Enzymes:

“Helper” Protein molecules

Presented by
sarmad
bashir
 Chemical reactions of life
Processes of life
 building molecules
 synthesis +
 breaking down molecules
 digestion

+
 INTRODUCTION OF ENZYMES

These are the proteins produced by the cell, which

are capable of catalyzing a chemical reaction in a
living organism to yeild a specific product without
getting used up.
 It act as a biological catalyst
 They never initiate any reaction rather only
accelerate the pre existing reaction
 Catalyst and substrate

catalyst: These are the agents, which in minute

amount increase the velocity of a reaction without
appearing in the final products.
The compound on which enzymes acts is called its
substrate.
Products
on what the enzyme helps produce from the reaction
Active site
part of enzyme that substrate molecule fits into
 Basic information

The study of enzymes is called enzymology.

Enzymes are known to catalyze more than 5,000
biochemical reaction types. Most enzymes
are proteins, although a few are catalytic RNA
molecules. Enzymes' specificity comes from their
unique three-dimensional structures.
 It’s shape that matters!

Lock & Key model

 shape of protein allows
enzyme & substrate to fit
 specific enzyme for each
specific reaction
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 Nomenclature

Names of enzymes usually end in ase along with the

name of its specific substrate
I. Oxidoreductase
II. Transferase
III. Hydrolases
IV. Ligases
V. Lyase
VI. Isomerases
 Enzyme Specificity

Enzymes have varying degrees of specificity

for substrates
Enzymes may recognize and catalyze:
- a single substrate
- a group of similar substrates
- a particular type of bond
 APOENZYME and HOLOENZYME

The enzyme without its non protein moiety is

termed as apoenzyme and it is inactive.
Holoenzyme is an active enzyme with its non
protein component.
Difference between coenzymes and cofactors

Co-factors : They are non protein inoraganic

substances which are required for the enzymes for
their activity. usually are metals Fe, Zn, Mg
Co-Enzymes: They are non protein organic
substances usually the derivatives of vitamins
especially NAD, FAD
 Prosthetic group and isoenzymes

Prosthetic group : it is the tightly bound coenzymes

that does not dissociate the enzyme .
Isoenzymes and isozymes
These are enzymes that catalyzes the same reaction
i.e they have the same chemical properties but are
different in their structure.
 Properties of enzymes

They are protein in nature

Enzymes never initiate any reaction instead they
accelerate the pre-existing reaction.
They reduce the energy of activation
Enzymes molecules contain a specific cleft or pocket
called the active site . The active site contain amino
acid chain that create a 3 dimensional structural
surface complementary to the substrate.
 Properties of enzymes

Enzymes are highly specific interacting with one

or few substrates catalyzing only one type of
chemical reactions.
It accelerated the reaction 3 to 8 times faster than
un catalyzed reactions.
Enzymes activity can be regulated i.e they can be
inhibited or activated
activation energy : It is the minimum amount of
energy in calories/moles which is required by the
reactants to start the reaction.
 ENZYME ACTIVITY

The activity of an Enzyme is affected by

its environmental conditions. Changing
these alter the rate of reaction caused by the
enzyme. In nature,
organisms adjust the conditions of their enzymes
to produce an Optimum rate of reaction,
where necessary, or they may have enzymes which
are adapted to function well in extreme
conditions where they live.
 FACTORS EFFECTING THE ENZYME ACTIVITY

The six factors are:

(1) Concentration of Enzyme
(2) Concentration of Substrate
(3) Effect of Temperature
(4) Effect of pH
(5) Effect of Product Concentration
(6) Effect of Activators.
 Concentration of Enzyme

As the concentration of the enzyme is increased, the

velocity of the reaction proportionately increases . In
fact, this property of enzyme is made use in
determining the activities of serum enzymes for
diagnosis of diseases.
Aldolase ,cpk,GGT,
 Concentration of Substrate

Increase in the substrate concentration gradually

increases the velocity of enzyme reaction within the
limited range of substrate levels. A rectangular
hyperbola is obtained when velocity is plotted
against the substrate concentration 
 Effect of Temperature

Velocity of an enzyme reaction increases with increase

in temperature up to a maximum and then declines. 
The optimum temperature for most of the enzymes is
between 40°C-45°C. However, a few enzymes (e.g.
venom phosphokinases, muscle adenylate kinase) are
active even at 100°C. In general, when the enzymes
are exposed to a temperature above 50°C,
denaturation leading to derangement in the native
(tertiary) structure of the protein and active site are
seen. Majority of the enzymes become inactive at
higher temperature (above 70°C).
 Effect of pH

Increase in the hydrogen ion concentration (pH)

considerably influences the enzyme activity and a
bell-shaped curve is normally obtained. Most of the
enzymes of higher organisms show optimum activity
around neutral pH (6-8). There are, however, many
exceptions like pepsin (1-2), acid phosphatase (4-5)
and alkaline phosphatase (10-11) for optimum pH.
 Effect of Product Concentration

The accumulation of reaction products generally

decreases the enzyme velocity. For certain’ enzymes,
the products combine with the active site of enzyme
and form a loose complex and, thus, inhibit the
enzyme activity. In the living system, this type of
inhibition is generally prevented by a quick removal
of products formed.
 Effect of Activators.

Some of the enzymes require certain inorganic

metallic cations like Mg2+, Mn2+, Zn2+, Ca2+, Co2+,
Cu2+, Na+, K+ etc. for their optimum activity. Rarely,
anions are also needed for enzyme activity e.g.
chloride ion (CI–) for amylase.
Two examples of Enzyme Inhibitors
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a. Competitive inhibitors: are

chemicals that resemble an enzyme’s
normal substrate and compete with it
for the active site.

Substrate
Enzyme
Competitive inhibitor
 Inhibitors
b. Noncompetitive
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inhibitors:
Inhibitors that do not enter the
active site, but bind to another part
of the enzyme causing the enzyme to
change its shape, which in turn
alters the active site.
Substrate Noncompetitive
Enzyme Inhibitor
active site
altered