increases the amount of reactant
molecules that achieve a sufficient level of energy, so that they reach the
activation energy and form the product.
Example:
Carbonic anhydrase catalyses the hydration of 10⁶ CO₂ molecules per
second which is 10⁷x faster than spontaneous hydration.
ENZYMES LOWER THE ACTIVATION
ENERGY OF A REACTION
KINETICS OF ENZYMES CATALYSIS
Enzymes catalysis:
“ It is an increase in the rate of reaction with the help of enzyme(as
catalyst).”
Substrate concentration
EFFECT OF TEMPERATURE
Raising the temperature increases the rate of enzyme catalyzed reaction by increasing
kinetic energy of reacting molecules.
The temperature coefficient is a factor Q₁₀ by which the rate of biological processes
increases for a 10 ᵒC increase in temperature.
However some times heat energy can also increase kinetic energy to a point that
exceed the energy barrier which results in denaturing of enzymes.
EFFECT OF PH
Rate of almost all enzymes catalyzed reactions depends on pH
High or low pH value than optimum value will cause ionization of enzyme
which result in denaturation of enzyme
A change in pH can alter the ionization of
the R groups of the amino acids. When
the charges on the amino acids change,
hydrogen bonding within the protein
molecule change and the molecule
changes shape. The new shape may not
be effective.
PH AFFECTS THE FORMATION OF HYDROGEN
BONDS AND SULPHUR BRIDGES IN PROTEINS AND SO
AFFECTS SHAPE
MICHAELIS-MENTEN MODEL & EFFECTS OF
SUBSTRATE CONCENTRATION
Michaelis-Menten Model:
“According to this model the enzyme reversibly combines with
substrate to form an ES complex that subsequently yields product,
regenerating the free enzyme.”
PHARMACEUTICAL IMPORTANCE
Enzymes are virtually involved in all physiological processes
which makes them the targets of choice for drugs that cure or
ameliorate human disease.
INHIBITORS:
Any substance that can diminish the velocity of an enzyme
catalyzed reaction is called an inhibitor.
TYPES OF INHIBITION
REVERSIBLE INHIBITION
It is an inhibition of enzyme activity in which the inhibiting molecular
entity can associate and dissociate from the protein‘s binding site.
In this type of inhibition, inhibitor does not compete with the substrate
for the active site of enzyme instead it binds to another site known as allosteric
site.
TYPES OF ACTIVATION
Activation by co-factors.
Examples;
DNA polymerase is a holoenzyme that catalyzes the polymerization of de -
oxyribonucleotide into a DNA strand. It uses Mg- ion for catalytic activity.