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CHAPTER 4
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Energy
Energy
is capacity to do work
Free energy
A Criterion for spontaneous
change
Free energy is the portion of a
systems energy that can
perform work when
temperature is uniform
throughout the system.
The change in free energy
as a system goes from a
starting state to a different
stage is represented by G
(free energy change)
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EXERGONIC
1. Exergonic (energy-yielding)
2. In exergonic reactions free energy is released
3. The product have less energy than the reactant
4. Exothermic (heat releasing)
5. Spontaneously
6. E.g., cellular respiration
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Endergonic
1. Endergonic (energy-requiring)
2. There is a net input of free energy
3. The product contains more energy than was present in the
reactants
4. Endothermic reactions (absorb heat)
5. Non-Spontaneously
6. E.g., protein synthesis, photosyntensis
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Activation energy
a typical chemical reaction may be
represented as :
A B + C
in this case A represents the substrate and
B and C are the products.
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Enzymes and activation energy
Activation energy (E
A
)
is the amount of energy
necessary to push the
reactants over an
energy barrier.
Enzyme speed
reactions by lowering
E
A
.
The transition state can
then be reached even at
moderate temperatures.
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At the summit the
molecules are at
an unstable point,
the transition state.
The difference
between
free energy of the
products and the
free
energy of the
reactants
is the delta G.
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Enzymes do not change delta G.
It hastens reactions that would occur eventually.
Because enzymes are so selective, they
determine which chemical processes will occur
at any time.
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ENZYMES
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Enzyme
1. All are globular protein
2. Being protein, they are coded by DNA
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Properties of Enzyme
1. They are catalysts
2. They are very efficient. Very small amount of
catalysts brings about the change of large
amount of substrates
3. They are highly specific
4. Enzyme lower the activation energy
5. The catalyzed reaction is reversible
6. Enzymes posses active sites where the
reaction takes place
7. Their presence does not alter the nature of
properties of the end product of the reaction
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Factors affecting the rate of enzyme
reactions
Enzyme Concentration
Substrate Concentration
Temperature
pH
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Enzyme Concentration
Rate of reaction is
proportional to the
enzyme concentration
(pH and temperature
kept constant)
The rate of reaction
increased by increasing
an enzyme
concentration
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3. At high substrate concentration, the active sites are
virtually saturated with substrate
4. Any extra substrate has to wait the complex has
released the product
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Substrate Concentration
1. The rate of enzyme
reaction increases
with increasing
substrate
concentration
2. The theoretical
maximum rate
(Vmax) is never quite
obtained. This is
because when any
further increase in
substrate
concentration
produce no
significant.
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Temperature
1. The temperature that
promotes maximum
activity is referred to
as optimum
temperature
2. Temperature
increased above this
level, a decreased of
activity occurs
3. Optimum temperature
of most mammalian is
about 37 40
o
C
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pH
1. Every enzyme functions most efficiently over a particular pH range
2. As pH decreases, acidity increases and the concentration of H+ ions
increases. This increases the number of positive charges in the medium
3. Extreme pH are encountered by an enzyme, then it will be denaturized
4. Optimum pH values for some enzymes
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Optimum pH values for some
enzymes
Enzyme Optimum pH
Pepsin
2.00
Sucrase
4.50
Enterokinase
5.50
Salivary Amylase
4.80
Catalase
7.60
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ENZYME ACTION
MECHANISM
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Enzyme structure and function :-
1. enzymes are complex three dimensional globular
proteins
2. some of enzyme have other associates molecules
3. enzyme molecule is normally larger than the substrate
molecule
4. only a small part of the enzyme molecule actually
comes into contact with the substrate - active site.
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5. only a few of the amino acids which so called
catalytic amino acids make up the active site
6. and they are often some distance apart in the
protein chain but are brought into close proximity by
the folding of that chain
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Mechanism of enzyme action
2 hypothesis
Lock and Key Hypothesis
Proposed by Emil Fisher, 1890
Induced Fit Hypothesis
Proposed by Daniel Koshland, 1959
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Lock and Key Hypothesis
Active site of the
enzyme is
complementary to the
structure of the
substrate molecule.
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Lock and Key Hypothesis
Mechanism
Substrate (the key) fits into a rigid active site
of the enzyme (the lock), like a key into lock.
Forming enzymes-substrate complex
Reaction product molecules leaves active site
of the enzyme
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Mechanism of enzyme action
Enzymes are thought to operate on a lock and
key mechanism
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In the same way that a key fits a lock very
precisely, so the substrate fits accurately into
the active site of the enzyme molecule.
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The two molecules form a temporary structure called the
enzyme-substrate complex.
The products have a different shape from the substrate and
so, once formed, they escape from the active site, leaving it
free to become attached to another substrate molecule.
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Modern interpretations of the lock and key
mechanism suggest that in the presence of the
substrate the active site may change in order to
suit the substrates shape.
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Modern interpretations of the lock and key
mechanism suggest that in the presence of
the substrate the active site may change in
order to suit the substrates shape.
The enzyme is flexible and moulds to fit the
substrate molecule in the same way that
clothing is flexible and can mould itself to fit
the shape of the wearer.
The enzyme initially has a binding
configuration which attracts the substrate.
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On binding to the enzyme, the substrate
disturbs the shape of the enzyme and causes
it to assume a new configuration.
It is this new configuration that is catalytically
active and affects the shape of the substrate,
thus lowering its activation energy.
This is referred to as an induced fit of the
substrate of the enzyme.
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COFACTOR
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COFACTORS
1. non protein substance
2. essential for some enzymes to function
efficiently.
3. may be bound tightly to the active site
as permanent residents
4. or they may bind loosely and reversibly
along with the substrate.
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Types of cofactors
Three types of cofactors
1. Activators
2. Coenzymes
3. Prosthetic group
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Activators (metal ions)
Substances which are necessary for the
functioning of the certain enzymes.
Enzyme thrombokinase,
prothrombin thrombin
during blood clotting
activated by calcium (Ca2+) ions.
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Salivary amylase
starch maltose
activated by chloride ( Cl- ) ions
These activators assist in forming the
enzyme- substrate complex by
moulding either the enzyme or
substrate molecule into a more suitable
shape.
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Coenzymes
non-protein organic substances which are
essential functioning of some enzymes,
but are not themselves bound to the
enzyme.
many coenzymes are derived from
vitamins.
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e.g.
nicotinamide adenine dinucleotide (NAD)
derived from nicotinic acid
a member of the vitamin B complex.
NAD acts as a coenzymes to
dehydrogenases by acting as a
hydrogen acceptor
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Prosthetic groups
organic molecules
bound to the enzyme
example: haem.
a ring- shaped organic molecule with iron at its center
an oxygen carrier in haemoglobin.
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Function of Cofactors
Work by binding briefly with the enzyme, they
sometimes alter its shape so that it can bind
more effectively with substrate
Sometimes help the enzyme to transfer a
particular group of atoms from one molecule to
another
Metal ions changing enzymes shape and
making it easier for substrate molecules to fit
into active site.
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Inhibition
reversible
and
irreversible
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Reversible Inhibitors
The effect of this type of inhibitor is temporary
Causes no permanent damage to the enzyme
The association of the inhibitor and enzyme is
a loose one
It can easily be removed
Removal of the inhibitor restores the activity of
the enzyme to normal
There are two types:
competitive inhibitors and
non-competitive inhibitors
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Competitive Inhibitors
It compete with the substrate for the active sites
The inhibitor may have structure with substrate
While it remains bound to the active site, it prevents a substrate molecule
from occupying that site and so reduces the rate of the reaction
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Competitive Inhibitors
The substrate continues to use any unaffected enzyme
The same quantity of product is formed
But take longer to make the products
Substrate and inhibitor are in direct competition
The greater the proportion of substrate, the greater their
chance of finding the active sites
If the concentration of the substrate is increased, less inhibition
occurs
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Non-Competitive Inhibitors
Not attach to the active site but elsewhere on the
enzyme molecule
They alter the shape of the enzyme
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Non-Competitive Inhibitors
Inhibitors and substrate are not competing for the
same sites
An increase in substrate concentration will not
therefore reduce the effect of the inhibitor.
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Non-Reversible Inhibitors
Inhibitors leave the enzyme permanently damaged
Enzyme unable to carry out its catalytic function
Heavy metal ions such as mercury (Hg 2+) and silver
(Ag + ) cause disulphide bonds to break
These bonds help to maintain the shape of the enzyme
molecule
Once broken the enzyme moleculeds structure
becomes irreversibly altered with the permanent loss of
its catalytic properties.
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Classification Of Enzymes
Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases
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The Classification Of Enzymes
Enzyme
group
Type of reaction
catalysed
Enzyme
examples
1.
Oxidoreductases
Transfer of O and H atoms
between substances, i.e. all
oxidation-reduction reactions.
Dehydrogenases
Oxidases
2. Transferases Transfer of a chemical group
from one substance to
another
Transaminases
Phosphorylases
3. Hydrolases Hydrolysis reactions Peptidases
Lipases
Phosphatases
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Enzyme
group
Type of reaction
catalysed
Enzyme
examples
4. Lyases Addition or removal of a
chemical group other than by
hydrolysis
Decarboxylases
5. Isomerases The rearrangement of groups
within a molecule
Isomerases
Mutases
6. Ligases Formation of bonds between
two molecules using energy
derived from the breakdown
of ATP
Synthetases