CHAPTER # 02

BIOMOLECULES
Introduction
A biomolecule, also known as a Biological Molecule, is any type of substance that is produced by cells and living
organisms. There are many types of biomolecules. The following are four major types of biomolecules: carbohydrates, lipids,
nucleic acids, and proteins. Among biomolecules, nucleic acids, namely DNA and RNA, have the unique function of storing an
organism’s genetic code: the sequence of nucleotides determines the amino acid sequence of proteins, which are of critical
importance to life on Earth. Twenty different types of amino acids can occur within a protein; the order in which they occur
plays a fundamental role in determining protein structure and function. Proteins themselves are major structural elements of
cells. They also serve as transporters, moving nutrients and other molecules in and out of cells, and
as enzymes and catalysts for the vast majority of chemical reactions that take place in living organisms. Proteins also
form antibodies and hormones, and they influence gene activity. Likewise, carbohydrates, which are made up primarily of
molecules containing atoms of carbon, hydrogen, and oxygen, are essential energy sources and structural components of all
living organisms, and they are among the most abundant biomolecules on Earth. Carbohydrates are used by living organisms
as the primary fuel, getting energy for their normal functioning. They are built from four types of sugar units:
monosaccharides, disaccharides, oligosaccharides, and polysaccharides. Lipids, another key biomolecule of living organisms,
fulfill a variety of roles, including serving as a source of stored energy and acting as chemical messengers. They also
form different membranes, which separate cells from their environments and compartmentalize the cell interior, giving rise
to organelles, such as the nucleus and the mitochondrion, in higher organisms.

CARBOHYDRATES/SACCHARIDES
A carbohydrate is a biomolecule consisting of carbon (C), hydrogen (H), and oxygen (O) atoms, usually with a hydrogen-
oxygen atom ratio of 2:1 (and so are called watered carbon ) and thus with the empirical formula Cm(H2O)n (where m may or
may not be different from “n”).” However, not all carbohydrates conform to this precise stoichiometric definition (e.g. uronic
acids) nor are all chemicals that do conform to this definition automatically classified as carbohydrates (e.g. formaldehyde).
Carbohydrates are probably the most abundant and widespread organic substances in nature, and they are
essential constituents of all living things. Carbohydrates are formed by green plants from carbon dioxide and water during the
process of photosynthesis. Carbohydrates serve as energy sources and as essential structural components in organisms;
besides, some parts of the structure of nucleic acids consist of carbohydrates.

Classification of Carbohydrates
There are many types of classification schemes for carbohydrates. One of the most common ones is the classification in
which carbohydrates are divided into four categories: Monosaccharides, Disaccharides, Oligosaccharides,
and Polysaccharides.

The following picture shows the classification of Carbohydrates

Oligosaccharides

Raffinose
Stachyose

Monosaccharides (One Sugar Molecule)

Monosaccharides, also known as simple sugars, are the simplest form of carbohydrates and the most basic units
(monomers) of carbohydrates. The general formula of Monosaccharides is (CH 2O)n. They are usually colorless, water-soluble,
and crystalline solids. Contrary to their name (sugars), only a few monosaccharides have a sweet taste. Examples of
monosaccharides include glucose [(dextrose) (C6H12O6)], fructose/Levulose (C6H12O6), and galactose (C6H12O6).
Monosaccharides are building blocks of disaccharides (such as sucrose and lactose) and polysaccharides (such
as cellulose and starch).

Forms of Glucose: The main difference between Glucose and Dextrose is that glucose includes both D-form and L-form of
glucose whereas dextrose includes only the D-form of glucose. In other words, dextrose is the common name used for D-
glucose. Glucose is also known as dextrose because it is dextrorotatory (meaning that as an optical isomer it rotates plane-
polarized light to the right). L-Form of Glucose does not occur naturally in living organisms. However, it can be synthesized in
the laboratory.
Disaccharide/Biose/Double Sugar (Two Sugar Molecules)
A disaccharide (also called a double sugar or biose) is a sugar formed when two monosaccharides are joined by a
glycosidic linkage: the formation of a glycosidic linkage (which is a covalent bond) releases one molecule of water. Like
monosaccharides, disaccharides are simple sugars, soluble in water. Three common examples are sucrose (table
sugar), lactose, and maltose. Sucrose is formed from glucose and fructose, and lactose is made up of glucose plus galactose.
The most common types of disaccharides—sucrose, lactose, and maltose—have 12 carbon atoms, with the general formula
C12H22O11. The differences in these disaccharides are the result of their atomic structure, i.e, they are isomers of one another.

Oligosaccharide  (3-10 Sugar Molecules)

An oligosaccharide is a saccharide polymer containing a small number (typically three to ten) of monosaccharides.
Oligosaccharides are prebiotics, meaning food for tiny beneficial microorganisms in the intestine. In this sense, this class of
carbohydrates is defined as a fermentable combination of simple sugars. Oligosaccharides can have many functions including
cell recognition and cell binding. For example, glycolipids have an important role in the immune response.

Polysaccharides  (More than 10 Sugar Molecules)

Polysaccharides are the most abundant carbohydrates found in food. They are long-chain polymeric carbohydrates
composed of monosaccharide units, always more than 10 units, bound together by glycosidic linkages. They can react with
water (hydrolysis) using amylase enzymes as a catalyst, which produces constituent sugars (monosaccharides,
or oligosaccharides). They range in structure from linear to highly branched. Examples include storage polysaccharides such
as starch, glycogen, and galactogen and structural polysaccharides such as cellulose and chitin.

THE STORAGE OF ENERGY: GLYCOGENESIS AND GLYCOGENOLYSIS

Glycogenesis is the formation of glycogen (a complex carbohydrate) from glucose. Glycogenesis takes place when blood
glucose levels are sufficiently high to allow excess glucose to be stored in liver and muscle cells. Glycogenesis is stimulated by
the hormone insulin. Insulin facilitates the uptake of glucose into muscle cells, though it is not required for the transport of
glucose into liver cells. However, insulin has profound effects on glucose metabolism in liver cells, stimulating glycogenesis
and inhibiting glycogenolysis, the breakdown of glycogen into glucose. Glycogenolysis is the reverse of glycogenesis. In this
process, the glycogen stored in the Liver and Muscle Cells is broken down into glucose to provide immediate energy and to
maintain blood glucose levels during fasting. Glycogenolysis occurs primarily in the liver and is stimulated by the
hormones glucagon and epinephrine (adrenaline). Insulin, Glucagon, and epinephrine (adrenaline) are secreted by the
Pancrease.

PROTEIN
Protein is one of the four major types of macromolecules. It is composed of one or more chains of amino acid molecules. Each
long chain of amino acids is called a polypeptide – the chemical bond linking adjacent amino acids called a peptide bond. A
protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 monomers, are rarely
considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The sequence of amino acids is
crucial in determining the properties of the protein: for example, the disease sickle cell anemia is caused by one amino acid
being in the wrong place in hemoglobin. Therefore, the system for organizing the exact number and sequence of amino acids
for proteins must be highly accurate and efficient. The sequence of amino acid residues in a protein is defined by
the sequence of genes in the genetic material. In general, the genetic code specifies 20 standard amino acids. Shortly after or
even during synthesis, polypeptides are often chemically modified by the post-translational modification, which alters the
physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Some proteins have
non-peptide groups attached, which can be called prosthetic groups or cofactors. Once formed, proteins only exist for a
certain period and are then degraded and recycled by the cell's machinery through the process of protein turnover. A
protein's lifespan is measured in terms of its half-life and covers a wide range. They can exist for a few minutes or many years
with an average lifespan of 1–2 days in mammalian cells. Abnormal or misfolded proteins are degraded more rapidly either
due to being targeted for destruction or due to being unstable.
Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms and
participate in virtually every process within cells. Many proteins are enzymes that catalyze biochemical reactions and are vital
to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in
the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell
signaling, immune responses, cell adhesion, and the cell cycle. In animals, proteins are needed in the diet to provide essential
amino acids (that cannot be synthesized by the body) to the body. Digestion breaks the proteins down for use in the
metabolism.

Constituents of protein
Proteins are highly complicated nitrogenous compounds made up of amino acids. Proteins consist of carbon, hydrogen,
oxygen, nitrogen, and sulfur. Proteins are polymers of amino acids. Amino acids are linked with each other through a peptide
linkage. A peptide bond forms as a result of the elimination of a water molecule. All proteins yield amino acids upon
hydrolysis.
Amino acids
 Amino acids are biological molecules composed of amino (–NH2) and carboxylic acid (–COOH) functional groups, linked
to the same carbon atom. The general formula of amino acids is shown in the figure below. “R” is the side chain. It can be a
Hydrogen atom or any other hydrocarbon. There are 20 types of amino acids. Eleven out of twenty are synthesized by the
body and hence are called non-essential amino acids. The other ten amino acids are taken up by the body in the form of food
and are known as essential amino acids. Within the cell, the ribosome assembles amino acid molecules to form protein.

The following picture shows the formula of Amino Acids

Amino acids are classified into three groups:

 Essential/Basic/indispensable Amino Acids
Essential amino acids cannot be made by the body (Mammalians) fast enough to supply their demand. As a result,
they must come from food. The 9 essential amino acids are histidine, isoleucine, leucine, lysine, methionine,
phenylalanine, threonine, tryptophan, and valine.
 Nonessential Amino Acids
The amino acids that are produced by the body itself are called non-essential amino acids: these are made by
plants. Nonessential amino acids include alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine,
glycine, proline, serine, and tyrosine.
Conditional Amino Acids
Conditional amino acids are usually not required, except in times of illness and stress.
Conditional amino acids include arginine, cysteine, glutamine, tyrosine, glycine, ornithine, proline, and serine.

Functions of Proteins in The Body

The following are the main functions of proteins in the body:
 Growth and Maintenance
Protein is required for the growth and maintenance of tissues. One’s body’s protein needs are dependent upon
one’s health and activity level. The body needs protein for the growth and maintenance of tissues. Under normal
circumstances, one’s body breaks down the same amount of protein that it uses to build and repair tissues. Other
times, it breaks down more protein than it can create, thus increasing one’s body’s needs. This typically happens in
periods of illness, during pregnancy, while breastfeeding, fasting, etc. People recovering from an injury or surgery, older
adults, and athletes require more protein as well.
 Causes Biochemical Reactions: Enzymes
Enzymes are proteins that allow key chemical reactions to take place within the body. Enzymes are proteins that
aid the thousands of biochemical reactions that take place within and outside of cells. Enzymes may also function
outside the cell, such as digestive enzymes like lactase and sucrase, which help digest sugar. Some enzymes require
other molecules, such as vitamins or minerals, for a reaction to take place. Bodily functions that depend on enzymes
include:
o Digestion
o Energy production
o Blood clotting
o Muscle contraction
 Act as Messengers: hormones
Some hormones are made up of protein. Hormones are chemical messengers that aid communication among cells,
tissues, and organs. They’re made and secreted by endocrine tissues or glands and then transported in the blood to
their target tissues or organs where they bind to protein receptors on the cell surface. Hormones can be grouped into
three main categories:
o Protein and peptides: These are made from chains of amino acids, ranging from a few to several hundred.
o Steroids: These are made from fat cholesterol. Sex hormones (testosterone and estrogen) are steroid-based
hormones.
o Amines: These are made from the individual amino acids tryptophan or tyrosine. These hormones are related to
sleep regulation and metabolism.

Protein and polypeptides make up most of the body’s hormones. Some examples include
 Insulin: Signals the uptake of glucose or sugar into the cell.
 Glucagon: Signals the breakdown of stored glucose in the liver.
  HGH (human growth hormone): Stimulates the growth of various tissues, including bone.
 ADH (antidiuretic hormone): Signals the kidneys to reabsorb water.
 ACTH (adrenocorticotropic hormone): Stimulates the release of cortisol, a key factor in metabolism.
 Provides Structural Support
Some proteins are fibrous and provide cells and tissues with stiffness and rigidity. These proteins include
keratin, collagen, and elastin, which help form the connective framework of certain structures in the body. Keratin is a
structural protein that is found in the skin, hair, and nails. Collagen is the most abundant protein in the body and is the
structural protein of the bones, tendons, ligaments, and skin. Elastin is several hundred times more flexible than
collagen. Its high elasticity allows many tissues in the body to return to their original shape after stretching or
contracting.

 Maintains Proper pH
Proteins act as a buffer system, helping the body maintain proper pH values of the blood and other bodily fluids.
Protein plays a vital role in regulating the concentrations of acids and bases in the blood and other bodily fluids. The
balance between acids and bases is measured using the pH scale. It ranges from 0 to 14, with 0 being the most acidic, 7
neutral, and 14 the most alkaline. Examples of the pH value of common substances include
 pH 2: Stomach acid
 pH 4: Tomato juice
 pH 5: Black coffee
 pH 7.4: Human blood
 pH 10: Milk of magnesia
 pH 12: Soapy water
A variety of buffering systems allows bodily fluids to maintain normal pH ranges. A constant pH is necessary, as even a
slight change in pH can be harmful or potentially deadly. One way the body regulates pH is with proteins.

 Balances Fluids
Proteins in the blood maintain the fluid balance between the blood and the surrounding tissues. Proteins regulate
body processes to maintain fluid balance. Albumin and globulin are proteins in the blood that help maintain the body’s
fluid balance by attracting and retaining water. If one doesn’t eat enough protein, one’s levels of albumin and globulin
eventually decrease. Consequently, these proteins can no longer keep blood in the blood vessels, and the fluid is forced
into the spaces between the cells. As the fluid continues to build up in the spaces between the cells, swelling or edema
occurs, particularly in the stomach region. This is a form of severe protein malnutrition called kwashiorkor that
develops when a person is consuming enough calories but does not consume enough protein.

 Bolsters Immune Health

Proteins form antibodies to protect the body from foreign invaders, such as disease-causing bacteria and viruses.
Proteins help form immunoglobulins, or antibodies, to fight infection. Antibodies are proteins in the blood that help
protect the body from harmful invaders like bacteria and viruses. When these foreign invaders enter the cells, the body
produces antibodies that tag them for elimination. Without these antibodies, bacteria and viruses would be free to
multiply and overwhelm the body with the disease they cause. Once the body has produced antibodies against a
particular bacteria or virus, the cells never forget how to make them. This allows the antibodies to respond quickly the
next time a particular disease agent invades the body. As a result, the body develops immunity against the diseases to
which it has been exposed once.

 Transports and Stores Nutrients

Some proteins carry substances throughout the bloodstream — into cells, out of cells, or within cells, and others
store them. The substances that are transported by these proteins include nutrients like vitamins or minerals, blood
sugar, cholesterol, and oxygen. For example, hemoglobin is a protein that carries oxygen from the lungs to body tissues.
Glucose transporters (GLUT) move glucose to the cells, while lipoproteins transport cholesterol and other fats in the
blood. Proteins also have storage roles. Ferritin is a storage protein that stores iron. Another storage protein is casein,
which is the principal protein in milk that helps babies grow.

 Provides Energy and Repairing

Protein can serve as a valuable energy source but only in situations of fasting, exhaustive exercise, or inadequate
calorie intake. Protein contains four calories per gram, the same amount of energy that carbs provide. Fats supply the
most energy, at nine calories per gram. However, the last thing the body wants to use for energy is protein since this
valuable nutrient is widely used throughout the body. Carbs and fats are much better suited for providing energy, as the
body maintains reserves for use as fuel. Moreover, they’re metabolized more efficiently compared to protein.
Protein supplies the body with very little of its energy needs under normal circumstances. However, in a state of fasting
(18–48 hours of no food intake), the body breaks down skeletal muscle so that the amino acids can supply the body
with energy. One’s body also uses amino acids from broken-down skeletal muscle if carbohydrate storage is low. This
can occur after exhaustive exercise or if one doesn’t consume enough calories in general.
 LIPID
Introduction
Lipids are hydrophobic macromolecules made up of diverse types of monomers, and hence cannot be called true polymers.
These are molecules that contain hydrocarbons and are structural and functional units, among others, of the cell. Examples of
lipids include fats, oils, waxes, certain vitamins (such as A, D, E, and K), hormones, and most of the cell membrane that is not
made up of protein.” Generally, the building blocks of lipids are fatty acids.
There are three main types of lipids:
 Triglycerides (oils and fats)
 Diglycerides (phospholipids)
 Steroids (cholesterol, etc.)
The functions of lipids include storing energy, signaling, and acting as structural components of cell membranes. Lipids have
applications in the cosmetic and food industries as well as in nanotechnology.
Triglycerides
Triglycerides make a type of lipid that is made up of “Triglycerol” monomers, which are made up of glycerol (one
molecule) and fatty acids (two molecules). The two common types of triglycerides are fats and oils. Fats are saturated and oils
are unsaturated triglycerides. In the following classification, oils are considered to be a subtype of fats.

FATS
Most of the fat the body needs is made by itself, but there are some fats the body cannot make. They must be taken through
food. These fats are called “essential” fats. Essential fats include Omega-3 fats (found in foods such as fish and flaxseed) and
Omega-6 fats (found in foods such as nuts, seeds, and corn oil (‫)مکی‬
There are three main types of fat in the foods one eats:
1. saturated fats (from animal foods)
2. Trans fats (from commercially prepared, processed foods) 
3. unsaturated fats (that are most often acquired from plant foods)

Unsaturated Fats
Unsaturated fats, which are liquid at room temperature, are considered beneficial fats because they can improve blood
cholesterol levels, ease inflammation, stabilize heart rhythms, and play several other beneficial roles. Unsaturated fats are
predominantly found in foods from plants, such as vegetable oils, nuts, and seeds.
There are two types of “good” unsaturated fats:
1. Monounsaturated fats are found in high concentrations in:
 Olive, peanut, and canola oils
 Avocados
 Nuts such as almonds, hazelnuts, and pecans
 Seeds such as pumpkin and sesame seeds
2. Polyunsaturated fats are found in high concentrations in
 Sunflower, corn, soybean, and flaxseed oils
 Walnuts
 Flax seeds
 Fish
Canola oil – though higher in monounsaturated fat, it’s also a good source of polyunsaturated fat. Omega-3 fatty acids and
omega-6 fatty acids are important types of polyunsaturated fat. The body can’t make these, so they must come from food. An
excellent way to get omega-3 fats is by eating fish 2-3 times a week. Good plant sources of omega-3 fats include flax seeds,
walnuts, and canola or soybean oil. Higher blood omega-3 fats are associated with a lower risk of premature death among
older adults, according to a study by HSPH faculty. These fatty acids reduce LDL cholesterol and raise HDL cholesterol.
Saturated Fats
All foods containing fat have a mix of specific types of fats. Even healthy foods like chicken and nuts have small amounts of
saturated fat, though much less than the amounts found in beef, cheese, and ice cream. Saturated fat is mainly found in
animal foods, but a few plant foods are also high in saturated fats, such as coconut, coconut oil, palm oil, and palm kernel oil.
The main sources of saturated fat in the diet are
 Pizza and cheese
 Whole and reduced-fat milk, butter, and dairy desserts
 Meat products
 Cookies and other grain-based desserts
It is mostly suggested, by health professionals, that saturated fats must be less than 10% of one’s daily food intake
Trans Fats
“Trans fatty acids, more commonly called trans fats, are a by-product of industrial hydrogenation.”
Trans fats are also naturally found in beef fat and dairy fat in small amounts. They do not have even a single health benefit.
Trans fats are the worst type of fat for the heart, blood vessels, and rest of the body because they:
 Raise bad LDL and lower good HDL
 Create inflammation,– a reaction related to immunity – which has been implicated in heart disease, stroke, diabetes,
and other chronic conditions
 Contribute to insulin resistance, and hence cause Type-2 diabetes.
  Can have harmful health effects even in small amounts – for each additional 2 percent of calories from trans fat
consumed daily, the risk of coronary heart disease increases by 23 percent.

NUCLEIC ACIDS
Introduction
Nucleic acids are biomolecules essential to all known forms of life. The monomers nucleic acids are called nucleotides. A
nucleotite is made of three components: one 5-Carbon Sugar (Deoxyribose or Ribose), one Phosphate Group and
one Nitrogenous Base. The two main classes of nucleic acids are Deoxyribonucleic Acid (DNA) and Ribonucleic Acid (RNA). If
the sugar is ribose, the polymer is RNA; if the sugar is the ribose derivative deoxyribose, the polymer is DNA.

Structure of Nucleic Acids

A nucleotide is made up of three parts that are attached by bonds. The three parts are a one 5-Carbon Sugar (Deoxyribose or
Ribose), one Phosphate Group and one Nitrogenous Base.

Phosphate Group
The phosphate group is made up of a phosphorus atom with four negatively charged oxygen atoms attached to it.

5-carbon sugar/Pentose
The 5-carbon sugar includes ribose and deoxyribose, which are present in nucleic acid. Both ribose and deoxyribose have five
carbon atoms and one oxygen atom. Attached to the carbon atoms are hydrogen atoms and hydroxyl groups. In ribose sugar,
there are hydroxyl groups attached to the second and third carbon atoms. In deoxyribose sugar, there is a hydroxyl group
attached to the third carbon atom, but only a hydrogen atom is attached to the second carbon atom.

Nitrogen base
The four nucleobases in DNA are Guanine, Adenine, Cytosine and Thymine; in RNA, Uracil is used in place of thymine.

Nucleic acid bonds

The bonds that hold together the Phosphate Group, sugar, and nitrogen molecules are called Glycosidic Bonds and
Ester Bonds. Glycosidic bonds are made between a 5-carbon sugar and the a nitrogenous base. Ester bonds are made
between a 5-carbon sugar and the phosphate group.

The Function Of Nucleic Acid

Each type of nucleic acid carries out a different function in the cells of all living things.

DNA
DNA is responsible for storing and coding genetic information in the body. The structure of DNA allows for genetic
information to be inherited by children from their parents. Besides, instructions for all the proteins an organism would make
are stored in DNA. It is also responsible for the programmed death of cells.

For Details of DNA, see “The Basis of Life”

RNA
Ribonucleic acid (RNA) functions in converting genetic information from genes into the amino acid sequences of
proteins. The three universal types of RNA include transfer RNA (tRNA), messenger RNA (mRNA), and ribosomal RNA
(rRNA). Messenger RNA acts to carry genetic sequence information between DNA and ribosomes, directing protein
synthesis. Ribosomal RNA reads the DNA sequence and catalyzes peptide bond formation. Transfer RNA serves as the carrier
molecule for amino acids to be used in protein synthesis and is responsible for decoding the mRNA. In addition, many
other classes of RNA are now known. Besides these functions, RNA is also involved in the formation synthesis of new cells in
the body.

Examples of Nucleic Acids

Besides DNA and RNA, there are some other very important molecules. They include adenosine triphosphate (ATP),
Nucleoside Triphosphates, Guanosine Triphosphate (GTP), Cytidine Triphosphate (CTP), and uridine triphosphate (UTP), etc.
These Nucleic Acids are energy-producing molecules. Adenosine Triphosphate (ATP) is the most important one.

Adenosine Triphosphate (ATP)

Adenosine triphosphate (ATP), made up of an adenine nitrogenous base, a 5-carbon ribose sugar, and three phosphate
groups, is involved in generating energy for cellular processes. The bonds between the three phosphate groups are high-
energy bonds, and supply the cell with energy. All living cells use ATP for energy to allow them to carry out their functions.
 ENZYME
Introduction
In the body of an organism, different types of biochemical reactions take place. Generally, these reactions are very slow.
Some special substances called biochemical catalysts optimize these reactions for the proper function of the body. Most
biochemical catalysts are made up of protein and are called enzymes. However, biochemical catalysts are also made of nucleic
acids, particularly RNA. These catalysts are known as Ribozymes: ribozymes are catalytically active RNA molecules or RNA–
protein complexes, in which solely the RNA provides the catalytic activity. 

Importance of Enzymes
Most biochemical reactions are regulated by enzymes. Without enzymes, many of these reactions would not take place
at a perceptible (noticeable) rate. Enzymes catalyze all aspects of cell metabolism. This includes the digestion of food, in which
large nutrient molecules (such as proteins, carbohydrates, and fats) are broken down into smaller molecules; the conservation
and transformation of chemical energy; and the construction of cellular macromolecules from smaller precursors. Many
inherited human diseases, such as albinism, are the result of the deficiency of a particular enzyme.
Enzymes also have some valuable industrial and medical applications. The fermenting of wine, the leavening of bread,
the curdling (‫ )دہی بنانا‬of cheese, and brewing (‫ )کشیدہ کرنا‬of beer have been practiced since earliest times. However, their
procedure was not known. Enzymes were first discovered in the 19 th century: in 1833 Anselme Payen discovered the first
enzyme, diastase, and in 1878 German physiologist Wilhelm Kühne (1837–1900) coined the term enzyme. Since then,
enzymes have assumed increasing importance in industrial processes that involve organic chemical reactions. The uses of
enzymes in medicine include killing disease-causing microorganisms, promoting wound healing, and diagnosing certain
diseases.

Composition of Enzymes
All biochemical catalysts were once thought to be proteins. However, this axiom was refuted by the discovery of
biochemical catalysts made up of nucleic acids in the 1980s. These nucleic acid catalysts are known as ribozymes (or catalytic
RNAs).
A large protein enzyme molecule is composed of one or more amino acid chains called polypeptide chains. If the
enzyme is subjected to changes, such as fluctuations in temperature or pH, the protein structure may lose
its integrity (denature) and its enzymatic ability. Denaturation is sometimes, but not always, reversible.

Cofactors
Some enzymes require a non-protein molecule for proper functioning. This molecule is known as a co-factor. A cofactor
may be either an organic molecule, such as a vitamin or an inorganic metal ion (Mg2+, Fe2+, Cu2+, Zn2+, etc.); some enzymes
require both. If the cofactor is covalently bonded, it is known as a prosthetic group. If the co-factor is an organic compound
and is loosely attached to the protein, it is known as a coenzyme. If the co-factor is an inorganic compound and is loosely
attached to the protein, it is known as an activator.

An enzyme whose coenzyme/prosthetic group is removed is called an apoenzyme. An activated enzyme consisting of a
polypeptide chain and a cofactor is known as a holoenzyme.

Characteristics of Enzymes
 All proteinous biochemical catalysts are known as enzymes. The other way round, all enzymes are proteins: all
biochemical catalysts were once thought to be proteins. However, this axiom was refuted by the discovery of
biochemical catalysts made up of nucleic acids in the 1980s. These nucleic acid catalysts are known as ribozymes (or
catalytic RNAs).
 They increase the rate of reaction without themselves being used up.
 Their presence does not affect the nature or properties of the end products of a chemical reaction.
 A small amount of an enzyme can accelerate a chemical reaction.
 Enzymes are very specific in their action; a single enzyme catalyzes only a single chemical reaction or a group of related
reactions.
 They are sensitive to even a minor change in pH, temperature, and substrate concentration.
 Some enzymes require a co-factor for their proper functioning.
 They lower the activation energy of the reactions.

What do Enzymes do?

All chemical reactions require activation energy, which is defined as the minimum amount of energy required to start a
reaction. The need for activation energy acts as a barrier to the beginning of a reaction. An enzyme lowers the energy required
to start a chemical reaction. In other words, an enzyme lowers the activation energy of a chemical reaction. Thus, in the
presence of enzymes, reactions proceed at a faster rate. Enzymes lower the activation energy in several ways. They may alter
the shape of the substrate. Some enzymes do so by disrupting the charge distribution on substrates. Enzymes may also lower
activation energy by bringing substrates in the correct orientation to react.
Working of Enzymes
An enzyme is a three-dimensional globular protein that has specific chemical composition and shape. Every enzyme
recognizes and reacts with a special chemical substance called the substrate. Any enzyme, therefore, reacts only with its
specific substrate and transforms it into the product (s). It is then released unaltered and thus can be used again and again.

E (Enzyme) + S (Substrate) ↔ ES (Enzyme Substrate Complex) ↔ E + P (product)

An enzyme and its substrate combine with each other through a definite charge-bearing site of an enzyme called the active
site.
The active site of the enzyme is made up of two regions: the binding site and the catalytic site. The binding site helps the
enzyme in the recognition and binding of a proper substrate to produce an ES complex. This interaction activates the catalytic
site. The activated catalytic site catalyzes the transformation of the substrate into the product (s). The enzyme after catalysis
detaches itself from the products and remains unchanged. The enzyme requires an aqueous medium for its activity.

Models for Enzyme-Substrate interaction

There are two main models to theorize the enzyme-substrate interaction, i.e., how enzymes catalyze chemical reactions:
the Lock-and-Key Model and Induced-Fit-Model.
 The Lock-And-Key Model: According to the Lock-and-Key Model, As a specific key can open only a specific lock, in the
same manner, a specific enzyme can transform a substrate into the products (s). The enzyme and the substrate possess
specific geometric shapes that fit exactly into one another. Enzymes are highly specific. An enzyme can activate only
one type of enzyme or a group of closely related enzymes. This model was proposed by Emil Fischer in 1890. However,
new research does not support this model.
The following picture shows the Lock and Key Model

 Induced Fit Model: The induced-fit model was first proposed by Koshland in 1958. According to this model, when a
substrate combines with an enzyme, it induces changes in the enzyme structure. The change in structure enables the
enzyme to perform its catalytic activity more effectively.
The following picture shows the Lock and Key Model
Factors Affecting The Rate of Enzyme Action
The functional specificity of every enzyme is the consequence of its specific chemistry and configuration. Any factor that
can alter the chemistry and shape of an enzyme can affect its rate of catalysis. Some of the important factors that can affect
the rate of enzyme action are the concentration of the enzyme, the concentration of the substrate, temperature, and pH of
the medium.
The concentration of the Enzyme
The rate of a reaction is directly proportional to the concentration of the enzyme required for its catalysis up to a
definite point; If the amount of enzyme is increased by twofold the reaction rate is doubled. More enzymes mean more active
sites and the conversion of more substrates. However, when the number of enzyme molecules becomes equal to that of the
substrates present, an increase in the concentration does not affect the rate of the reaction.

The concentration of the Enzyme

When the concentration of the enzyme is constant, up to a limit, the rate of a reaction is directly proportional to the
concentration of the substrate because enzyme molecules can find substrate molecules easily. If a certain limit, the
concentration of the substrate does not matter.

Temperature
The rate of enzyme-controlled reactions may increase with an increase in temperature but up to a certain limit. All
enzymes can work at their maximum rate at a specific temperature called optimum temperature. For enzymes in the human
body, 37°C is the optimum temperature.
Heat provides activation energy and, therefore, chemical reactions are accelerated at high temperatures. Heat also
supplies kinetic energy to the reacting molecules, causing them to move rapidly. Thus the reactants move more quickly and
the chances of their collision with each other are increased. However, a further increase in heat energy also increases the
vibrations of atoms that make up the enzyme molecule. If the vibrations become too violent, the globular structure essential
for enzyme activity is lost and the enzyme is said to be denatured.

PH Value of the Medium

Every enzyme functions most effectively over a narrow range of pH known as the optimum pH. A slight change in pH can
change the ionization of the amino acids at the active site. Moreover, it may affect the ionization of the substrates. Under
these changed conditions enzyme activity is either retarded or blocked completely. Extreme changes in pH cause the bonds in
the enzyme to break, resulting in enzyme denaturation. Pepsin has an optimum of pH 2.0 and a working range of between pH
1-4. Catalase has an optimum pH of 9 and a working range of between pH 7-11.
The following picture shows values of optimum PH for different enzymes

Inhibitors
An inhibitor is a chemical substance that can react (in place of the substrate) with the enzyme but is not transformed into
the product(s) and thus blocks the active site temporarily or permanently for the substrate. Examples include poisons, like
cyanide, antibiotics, anti-metabolites, and some drugs. Inhibitors can be divided into two types: (i) Irreversible (ii) Reversible
 Irreversible Inhibitors: They check the reaction rate by occupying the active sites or destroying the globular structure.
They occupy the active sites by forming covalent bonds or they may physically block the active sites.
 Reversible Inhibitors: They form weak linkages with the enzyme. Their effect can be neutralized completely or partly by
an increase in the concentration of the substrate. They are further divided into two major types: A. Competitive B. Non-
competitive
o Competitive Inhibitors: Because of their structural similarity with the substrate, they may be selected by the
binding sites, but are not able to activate the catalytic sites. Thus, they block the reaction.
o Non-Competitive Inhibitors: They form an enzyme-inhibitor complex at a point other than the active site. They
alter the structure of the enzyme in such a way that even if a genuine substrate binds the active site, catalysis
fails to take place.