BIOMOLECULES &

ENZYMES
1. BIO-MOLECULES :

■ DEFINITION :
■ Biomolecules are the most essential organic molecules, which are involved in
the maintenance and metabolic processes of living organisms. These non-living
molecules are the actual foot-soldiers of the battle of sustenance of life. They
range from small molecules such as primary and secondary metabolites and
hormones to large macromolecules like proteins, nucleic acids, carbohydrates,
lipids etc.
■ TYPES :
■ There are four major classes of Biomolecules – Carbohydrates, Proteins,
Nucleic acids and Lipids.
2. CARBOHYDRATES :

■ DEFINITION :
■ Carbohydrates are macronutrients and are one of the three main ways by which our
body obtains its energy. They are called carbohydrates as they comprise of carbon,
hydrogen, and oxygen at their chemical level. Carbohydrates are essential nutrients
which include sugars, fibers, and starches.
■ SOURCE :
■ They are found in grains, vegetables, fruits, and in milk and other dairy products.
They are the basic food groups which play an important role in a healthy life.
■ CLASSIFICATION :
■ The carbohydrates are further classified into simple and complex which is mainly
based on their chemical structure and degree of polymerization.
 2. CARBOHYDRATES :
■ SIMPLE CARBOHYDRATE :
■ Simple carbohydrates have one or two sugar molecules.
In simple carbohydrates, molecules are digested and
converted quickly resulting in a rise in the blood sugar
levels.
■ They are abundantly found in milk products, beer, fruits,
refined sugars, candies, etc.
■ These carbohydrates are called as empty calories, as
they do not possess fiber,vitamins and minerals.
1. MONOSACCHARIDES :
■ Glucose is an example of a carbohydrate monomer or
monosaccharide. Other examples of monosaccharides
include mannose, galactose, fructose, etc.
 2. CARBOHYDRATES :
■ Monosaccharides may be further classified depending
on the number of carbon atoms:
1. Trioses (C3H6O3): These have three carbon atoms
per molecule. Example: Glyceraldehyde.
2. Tetroses (C4H8O4): These monosaccharides have
four carbon atoms per molecule. Example: Erythrose.
3. Pentoses (C5H10O5): These monosaccharides have
five carbon atoms per molecule. Example : Ribose.
4. Hexoses (C6H12O6): These have six carbon atoms
per molecule. Example : Glucose.
5. Heptoses (C7H14O7): These have seven carbon
atoms per molecule. Example : Sedoheptulose.
2. CARBOHYDRATES :

2. DISACCHARIDES :
■ Two monosaccharides combine to form a
disaccharide.
■ Examples of carbohydrates having two
monomers include- Sucrose, Lactose,
Maltose, etc.
3. OLIGOSACCHARIDES :
■ Carbohydrates formed by the
condensation of 2-9 monomers are
called oligosaccharides.
■ By this convention, trioses, pentoses,
hexoses are all oligosaccharides.
2. CARBOHYDRATES :

■ COMPLEX CARBOHYDRATES (POLYSACCHARIDES):

■ Complex carbohydrates have two or more sugar molecules, hence they are referred
to as starchy foods. In complex carbohydrates, molecules are digested and
converted slowly compared to simple carbohydrates.
■ They are abundantly found in lentils, beans, peanuts, potatoes, peas, corn, whole-
grain bread, cereals, etc.
■ Polysaccharides are complex carbohydrates formed by the polymerization of a large
number of monomers.
■ Examples of polysaccharides include starch, glycogen, cellulose, etc. which exhibit
extensive branching and are homopolymers – made up of only glucose units.
2. CARBOHYDRATES :

■ FUNCTIONS OF CARBOHYDRATES :
■ The main function of carbohydrates is to provide energy and food to the body and
to the nervous system.
■ Carbohydrates are known as one of the basic component of food including sugars,
starch, and fibre which are abundantly found in grains, fruits, and milk products.
■ Carbohydrates are also known as starch, simple sugars, complex carbohydrates and
so on.
■ It is also involved in fat metabolism and prevents ketosis.Inhibits the breakdown of
proteins for energy as they are the primary source of energy.
■ An enzyme by name amylase assists in the breakdown of starch into glucose,
finally to produce energy for metabolism.
3. PROTEINS :

■ DEFINITION :
■ Basically, proteins are the fundamental
building blocks of our body. They are large
and complex macromolecules or bio-
molecules which perform a major role in
the functioning and regulating of our body
cells, tissues and other organs in the
human body.
■ They are also used in providing strength to
our body in producing hormones, enzymes,
and other metabolic chemicals.
■ They are also involved in functioning and
regulating of our body cells, tissues and
organs.
3. PROTEINS :

■ Proteins are composed of amino acids, arranged into different groups. These
fundamental amino acids sequences are specific and its arrangements are
controlled by the DNA.
■ Since our body cannot synthesize these essential amino acids by its own, we
should have plenty of protein foods in our everyday diet to keep our body
metabolisms stable.
■ PROTEIN STRUCTURE :
■ In general, they are two types of protein molecules fibrous proteins and globular
proteins. Fibrous proteins are insoluble and elongated. Globular proteins are
soluble and compact. Fibrous and Globular proteins may comprise one or four
types of protein structures and they include primary, secondary, tertiary and
quaternary structure.
 3. PROTEINS :
1. PRIMARY STRUCTURE: It is a specific sequence of
amino acids. The order of amino acids bonded
together is detected by information stored in genes.
2. SECONDARY STRUCTURE: It is a three-dimensional
form of a local segment of proteins. They are formed
by hydrogen bonds between the atoms along the
backbone of the polypeptide chain.
3. TERTIARY STRUCTURE: It is determined by R-groups.
It is a three-dimensional shape of a protein. Many
numbers of tertiary structure fold to form Quaternary
Structure.
4. QUATERNARY STRUCTURE: It is the arrangement of
multiple folded protein subunits in a multi-subunit
complex.
3. PROTEINS :

■ SOURCE :
■ The most common food which has a higher amount of protein are eggs, almond,
chicken, oats, fish and seafood, soy, beans and pulses, cottage cheese, Greek
yogurt, milk, broccoli, and quinoa.
■ FUNCTIONS OF PROTEINS:
1. ENZYMES: Enzymes mostly carry out all numerous chemical reactions which take
place within a cell. They also help in regenerating and creating DNA molecules and
carry out complex processes.Hormones: Proteins are involved in the creation of
various types of hormones which help in balancing the components of the body.
For example hormones like insulin, which helps in regulating blood sugar and
secretin. It is also involved in the digestion process and formation of digestive
juices.
 3. PROTEINS :
2. ANTIBODY: Antibody also known as an
immunoglobulin. It is a type of protein which is
majorly used by the immune system to repair
and heal the body from foreign bacteria. They
often work together with other immune cells to
identify and separate the antigens from
increasing until the white blood cells destroy
them completely.
3. ENERGY: Proteins are the major source of
energy that helps in the movements of our
body. It is important to have the right amount
of protein in order to convert it into energy.
Protein, when consumed in excess amounts,
gets used to create fat and becomes part of
the fat cells.
4. LIPIDS :

■ DEFINITION:
■ These organic compounds are nonpolar
molecules, which are soluble only in nonpolar
solvents and insoluble in water because water is
polar molecules.
■ SOURCE:
■ In the human body, these molecules can be
synthesized in the liver and are and generally
found in the oil, butter, whole milk, cheese, fried
foods, and also in some red meats.
■ CLASSIFICATION OF LIPIDS :
■ Lipids can be classified into two major classes:
4. LIPIDS :

■ NON SAPONIFIABLE LIPIDS :

■ A non saponifiable lipid cannot be broken up into smaller molecules by hydrolysis,
which includes triglycerides, waxes, phospholipids, and sphingolipids.
■ SAPONIFIABLE LIPIDS :
■ A saponifiable lipid contains one or more ester groups allowing it to undergo
hydrolysis in the presence of an acid, base, or enzymes.
■ Nonsaponifiable lipids include steroids, prostaglandins, and terpenes.
■ Each of these categories can be further broken down into non-polar and polar lipids.
Nonpolar lipids, such as triglycerides, are used for energy storage and fuel.Polar
lipids, which can form a barrier with an external water environment, are used in
membranes.
4. LIPIDS :

■ Polar lipids include glycerophospholipids and sphingolipids.

■ Fatty acids are important components of all of these lipids.
■ TYPES OF LIPIDS :
■ Within these two major classes of lipids, there are several
specific types of lipids important to live, including fatty acids,
triglycerides, glycerophospholipids, sphingolipids, and
steroids.
■ These are broadly classified as simple lipids and complex
lipids.
1. SIMPLE LIPIDS :
■ Esterss of fatty acids with various alcohols.
■ Fats: Esters of fatty acids with glycerol. Oils are fats in the
liquid state.
4. LIPIDS :

■ Waxes: Esters of fatty acids with higher molecular weight monohydric alcohols.
2. COMPLEX LIPIDS :
■ Esters of fatty acids containing groups in addition to alcohol and a fatty acid.
■ Phospholipids: Lipids containing, in addition to fatty acids and alcohol, a
phosphoric acid residue. They frequently have nitrogen-containing bases and
other substituents, eg, in glycerophospholipids the alcohol is glycerol and in
sphingophospholipids the alcohol is sphingosine.
■ Glycolipids (glycosphingolipids): Lipids containing a fatty acid, sphingosine, and
carbohydrate.
4. LIPIDS :

■ Other complex lipids: Lipids such as sulfolipids and amino lipids. Lipoproteins may
also be placed in this category.
3. PRECURSOR AND DERIVED LIPIDS :
■ These include fatty acids, glycerol, steroids, other alcohols, fatty aldehydes, and
ketone bodies, hydrocarbons, lipid-soluble vitamins, and hormones. Because they
are uncharged, acylglycerols (glycerides), cholesterol, and cholesteryl esters are
termed neutral lipids. These compounds are produced by the hydrolysis of simple
and complex lipids.
■ SOME IMPORTANT LIPIDS :
■ FATTY ACIDS : Fatty acids are carboxylic acids (or organic acid), often with long
aliphatic tails (long chains), either saturated or unsaturated.
 4. LIPIDS :
■ SATURATED FATTY ACIDS : When a fatty acid is saturated it is an
indication that there are no carbon-carbon double bonds. The
saturated fatty acids have higher melting points than unsaturated
acids of the corresponding size due to their ability to pack their
molecules together thus leading to a straight rod-like shape.
■ UNSATURATED FATTY ACIDS : If a fatty acid has more than one
double bond then this is an indication that it is an unsaturated fatty
acid.
■ Most naturally occurring fatty acids contain an even number of
carbon atoms and are unbranched.
■ Unsaturated fatty acids, on the other hand, have a cis-double bond(s)
that create a kink in their structure which doesn’t allow them to
group their molecules in straight rod-like shape.
4. LIPIDS :
■ WAXES : Waxes are “esters” (an organic compound
made by replacing the hydrogen with acid by an alkyl
or another organic group) formed from long-chain
carboxylic acids and long-alcohols.
■ Waxes are seen all over in nature. The leaves and
fruits of many plants have waxy coatings, which may
protect them from dehydration and small predators.
■ The feathers of birds and the fur of some animals
have similar coatings which serve as a water
repellent.
■ PHOSPHOLIPIDS: Membranes are chiefly made of
phospholipids which are Phosphoacylglycerols.
 4. LIPIDS :
■ Triacylglycerols and phosphoacylglycerols are similar however
the terminal OH group of the phosphoacylglycerol is esterified
with phosphoric acid instead of fatty acid which leads to the
formation of phosphatidic acid.
■ The name phospholipid comes from the fact that
phosphoacylglycerols are lipids that contain a phosphate group.
■ STEROIDS : Steroids are a type of hormone which is usually
recognized by their tetracyclic skeleton, consisting of three
fused six-membered and one five-membered ring, as shown in
the diagram above. The four rings are designated as A, B, C & D
as noted in blue, and the numbers in red represent the carbons.
■ CHOLESTEROL : Cholesterol is waxy like substance, found only
in animal source foods.
4. LIPIDS :

■ Triglycerides, LDL, HDL, VLDL are different types of cholesterol found in the blood
cells.Cholesterol is an important lipid found in the cell membrane. It is a sterol,
which means that cholesterol is a combination of steroid and alcohol. In the human
body, cholesterol is synthesized in the liver.
■ These compounds are biosynthesized by all living cells and are essential for the
structural component of the cell membrane.In the cell membrane, the steroid ring
structure of cholesterol provides a rigid hydrophobic structure that helps boost the
rigidity of the cell membrane.
■ Without cholesterol, the cell membrane would be too fluid.It is an important
component of cell membranes and is also the basis for the synthesis of other
steroids, including the sex hormones estradiol and testosterone, as well as other
steroids such as cortisone and vitamin D.
4. LIPIDS :

■ FUNCTIONS:
1. Fats incorrect amounts are necessary for the proper functioning of our body.
2. Many fat-soluble vitamins need to be associated with fats in order to be
effectively absorbed by the body.
3. They also provide insulation to the body.
4. They are an efficient way to store energy for longer periods.
5. NUCLEIC ACID :

■ DEFINITION :
■ A nucleic acid is a linear polymer of nucleotides which form an integral part of the
information transfer system in cells. Examples of nucleic acids are DNA
(Deoxyribonucleic acid) and RNA (Ribonucleic acid). In order to study the structure
of a nucleic acid, it is essential to study the structure of its monomer. Nucleotides
are made up of a sugar molecule, a nitrogenous base, and a phosphate group.
■ COMPONENTS :
1. NUCLEIC ACID AND SUGAR MOLECULES : The sugar molecule in nucleotides could
be either ribose (C5H10O5) or deoxyribose (C5H10O4) and both the sugars are in
their Pentagon or furanose state.
 5. NUCLEIC ACID :

2. NITROGENOUS BASE: A nucleotide consists of a nitrogenous

base which could be either purine or pyrimidine. There are two
purine bases-Adenine (A) and Guanine (G) whereas pyrimidines
are of three types- Thymine (T), cytosine (C) and Uracil (U).
3. PHOSPHATE GROUP: When a phosphate group is added to a
nucleoside (one sugar molecule plus one nitrogenous base), it
forms a nucleotide.
■ DEOXYRIBOSE NUCLEIC ACID (DNA) :
■ Genes carry genetic information from one generation to the
other. The structure of nucleic acids such as DNA consists of a
long polymer of nucleotides connected by phosphodiester
bonds.
■ In the case of DNA, the nucleotides are deoxynucleotides. The
most widely accepted structure of DNA (right-handed double-
helix) was proposed by Watson and Crick in 1963.
5. NUCLEIC ACID :

■ The nitrogenous bases present in DNA are Adenine, Guanine, Thymine, and
Cytosine.
■ This suggests that there are four different types of deoxyribonucleotides in DNA-
deoxyadenosine monophosphate (dAMP), deoxyguanosine monophosphate (dGMP)
, deoxythymidine monophosphate (dTMP) and deoxycytidine monophosphate
(dCTP).
■ The two strands of the DNA helix are antiparallel to each other exhibiting
complementary pairing between two specific bases. Adenine pairs with thymine
(A=T), while guanine pairs with cytosine (G≡C).
■ If we imagine the structure of DNA in the form of a staircase model, the
complementary base pairs will form the stairs and the sugar-phosphate backbone
will form the stair railings.
 5. NUCLEIC ACID :
■ RIBONUCLEIC ACID (RNA) :
■ Ribonucleic acid is an example of the nucleic acid formed by
the polymerization of ribonucleotides.
■ It is a single-stranded chain formed by 7-12000
ribonucleotides.
■ This structure of nucleic acid contains ribose sugar, a
phosphate group, and a nitrogen base. The nitrogenous bases
in RNA are Adenine, Guanine, Cytosine, and Uracil (U). RNA is
formed from DNA by the process of transcription and is
generally involved in protein synthesis.
■ TYPES OF RNA:
■ Ribosomal RNA (rRNA), Transfer RNA (tRNA) and Messenger
RNA (mRNA).
5. NUCLEIC ACID:

■ FUNCTIONS :
■ DNA is the genetic material carrying hereditary information.
■ By the process of transcription, it gives rise to RNA which in turn contains the
code for the synthesis of proteins.
■ DNA controls cell metabolism along with differentiation and development of an
organism.
■ Mutations in DNA help organisms evolve and adapt to changing conditions.RNA
forms the genetic code in certain viruses such as HIV.
6. ENZYMES :

■ DEFINITION :
■ Enzymes can be defined as biological polymers that catalyze biochemical reactions.
■ The vast majority of enzymes are proteins with catalytic capabilities that are
essential for maintaining various life processes.
■ Metabolic processes and other chemical reactions in the cell are carried out by a
set of enzymes that are necessary to sustain life.The initial stage of metabolic
process depends upon the enzymes, which react with a molecule and is called the
substrate. Enzymes convert the substrates into other distinct molecules and are
called the products.
■ The regulation of enzymes has been a key element in clinical diagnosis because of
their role in maintaining life processes.
6. ENZYMES :

■ The macromolecular component of all enzymes consists of protein, except in the

class of RNA catalysts called ribozymes.
■ The word ribozyme is derived from the ribonucleic acid enzyme. Many ribozymes
are molecules of ribonucleic acid which catalyze reactions in one of their own
bonds or among other RNAs.
■ Enzymes exist in all fluids and tissues of the body. Intracellular enzymes catalyze
all the reactions that occur in metabolic pathways.
■ The enzymes in plasma membrane regulate catalysis in the cells in response to
cellular signals and enzymes in the circulatory system regulate clotting of blood.
Almost all the significant life processes are based on the enzyme functions.
6. ENZYMES :

■ Enzymes exist in all fluids and tissues of the body. Intracellular enzymes catalyze
all the reactions that occur in metabolic pathways.
■ The enzymes in plasma membrane regulate catalysis in the cells in response to
cellular signals and enzymes in the circulatory system regulate clotting of blood.
Almost all the significant life processes are based on the enzyme functions.
■ STRUCTURE:
■ Enzymes are a linear chain of amino acids that generate the three-dimensional
structure. The sequence of amino acids enumerates the structure, which in turn
identifies the catalytic activity of the enzyme.
■ The structure of the enzyme denatures when heated, leading to loss of enzyme
activity, which is typically connected to the temperature.
6. ENZYMES :

■ Enzymes are larger than their substrates, and their size varies, which range
from sixty-two amino acid residues to an average of two thousand five hundred
residues present within fatty acid synthase.
■ Only a small section of the structure is involved in catalysis and are situated
next to binding sites. The catalytic site and binding site together constitute the
enzyme’s active site.
■ A small number of ribozymes exists which serves as an RNA-based biological
catalyst. It reacts in complex with proteins.
6. ENZYMES :

■ TYPES OF ENZYMES :
■ Earlier, enzymes were assigned names based on the one who discovered it. With
further researches, classification became more comprehensive.
■ According to the International Union of Biochemists (I U B), enzymes are divided
into six functional classes and are classified based on the type of reaction in which
they are used to catalyze.
■ The six types of enzymes are oxidoreductases, hydrolases, transferases, lyases,
isomerases, ligases.
1. OXIDOREDUCTASES :The enzyme Oxidoreductase catalyzes the oxidation reaction
where the electrons tend to travel from one form of a molecule to the other.
6. ENZYMES :

2. TRANSFERASES : The Transferases enzymes help in the transportation of the

functional group among acceptors and donors molecules.
3. HYDROLASES : Hydrolases are hydrolytic enzymes, which catalyze the hydrolysis
reaction by adding water to cleave the bond and hydrolyze it.
4. LYASES : Adds water, carbon dioxide or ammonia across double bonds or
eliminate these to create double bonds.
5. ISOMERASES : The Isomerases enzymes catalyze the structural shifts present in a
molecule, thus causing the change in the shape of the molecule.
6. LIGASES : The Ligases enzymes are known to charge the catalysis of a ligation
process.
6. ENZYMES :

■ COFACTORS:
■ Cofactors are non-proteinous substances that associate with enzymes. A cofactor is
essential for the functioning of an enzyme. An enzyme without a cofactor is called an
apoenzyme. An apoenzyme and its cofactor together constitute the holoenzyme.
■ There are three kinds of cofactors present in enzymes:
■ PROSTHETIC GROUPS: These are cofactors tightly bound to an enzyme at all times. A fad
is a prosthetic group present in many enzymes.
■ COENZYME: A coenzyme is bound to an enzyme only during catalysis. At all other times,
it is detached from the enzyme. NAD+ is a commoncoenzyme
■ METAL IONS: For the catalysis of certain enzymes, a metal ion is required at the active
site to form coordinate bonds. Zn2+ is a metal ion cofactor used by a number of enzymes.
 6. ENZYMES :
■ MECHANISM OF ENZYME REACTION
■ The basic mechanism of enzyme action is to catalyze the
chemical reactions, which begins with the binding of the substrate
with the active site of the enzyme. This active site is a specific
area that combines with the substrate.
■ Enzyme Substrate Interactions : Enzymes are the Enzymes are the
biocatalysts with high molecular weight proteinous compound. It
enhances the reactions which occur in the body during various life
processes. It helps the substrate by providing the surface for the
reaction to occur.
■ The enzyme comprises hollow spaces occupying groups such as -
SH, -COOH, and others on the outer surface. The substrate which
has an opposite charge of the enzyme fits into these spaces just
like a key fits into a lock. This substrate binding site is called the
active site of an enzyme (E).
6. ENZYMES :

■ The favourable model of enzyme-substrate interaction is called the Induced-fit

Model.
■ This model states that the interaction between substrate and enzyme is weak,
and these weak interactions induce conformational changes rapidly and
strengthen binding and bring catalytic sites close enough to substrate bonds.
■ There are four possible major mechanisms of catalysis:
1. Catalysis By Bond Strain: The induced structural rearrangements in this type
of catalysis produce strained substrate bonds that attain transition state more
easily. The new conformation forces substrate atoms and catalytic groups like
aspartate into conformations that strain substrate bonds.
6. ENZYMES :

2. COVALENT CATALYSIS : The substrate is oriented to active place on the

enzymes in such a manner that a covalent intermediate develops between the
enzyme and the substrate, in catalysis that occurs by covalent mechanisms.
■ The best example of this involves proteolysis by serine proteases that have
both digestive enzymes and various enzymes of the blood clotting cascade.
■ These proteases have an active site serine whose R group hydroxyl produces a
covalent bond with a carbonyl carbon of a peptide bond and causes hydrolysis
of the peptide bond.
6. ENZYMES :

3. CATALYSIS INVOLVING ACIDS AND BASES : Other mechanisms also contribute to

the completion of catalytic events that are initiated by strain mechanism like the
use of glutamate as a general acid catalyst.
4. CATALYSIS BY ORIENTATION AND PROXIMITY : Enzyme-substrate interactions
bring reactive groups into proximity with one another. Also, groups like aspartate
are chemically reactive, and their proximity and towards the substrate favours their
involvement in catalysis.
■ ACTION AND NATURE OF ENZYMES:
■ Once substrate (S) binds to this active site, they form a complex (intermediate-ES)
which then produces the product (P) and the enzyme (E) The substrate which gets
attached to the enzyme has a specific structure, and that can only fit in a particular
enzyme.
6. ENZYMES :

■ Hence by providing a surface for the substrate, an enzyme slows down the
activation energy of the reaction.
■ The intermediate state where the substrate binds to the enzyme is called the
transition state.
■ By breaking and making the bonds, the substrate binds to the enzyme (remains
unchanged), which converts into the product and later splits into product and
enzyme.
■ The free enzymes then bind to other substrates, and the catalytic cycle
continues until the reaction completes.
6. ENZYMES :

■ The enzyme action basically happens in two steps:

■ Step1: Combining of enzyme and the reactant/
substrate.
■ E+S → [ES]
■ Step 2: Disintegration of the complex molecule to
give the product.
■ [ES]→E+P
■ Thus, the whole catalyst action of enzymes is
summarized as:
■ E + S → [ES] → [EP] → E + P
6. ENZYMES :

■ FACTORS AFFECTING ENZYME ACTIVITY :

■ The conditions of the reaction have a great impact on the activity of the
enzymes. Enzymes are particular about the optimum conditions provided for
the reactions such as temperature, pH, alteration in substrate concentration, etc.
■ Generally, an increase in temperature increases the activity of enzymes.
Because enzymes function in cells, the optimum conditions for most enzymes
are moderate temperatures.
■ At elevated temperatures, at a certain point activity decreases dramatically
when enzymes are denatured.
6. ENZYMES :

■ Purified enzymes in diluted solutions are denatured more rapidly than enzymes in
crude extracts.
■ Incubation of enzymes for long periods may also denature enzymes.
■ It is more suitable to use a short incubation time in order to measure the initial
velocities of the enzyme reactions. The International Union of Biochemistry
recommends 30 °C as the standard assay temperature.
■ Most enzymes are very sensitive to changes in pH. Only a few enzymes function
optimally below pH 5 and above pH 9.
■ The majority of enzymes have their pH-optimum close to neutrality. The change in
pH will change the ionic state of amino acid residues in the active site and in the
whole protein.
6. ENZYMES :

■ The change in the ionic state may change substrate binding and catalysis.
■ The choice of substrate concentration is also crucial because, at low concentrations, the
rate is dependent on the concentration, but at high concentrations, the rate is
independent of any further increase in substrate concentration.
■ ACTIVE SITE :
■ Enzymatic catalysis relies on the action of amino acid side chains arrayed in the active
centre. Enzymes bind the substrate into a region of the active site in an intermediate
conformation.
■ The active site is often a pocket or a cleft formed by the amino acids that participate in
substrate binding and catalysis. The amino acids that make up the active site of an
enzyme are not contiguous to one another along the primary amino acid sequence.
6. ENZYMES :

■ The active site amino acids are brought to the cluster

in the right conformation by the 3-dimensional folding
of the primary amino acid sequence.
■ Of the 20 different amino acids that make up protein,
the polar amino acids, aspartate, glutamate, cysteine,
Serine, histidine, and lysine have been shown most
frequently to be active site amino acid residues.
■ Usually, only two to three essential amino acid
residues are directly involved in the bond leading to
product formation. Aspartate, glutamate, and histidine
are the amino acid residues that also serve as proton
donors or acceptors.
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