FIRST YEAR BIOLOGY NOTE

WRITTEN AND COMPOSED BY Dr. Farhad

Cell: 03335014892
 Chapter 3

ENZYMES
METABOLISM
Sum up all the chemical reactions occur inside the body is called
metabolism. Metabolic reactions are also termed as biochemical
reactions or vital activities. Metabolism is of two types.
Anabolism
That type of chemical reactions in which large molecules are formed is
called anabolism.
Example
Photosynthesis
Catabolism
That type of chemical reactions in which large molecules are formed is
called anabolism.
Example
Respiration
ENZYMES

(En-in and Zyme – yeast)

History
A Swedish scientist Jon Jakob was the first to discover enzymes in
1835. The term "enzyme" was coined in 1877 by Wilhelm Kuhne.
Diastase (a mixture of amylases) was the first enzyme to be
discovered in 1833.
Definitions
1. Enzymes are biocatalyst synthesized inside the cells that alter
(speed up 103–108 times) the biochemical reactions without getting
involved itself in the chemical reaction.
2. Enzymes are simple or compound proteins or nucleic acids which
catalyzed biochemical reactions.
3. Enzyme are biocatalyst of the living system.
STRUCTURE OF ENZYME

Enzymes are proteins that are made up of several polypeptide chains,

also known as amino acids that have been folded and coiled numerous
times.
They have three-dimensional structures. Enzyme has a specific site on
its surface called active site.
Active site
The site on enzyme surface to which substrate is attached is called
active site. Active site is charge bearing site.

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 This site is formed of few amino acids. Active site has two portions.
1. Binding site: It is only involved in linkage formation with substrate.
2. Catalytic site: This site acts upon substrate and converts it into
products.
Allosteric site
The site other than active site is called allosteric site.

CHEMICAL NATURE OF ENZYME

Most of the enzymes are composed of simple proteins or complex
proteins. Some enzymes are also formed of nucleic acids.
Simple protein enzymes
Simple protein enzyme are only proteinaceous in nature.
Complex protein enzymes
Complex protein enzymes are called holoenzymes. Holoenzymes are
formed of two components.
1. Protein part (called apoenzyme)
2. Nonprotein part (called cofactors)
Cofactor is again classified into three groups.
(a) Prosthetic group
These are organic compounds which tightly attached to the
apoenzymes.
Examples: FAD (Flavine Adenine Dinucleotide),
(b) Coenzymes
These are also organic compounds but loosely attached to the
apoenzyme.
Examples: NAD (Nicotinamide adenine dinucleotide), NADP
(Nicotinamide adenine dinucleotide phosphate), CO-A, Vitamin B
biotin, folic acids etc.
(c) Metallic activators
These are metals which may be loosely or tightly attached to
apoenzymes and enhance their catalytic property.

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 Examples: K+, Fe2+, Fe3+, Cu2+, Co2+, Zn2+, Mn2+, Mg2+, Ca2+, and
Mo3+ etc.
Ribozymes
A few enzymes are catalytic RNA segments. Catalytic RNA
segments/molecules are called ribozymes.
Enzyme unit or activity
One unit of enzyme activity is the amount of enzyme that converts 1.0
M of the substrate per minute into the products at 25oC.

ENDOEZYME AND ECTOENZYME

Endoenzymes (intracellular enzymes)

Enzymes which are synthesized inside the cell and operate or utilized
there where they are synthesized are called endoenzymes.
Examples:
Respiratory enzymes
Exoenzymes (extracellular enzymes)
Enzymes which are synthesized inside the cell and operate or utilized
in other place or outside the cell are called endoenzymes.
Examples:
Photosynthetic enzymes

ZYMOGENE OR PROENZYMES

Zymogene or proenzymes are inactive enzyme which are activated

when required.
Examples:
Pepsinogen Pepsin
Trypsinogen Trypsin

ISOZYMES OR ISOENZYMES OR ALLOZYMES

ISOZYMES
Isoenzymes are enzymes that differ in amino acid sequence but
catalyze the same chemical reaction. They are also known as isozymes
or multiple form or allozymes.
The enzymes which are different structurally but catalyzed the same
chemical reaction are called isozymes.
Isoenzymes are produced as a result of mutation or due to allelic form
of genes.
Examples:
Alkaline phosphatase present in six different forms.
1. α1- ALP,
2. α2-heat labile ALP

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 3. α2-heat stable ALP
4. pre-β ALP
5. γ-ALP.

ENZYME NOMENCLATURE
Enzymes are named according to the type of reaction they catalyze
and/or their substrate by adding the suffix “-ase.
Examples:
Urea -----urease (substrate specific)
Lipids ----- lipase (substrate specific)
Proteins ----- protease (substrate specific)
Oxidation ----- oxidase (reaction specific)
Reduction ------ reductase (reaction specific) etc.
Not all enzymes have been named through this type of naming system.
Some enzyme are exceptional.
Examples:
Pepsin, Trypsin etc.

CLASSIFICATION OF ENZYMES

The enzymes are classified into six groups based on the bases of
reaction they catalyzed.
Oxidoreductases
Catalyze oxidation-reduction reactions involving electron or hydrogen
transfer between molecules.
Examples:
Dehydrogenases, peroxidases and oxygenases etc.
Transferases
Transfer functional groups like methyl, amino, and phosphate groups
between substrates.
Examples
Kinases, transaminases and transmethylases etc.
Hydrolases
Catalyze hydrolysis reactions that cleave bonds using water.
Examples
Proteases, lipases and phosphatases etc.
Lyases
Catalyze non-hydrolytic addition or removal of groups from substrates.
Examples
Decarboxylases and dehydratases etc.
Isomerases
Catalyze structural rearrangements within a single molecule.
Examples
Epimerases.

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Ligases
Catalyze bond formation between substrates by condensation
reactions coupled to ATP hydrolysis.
Examples
DNA ligase and acetyl CoA synthetase etc.

MODE OF ACTION OF ENZYME

Mode of action of enzymes can be explained under the following heads.
1. Formation of enzyme substrate complex
Following two important models are present to explain the enzyme-
substrate complex formation.
(a) Lock and key model
(b) Induce fit model
(a) Lock and Key Model
Lock and key hypothesis was proposed by Emil Fischer in the 1890. It
is also known as the template model. According to this model active
site of enzyme has rigid structure which allow to make complex with
specific substrate. The active site of the enzyme is complementary in
conformation to the substrate, so that enzyme and substrate recognize
each other.

(b) Induce Fit Model

Induce fit model was Proposed by Daniel Koshland in 1958. According
to this model active site of enzyme has flexible structure and
conformational changes occur during complex formation with
substrate. Likewise when we put our hand in gloves, its structure
transforms into the shape of our hands.

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2. Reaction mechanism
In any chemical reaction, a substrate is changed into product.
Substrate ---------- Product
When an enzyme combines with substrate, they form enzyme
substrate complex.
Enzyme + Substrate ------- Enzyme- Substrate Complex
Enzyme acts on substrate and changes it into products and enzyme is
released and used again.
Enzyme – substrate complex ------- Product + Enzyme
3. Molecular geometry
Once when substrate molecule makes complex with enzyme, enzyme
shape slightly changes which undergo distorting the substrate
molecules. In this way enzyme changes the substrate into products.
4. Energy changes

Activation Energy
Activation energy is minimum amount of energy which is required to
initiate a chemical reaction.
All chemical reactions have an energy barrier separating the reactants
and the products.
This barrier, called the free energy of activation, is the energy
difference between that of the reactants and a high-energy
intermediate that occurs during the formation of product.
For molecules to react, they must contain sufficient energy to
overcome the energy barrier of the transition state.
Enzyme accelerates the rate of reaction by lowering the free energy of
activation.

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 FACTOR AFFECTS OF ENZYME ACTIVITY
Following are some factors that affect enzyme activity.
Effect of Temperature
The degree of hotness or coldness is called temperature. There are
three different types of temperature which effect negatively or
positively the enzyme activity.
1. Optimum temperature
This is the temperature at which enzyme show maximum activity. Most
of the enzymes works efficiently in animal (mammals) at 40 oC. For
thermophilic bacteria optimum temperature is 90 oC. In arctic snow flea
works enzymes at -10oC.
2. Maximum temperature
As the temperature proceeds beyond the optimum temperature
enzyme activity decreases. At maximum temperature enzyme shows
minimum activity.
Denaturation of enzymes: When temperature is increased from
maximum level, three dimensional structure of enzyme is altered
and they lose their catalytic activities. This is called denaturation
of enzyme.
3. Minimum temperature
When temperature decreases below the optimum level, enzyme
activity also decreases. At very low temperature crystals formation
occur which stop thee biological activity.

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Effect of pH
Enzymes works efficiently at optimum pH. Most of the enzyme work
best at pH ranges from 7-8. Some enzyme work best in acidic
conditions i.e. protease enzyme in stomach work best at pH – 1.
Change the pH of the medium decrease the enzyme activities.

Effect of substrate concentration

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 Increase in enzyme concentration enhances enzyme activity. But when
all the available active of enzymes are saturated no effect is detected
furthermore. This point at which no increase occur is called [Link].

Effect of enzyme concentration

Increase in enzyme concentration directly proportional to enzyme
activity. As the enzyme concentration increases rate of reaction also
increases. It also depends upon the mutual equivalency of substrates
and enzymes.

INHIBITORS
Inhibitors
Chemicals or poisons which stop or decrease the enzymatic activity are
called inhibitors and the phenomena is called inhibition.
Types of inhibition
There are two basic types of inhibitions.
1. Reversible inhibition
2. Irreversible inhibition
1. Reversible inhibition
Reversible enzyme inhibition is a type of enzyme inhibition in which
inhibitor molecules bind to the enzyme through non-covalent
interactions. In this type of inhibition enzyme activity decreases.
There are three types of reversible enzyme inhibition i.e. competitive,
non-competitive and uncompetitive.

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 (a) Competitive inhibition
That type of inhibition in which both inhibitor and substrate compete
for active site is called competitive inhibition.
Example:
(b) Noncompetitive inhibition
That type of inhibition in which the inhibitors are attached other than
active site. In this case inhibitors do not compete with substrates.
Examples:
Various heavy metal ions (Ag+, Hg2+, Pb2+), cyanide and
insecticide etc.
(c) Uncompetitive inhibition
Uncompetitive inhibition is the inhibition of enzymatic activity by the
binding of the inhibitor at an allosteric site like in the case of
noncompetitive inhibition but the binding takes place with the enzyme-
substrate (ES) complex, and not the free enzyme molecule.
Examples:
Tetramethylene sulfoxide and 3-butylthiolene oxide

2. Irreversible inhibition
That type of inhibition in which the enzyme activity is permanently
stopped by destroying or denature the structure of enzymes. The
inhibitors attached to the enzyme covalently and the inhibition cannot
be reversed by the addition of excess substrate.
Example: Diisopropyl fluorophosphate (DIFP)

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 ALLOSTERIC AND FEED BACK INHIBITION
Allosteric inhibition
Inhibition in which the inhibitors bind to allosteric site (other than
active site) is called allosteric inhibition.

Feedback inhibition (End product inhibition)

That type of inhibition in which the product of enzymatic activity back
inhibits the enzyme activity.

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