Enzyme - Assignment DR - Kashif

An Assignment by:-
Group # 10
S.no. Group Member Arid No.
1 Saqib Rasheed (Group Coordinator) 18-ARID-6152.

Group Members:
2 Muhammad Mahrban
1-Saqib Rasheed
3 Muhammad Naeem
4 Muhammad Shoaib
5 Usama Abdul Khaliq
6 Muhammad Naveed Sattar

Tuesday; February 19, 2019.
Created by: Saqib Rasheed Bhatti 1
03:29:17 PM
Enzyme
A Bio-catalyst.

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Definition & Introduction:-
• Biological chemicals which accelerate
biological reactions taking place in animal
bodies are called enzymes.
• With the exception of a small group of
catalytic RNA molecules, all enzymes are
protein in nature.
• More than 3000 enzymes are known today.
• They are very specific and one enzyme can
react only with a single substrate.

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• Enzymes can accelerate a reaction upto1017.
• They accelerate the reaction by lowering the

activation energy.
• The existence of enzymes has been known since

1835 by the Swedish chemist Jon Jacob
Berzelius.
• The first enzyme was obtained in pure form by

James B. Sumner of Cornell University.

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• They are high molecular weight and two
amino acids are linked together by a bond
called Peptide bond.

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Enzymes can be denatured and precipitated
with salts, solvents and other reagents.
They have molecular weights ranging from
10,000 to 2,000,000.
Co-factors:
It is a non-protein substance which is essential
for some enzymes to function efficiently.
Types:-
There are three types:
1) Activators
2) Coenzymes
3) Prosthetic groups
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Activators : Coenzymes : Prosthetic
groups :
These are substances These are non-protein
which are necessary for organic substances which These are organic , non-
the functioning of certain are essential to the efficient protein molecules and
enzymes. They may assist functioning of some bound to the enzyme
in forming the E -S enzymes, but are not themselves.
complex by molding themselves bound to the
either the enzyme or enzyme. Many coenzymes
substrate molecule into a are derived from vitamins.
more suitable shape.
• For example: Enzyme • For example: • For example:

thrombokinase, which Nicotinamide adenine Haem is an iron-
converts prothrombin dinucleotide (NAD) act containing prosthetic
into thrombin during as a coenzyme to group. It may function as
blood clotting, is dehydrogenases by electron carrier and
activated by Calcium acting as a hydrogen oxygen carrier in
ions. acceptor in the Krebs haemoglobin.
Cycle.

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Properties of enzyme :
1) It speeds up chemical reactions but remain undestroyed at the end of
the reaction. i.e. it has the catalytic properties.
2) It works in either direction. i.e. it catalysis the forward and backward
reaction to the same extent. The direction in which the reaction goes
depends on the relative amounts of substrate and products present.
The products are continuously removed to maintain the reaction in
living organism. e.g. A + B ↔ C + D
3) An enzyme changes the rate only at which chemical equilibrium is
reached; it does not affect the position of the equilibrium.
4) An enzyme speeds up the rate of reaction by lowering the activation
energy barrier.
5) It works rapidly and therefore is required in small quantity.

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6) It is soluble in water and works in aqueous solution in
living cells.
7) All enzymes operate only on specific substrates. Only

substrates of particular shape will fit the active site of
an enzyme.
8) All enzymes are proteins, some may have other

associated molecules.
9) Enzyme may be denatured by excessive heat, extreme

pH or various chemicals. This is because enzymes are
soluble proteins. Such extremities or chemicals cause
enzymes to coagulate by breaking down bonds in the
molecule making them insoluble.

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10) The activity of an enzyme is affected by
temperature.
11) Enzyme activity is affected by pH of the

medium. It worked best at an optimum pH.
12) Some enzymes work efficiently only in the

presence of appropriate co-factors.
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Specificity of Enzymes:-
One of the properties of enzymes that makes
them so important as diagnostic and research
tools is the specificity they exhibit relative to the
reactions they catalyze. A few enzymes exhibit
absolute specificity; that is, they will catalyze
only one particular reaction. Other enzymes will
be specific for a particular type of chemical bond
or functional group. In general, there are four
distinct types of specificity:
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1. Absolute specificity - the enzyme will catalyze
only one reaction.
2. Group specificity - the enzyme will act only
on molecules that have specific functional
groups, such as amino, phosphate and
methyl groups.
3. Linkage specificity - the enzyme will act on a
particular type of chemical bond regardless
of the rest of the molecular structure.
4. Stereo chemical specificity - the enzyme will
act on a particular steric or optical isomer. a

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Classification:-
1. Addition or removal of water:-
 Hydrolases - these include esterase, carbohydrases, nucleases, deaminizes, amidases, and
proteases.
 Hydrases such as fumarase, enolase, aconitase and carbonic anhydrase.
2. Transfer of electrons:-
 Oxidases
 Dehydrogenases
3. Transfer of a radical
 Transglycosidases - of monosaccharides
 Transphosphorylases and phosphomutases - of a phosphate group
 Transaminases - of amino group
 Transmethylases - of a methyl group
 Transacetylases - of an acetyl group
4. Splitting or forming a C-C bond
 Desmolases
5. Changing geometry or structure of a molecule.
 Isomerases
6. Joining two molecules through hydrolysis of pyrophosphate bond in
ATP or other tri-phosphate
 Ligases
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Enzyme Kinetics
Basic Enzyme Reactions:-
Enzymes are catalysts and increase the speed of a
chemical reaction without themselves undergoing
any permanent chemical change. They are neither
used up in the reaction nor do they appear as
reaction products. The basic enzymatic reaction can
be represented as follows:
S+E P+E
where E represents the enzyme catalyzing the reaction, S the
substrate, the substance being changed, and P the product of
the reaction.
03:29:17 PM
Energy Levels:-
Chemists have known for
almost a century that for most
chemical reactions to proceed,
some form of energy is needed.
They have termed this quantity
of energy, "the energy of
activation." It is the magnitude
of the activation energy which
determines just how fast the
reaction will proceed. It is
believed that enzymes lower
the activation energy for the
reaction they are catalyzing.
Following figure illustrates this
concept.
03:29:17 PM
The Enzyme Substrate Complex:-
A theory to explain the catalytic action of
enzymes was proposed by the Swedish chemist
Savante Arrhenius in 1888. He proposed that the
substrate and enzyme formed some
intermediate substance which is known as the
enzyme substrate complex. The reaction can be
represented as:
S+E ES
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• If this reaction is combined with the original
reaction equation , the following results:
E+S ES P+ E
The existence of an intermediate enzyme-substrate
complex has been demonstrated in the laboratory, for
example, using catalase and a hydrogen peroxide
derivative. At Yale University, Kurt G. Stern observed
spectral shifts in catalase as the reaction it catalyzed
proceeded. This experimental evidence indicates that
the enzyme first unites in some way with the substrate
and then returns to its original form after the reaction
is concluded.
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Chemical Equilibrium:-
The study of a large number of chemical reactions reveals that
most do not go to true completion. This is likewise true of
enzymatically-catalyzed reactions. This is due to the reversibility
of most reactions. In general:
A+B K+1 C + D (Forward Reaction)
C+D K-1 A + B ( Reverse Reaction)
where K+1 is the forward reaction rate constant and K-1 is the
rate constant for the reverse reaction.
Combining the two reactions gives:
A+B K+1 C+D
K-1

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Applying this general relationship to enzymatic
reactions allows the equation:
E+S K+1 ES K+2 P+E

K-1 K-2
Equilibrium, a steady state condition, is reached when the forward

reaction rates equal the backward rates. This is the basic equation upon
which most enzyme activity studies are based.

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Factors affecting the rate of
enzymatic reaction :
1- Temperature :-
1. If temperature is reduced to near or below
freezing point, enzymes are inactivated only,
not denatured. They will regain their catalytic
influence when higher temperature are
restored.
2. As the temperature increase, the kinetic
energy of the substrate and enzyme molecules
increases and so they move faster. The faster
these molecules move, the more often they
collide with one another and the greater the
rate of reaction.
3. As the temperature increases further, the more
the atoms which make up the enzyme
molecules vibrate. This breaks the hydrogen
bonds and other forces which hold the
molecules on their precise shape. So the shape
of the active site altered and no longer fit the
substrate. The enzyme is said to be denatured
and loses its catalytic activity forever.
03:29:17 PM
2-pH:-
1. Changes in pH alter the ionic charge
of the acidic and basic groups that
help to maintain the specific shape of
the enzyme i.e. break the hydrogen
bonds. The pH change leads to an
alternation in enzyme shape,
particularly at its active site. i.e.
enzyme denatured
2. Under constant temperature and
pressure, every enzyme has a narrow
pH range within which it will function
effectively. As the pH of reacting
medium increases above or falls
below the optimum pH, enzyme
activity decreases. At either extreme
of pH, the enzyme is denatured.
3. Different enzymes may have
different optimum pH.
03:29:17 PM
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4-Substrate Concentration:-
1. At low substrate concentrations, the active sites of the
enzyme molecules are not all used because there are
not enough substrate molecules to occupy them all.
2. As substrate concentration is increased, more and
more sites come into use.
3. When over the saturation point, a point where all
active sites are being occupied by substrates,
increasing the substrate concentration cannot increase
the rate of reaction. This is because any extra substrate
has to wait for the E-S complex dissociated into
products and free enzyme.
4. Therefore at high substrate levels, both enzyme
concentration and the dissociation time are the
limiting factors.
03:29:17 PM
5-Concentration of End-products:-
1. As the end-products accumulate, the pH of the
medium may change so that the rate of reaction
may also be changed.
2. In some enzymatic reactions, the enzyme itself
combines with one of the end product i.e. those
end-products will inhibit the activity of the
enzymes -- negative feedback. this may be due
to the shape of the product similar to that of the
substrate and therefore can fit into the active
sites of enzymes.
3. So, rate of enzymatic reaction decreases with
the accumulation of the end-products.
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6-Inhibition:-
A variety of small molecules exist which can reduce the rate of
an enzyme-controlled reaction. They are called enzyme
inhibitors. Inhibition may be reversible or irreversible.
1-Reversible inhibition :-
The inhibitor can be easily removed from the enzyme and cause
no permanent damage.
a) Competitive inhibitors:-
 compete with the substrates for the active sites of enzyme
molecules as they are structurally similar to the substrate.
 while remain in the active sites, they prevent access of the
true substrate.
 if the substrate concentration is increased, the rate of
reaction will be increased.
For example: Malonic acid --- It compete with succinate for the
active sites of succinic dehydrogenase, an important enzyme in
the Krebs Cycle.
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b) Non- Competitive inhibitors:-
They alter the shape of the enzyme in such a
way that the active site can no longer
properly accommodate the substrate.
increase the substrate concentration will not
therefore reduce the effect of the inhibitor
as they are not competing the same site.
but increase the inhibitor concentration will
decrease the reaction rate.
For example :
Cyanide --- attaches itself to copper prosthetic
group of cytochrome oxidase, thereby
inhibiting respiration.
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2-Irreversible inhibition:-
The inhibitor combines with the enzyme permanently
and so the enzyme unable to carry out its catalytic
function forever. Heavy metal ions such as mercury and
silver cause disulphide bonds to break. These bonds help
to maintain the shape of the enzyme molecule. Once
broken the enzyme molecule’s structure becomes
irreversibly altered with the permanent loss of its
catalytic properties.
For example: DFP (the nerve gas used in Second World
War) --- forms enzyme-inhibitor complex with the amino
acid serine at the active site of enzyme acetyl
cholinesterase. This enzyme deactivates the chemical
transmitter substance acetylcholine so that a normal
transmission of nerve impulse can be propagated. If this
enzyme is inhibited, paralysis or death will be the end
result.
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The application of enzymes :-
There are three main advantages of using enzymes
in industrial processes.
1) They are specific in their action and are
therefore less likely to produce unwanted by-
products.
2) They are biodegradable and therefore cause les
environmental pollution.
3) They work in mild conditions, i.e. low
temperatures, neutral pH and normal
atmospheric pressure, and are therefore energy-
saving.
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Common use of the enzymes :-
1-Biological washing powders :
 contain enzymes, usually proteases.
 remove 'biological' stains such as food, blood and
so on.
 as to reduce allergic reactions to man, the enzymes
are encapsulated in wax from which they are
released only when in the wash.
2-Meat tenderizers :
 contain protease, made by Bacillus subtilis.
 as the main component of meat is protein, so the
protease may digest some peptide bonds of the
meat, this tenderizes the meat.
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Other Applications:-

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Enzyme - Assignment DR - Kashif

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An Assignment by:-

1 Saqib Rasheed (Group Coordinator) 18-ARID-6152.

5 Usama Abdul Khaliq

6 Muhammad Naveed Sattar

Tuesday; February 19, 2019.

Tuesday; February 19, 2019.

• They accelerate the reaction by lowering the

• The existence of enzymes has been known since

• The first enzyme was obtained in pure form by

Tuesday; February 19, 2019.

Tuesday; February 19, 2019.

• For example: Enzyme • For example: • For example:

Tuesday; February 19, 2019.

Tuesday; February 19, 2019.

7) All enzymes operate only on specific substrates. Only

8) All enzymes are proteins, some may have other

9) Enzyme may be denatured by excessive heat, extreme

Tuesday; February 19, 2019.

11) Enzyme activity is affected by pH of the

12) Some enzymes work efficiently only in the

Tuesday; February 19, 2019.

Tuesday; February 19, 2019.

E+S K+1 ES K+2 P+E

Equilibrium, a steady state condition, is reached when the forward

Tuesday; February 19, 2019.

Tuesday; February 19, 2019.

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