BIOMOLECULES

By LPS
For GMD 4
 Biomolecules:
 Organic as well as inorganic matter in protoplasm of cell
(make life possible in a cell)
 All the elements present in a sample of earth’s crust are also
present in a sample of living tissue
 water is the most abundant chemical in living organisms

 HOW TO ANALYSE CHEMICAL COMPOSITION?

1. Take any living tissue (a vegetable or a piece of liver, etc.)
and
2. grind it in trichloroacetic acid (Cl3CCOOH) using a mortar
and a pestle (We obtain a thick slurry)
3. If we were to strain this through a cheesecloth or cotton we
would obtain 2 fractions:
 1. LIVING TISSUE

3. MAKE SLURRY

4. STRAIN THROUGH
2. GRIND IN PESTLE & MORTAR CHEESE CLOTH

ACID INSOLUBLE POOL/ RETENTATE

ACID SOLUBLE POOL/ FILTRATE

(a). One is called the Filtrate/ Acid-soluble pool (contains
those compounds that have molecular weights ranging from
18 to around 800 daltons (Da) approximately (aka
Micromolecules)

(b). The second, the Retentate/ Acid-insoluble fraction has

only 4 types of organic compounds i.e. proteins, nucleic
acids, polysaccharides and lipids. These classes of
compounds with the exception of lipids, have molecular
weights in the range of 10 thousand daltons and above

 Scientists have found thousands of organic compounds in

the acid-soluble pool and also inorganic compounds
How do we know this?
 Ans:
1. Take a small amount of a living tissue (say a leaf or liver)
and dry it. All the water evaporates, gives dry weight
2. Now if the tissue is fully burnt, all the carbon compounds
are oxidised to gaseous form (CO2, water vapour). What
remaining is called ‘ash’
3. Ash contains inorganic matter (like calcium, magnesium,
sulphate, phosphate, etc are seen in the acid-soluble
fraction
4. Analysis for compounds gives an idea of the kind of organic
and inorganic constituents present in living tissues
5. From a chemistry point of view, one can identify functional
groups like aldehydes, ketones, aromatic compounds, etc.
6. But from a biological point of view, we shall classify them
 Chemical nature of Protoplasm: out of 34, main
elements are:

 Intracellular cations concentration: K>Na>Ca

 Primary and Secondary metabolites:
 Organic compounds including amino acids, sugars, etc
 we can call these biomolecules as ‘metabolites’
 2 types:
1. Primary metabolites:
 Have identifiable functions & play roles in normal
physiologial processes
2. Secondary metabolites:
 Do not play roles in normal physiologial processes
 However, many of them are useful to ‘human welfare’ (e.g.,
rubber, drugs, spices, scents and pigments)
 Some have ecological importance
 Carbohydrates:

 Main source of energy

 First respiratory substrate
 Generalised formula: C x(H2O)y
 For example: If x= 6 & y= 6 then compound is C6H12O6
 Compounds of C, H & O with ratio of H and O is 2:1, so
they are also called as Hydrates of carbon
 Simple carbohydrates which are water soluble and sweet in
taste are called Sugars
 Chemically all carbohydrates are polyhydroxy aldehydes or
ketones
Q. Which substance is most abundant in cell

(1) Carbohydrates
(2) Proteins
(3) Water
(4) Fats
Q. Which substance is most abundant in cell

(1) Carbohydrates
(2) Proteins
(3) Water
(4) Fats
 Classification of carbohydrates:
 On the basis of numbers of Saccharides (carbohydrate
units) in hydrolysis (Hydro: water, Lysis: breakdown),
carbohydrates are classified as:
1. Monosaccharides
2. Oligosaccharides
3. Polysaccharides

1. Monosaccharides:
 Simplest sugars (can not be further hydrolysed)
 Number of C & O atoms same
 A 6 membered ring is known as Pyranose and 5 membered
ring is Furanose
 (Pyranose ring) (Furanose ring)

 Monosaccharides occur in D and L conformation with the

exception of Dihydroxyacetone which does not has Chiral
carbon (central carbon which has all its 4 valences are
satisfied by different functional groups in its structure)
 Monosaccharides are composed of 3-7 carbon atoms

, arabinose

 Glucose:
 Forms main energy source &
is respiratory substrate 4 1 4 1
1 1
4 1 3 4
 High amounts in grapes, so 1 4 1

aka grape sugar 4

 High levels in blood so aka

 So aka corn sugar/ blood sugar/ grape sugar/ dextrose
(rotates plane polarised light to right)

 Fructose: Fructose

 aka Fruit sugar/ Levulose

(rotates plane polarised
light to left)
 Sweetest sugar 6

4 1
4
 Galactose:
 aka Brain sugar (supports brain
develpoment in infants)
 Never present in free form (always present with another
 Xylose: Found in cell wall of plants
 Thaumatin: sweetest carbohydrate, mixture of proteins
isolated from katemfe fruit via Thaumatococcus danielli
bacteria
 Aspartame/Aspartin: Commonly used as an artificial
sweetener
 Saccharine: Non nutritive Artificial sweetener (made in lab.)

 Derivatives of Monosaccharides:
1. Amino sugars:
 The hydroxyl group in the
second carbon atom is
displaced with the amino
group. e.g. Glucosamine,
2. Sugar alcohol: The aldehyde group (CHO) in the sugar is
displaced with the primary alcohol (CH2OH). e.g. Sorbitol
and Mannitol are formed from glucose and mannose,
respectively 1

3. Sugar acids: The terminal CHO

or CH2OH group of the sugar gets
oxidised to produce a carboxyl
functional group COOH e.g.
Glucoronic acid, Galacturonic acid
4. Deoxy sugars: Formed via deoxygenation (removal of O)
e.g. Deoxygenation (at 2nd carbon) of ribose produce
deoxyribose

2. Oligosaccharides:
 The carbohydrates on hydrolysis give 2 to 10
monosaccharide units (monomers)
 Glycosidic bond binds 2 monosaccharides together
 Glycosidic bond is formed when the aldehyde or ketone
group of one monosaccharide reacts with the OH group
of another monosaccharide with loss of one molecule of
H2O
Q. Monosaccharide is

(1) Pentose Sugar

(2) Hexose Sugar
(3) Only Glucose
(4) all the above
Q. Monosaccharide is

(1) Pentose Sugar

(2) Hexose Sugar
(3) Only Glucose
(4) all the above
Q. Carbohydrates are stored in mammals as:

(1) Glucose in liver

(2) Glycogen in muscles and spleen
(3) Lactic acid in muscles
(4) Glycogen in liver and muscles
Q. Carbohydrates are stored in mammals as:

(1) Glucose in liver

(2) Glycogen in muscles and spleen
(3) Lactic acid in muscles
(4) Glycogen in liver and muscles
 Type of Oligosaccharides:
 Disaccharides:
 Composed of two monosaccharide units e.g. Maltose,
Sucrose, Lactose, Trehalose
 All disaccharides are water soluble and sweet in taste, so
they are known as sugars
 Examples:
 Maltose/ Malt sugar: Maltose has α -1'-4’’ glycosidic
linkage between α -D glucose and β -D glucose
 Lactose/ Milk sugar: with β-1'-4" glycosidic linkage
between glucose and galactose α -glycosidic bond: when OH of
both molecules are at same
orientation
β-glycosidic bond: when OH of
both molecules are at different
orientation

 Sucrose/ invert sugar/Cane Sugar or Table Sugar or

Commercial Sugar: Composed of α -D Glucose and
fructose & join via α1- β2 linkage
 Trehalose: binds with 1-1 glycosidic linkage b/w α- glucose
& β- glucose (present in haemolymph of insects)

 Trisaccharides: e.g Raffinose

(Galactose+Glucose+Fructose)

 Tetrasaccharides: e.g. Stachyose (Gal.+Gal.+Glu.

+Fructose)
 Reducing & Non- reducing Sugars:

 Reducing sugars:
 Can reduce Cu2+ ions to Cu+ ions with their free CHO or
ketone group
 e.g. All monosaccharides & Disaccharides (except Sucrose,
Trehalose etc), Some polysaccharides

 This property helps detecting presence of glucose in urine

via Fehling’s & Benedict’s test
3. Polysaccharides:
 Composed of large number of monosaccharide units

 Are insoluble in water and do not taste sweet

 Although polysaccharide is non reducing but in a

polysaccharide chain right end is reducing and left end is
non reducing
 On structural basis polysaccharides are of 2 types:

A. Homopolysaccharides
B. Heteropolysaccharides
Q. Sugar which found in haemolymph of insects
is called

(1) Maltose
(2) Lactose
(3) Trehalose
(4) Galactose
Q. Sugar which found in haemolymph of insects
is called

(1) Maltose
(2) Lactose
(3) Trehalose
(4) Galactose
Q. Starving person will first use

(1) Fats
(2) Glycogen
(3) Blood protein
(4) Muscle protein
Q. Starving person will first use

(1) Fats
(2) Glycogen
(3) Blood protein
(4) Muscle protein
A. Homopolysaccharides:

 Composed of same monomers

 Biologically important homopolysaccharides are as
follows:

 STORAGE POLYSACHHARIDES:

(a). Starch: It is main stored food in plants. Starch is polymer

of α -D-glucose units. Starch consists of 2 types of chains

(i) Amylose: 250-1000 glucose units are arranged in an

unbranched chain by α 1'-4" linkage
(ii) Amylopectin: A branched chain molecule. Approximately
2000-200000 glucose units are linked by α - 1',4“ linkage
& α - 1',6" linkage (at branch point after every 25 th glucose
unit)

 Starch gives blue colour with iodine (Starch form helical

structure so can hold I2 molecules in the helical portion so
starch-I2 is blue in colour)
(b). Glycogen or animal starch:
 Storage form of carbohydrate in animals, storage region of
glycogen is liver and muscles
 Glycogen is highly branched polymer of α -D-glucose
(around 30000 molecules)
 Glycogen is formed by the 1',4" bond linkage at long chain
and 1',6" bond linkage (at branching point)
 Glycogen gives red colour with iodine.
 Glycogen is store food of
fungi
(c). Inulin:
 Linear polymer of fructose units linked with β -1',2" bonds

 Inulin is found in roots & tubers of Dahlia and Artichoke

 It is water soluble polysaccharide

 it is used to know the glomerular filtration rate (kidney

functioning) as it is not metabolised in human body &
readily filtered through kidneys Dahlia

 It is smallest storage polysaccharide

 STRUCTURAL POLYSACCHARIDES:

(d). Chitin:

 Linear polymer of N-acetyl-D-glucosamine with β-1',4“

linkage

 Chitin is an important component of exoskeleton of

Arthropods and cell walls of fungi (aka Fungal cellulose)

 Second most abundant organic molecule on earth

Q. Sucrose is composed of :

(1) Glucose & Fructose

(2) Glucose & Glycogen
(3) Two molecules of Glucose
(4) Glycogen & Fructose
Q. Sucrose is composed of :

(1) Glucose & Fructose

(2) Glucose & Glycogen
(3) Two molecules of Glucose
(4) Glycogen & Fructose
Q. Sweetest sugar among the naturally occuring
sugar:

(1) Glucose
(2) Fructose
(3) Sucrose
(4) Saccharine
Q. Sweetest sugar among the naturally occuring
sugar:

(1) Glucose
(2) Fructose
(3) Sucrose
(4) Saccharine
(e). Cellulose:
 Linear polymer of β -D-glucose units (6000 to 10,000)

 It has β 1'-4" linkage

 Partial digestion yields a cellobiose units (Disaccharide)

 Cellulose is main component of plant cell wall

 In wood, cellulose is 50% and in cotton, it is 90%.

 Most abundant organic molecule on earth

 Urochordates animals have cellulose like material and it is called

 It is also used to form Rayon fibre (Artificial silk).
 Paper made from plant pulp is cellulose

B. Heteropolysaccharide:

 Consists of more than one type of monosaccharide

monomers

(a). Hyaluronic acid:

 Hyaluronic acid is made up of D-glucuronic acid and N-

acetyl- D-glucosamine arranged in alternate orders
 Found in vitreous humour, umbilical cord, joints and CT in
the form of lubricating agent

 Accounts for toughness & rigidity of cartilage & tendon

(b). Peptidoglycan:

 Composed of N-acetyl Glucosamine + N-acetyl muramic

acid + peptide chain of 4-5 amino acids

 Present in cell wall of bacteria (degraded by enzyme

lysozyme present in tears, nasal mucus, gastric secretion)
(c). Agar-Agar:
 It is composed of D-galactose and L-galactose (1,3 linkage)
units and after every 10th unit a sulphate group is present it
is used for preparing culture medium

 It is a Mucopolysaccharide which is obtained from some

red algae: Gracilaria, Gelidium, Chondrus. Basic Structure
of aa

 Amino acids:
 Amino acids are organic compounds containing an amino
group (NH2) and an acidic group (COOH) as substituents
on the same carbon i.e., the α-carbon Hence, they are called
α -amino acids
 Proline amino acid has an R group that’s linked back to
its own amino group, forming a ring structure. This makes
it an exception to the typical structure of an
amino acid

 Cysteine aa contains a thiol (-SH) group and can form

covalent bonds (disulfide bond) with other cysteines to
form Cystine.
 There are four substituent groups occupying the 4 valency
positions (hydrogen, carboxyl group, amino group and a
variable group designated as R group)

 Based on the nature of R group there are many amino acids

 However, those which occur in proteins are only of 20

types

 The R group in these proteinaceous amino acids could be a

hydrogen (the amino acid is called glycine a methyl group
(alanine), hydroxy methyl (serine), etc.
Based on number of amino and carboxyl groups, there are:
1. Acidic aa: These have extra COOH group (e.g., glutamic acid/
Glutamate, aspartic acid/ Aspartate)

2. Basic aa: Have an additional NH2 group (e.g. lysine, Arginine)

3. Neutral aa: Have one NH2 group & one COOH group
(e.g. Valine, Glycine, Alanine, leucine, Isoleucine, phenylalanine,
Proline, methionine, serine, threonine, tyrosine, cysteine,
glutamine, asparagine, tryptophan)
 Aromatic amino acids: Have cyclic structure with
straight side chain (Tyrosine, phenylalanine, tryptophan)
phenylalanine

 Essential amino acids: Certain amino acids are essential

for our health and they have to be supplied through our diet
so are called (obtained from Dietary proteins)

 e.g. Methionine, isoleucine, leucine, lysine, Histidine

valine, phenylalanine, threonine, tryptophan
 Non-essential amino acids: Our body can make itself,
so not necessary to take these from diet. e.g. Alanine,
Cysteine, Glutamate, Glycine, Proline

 A particular property of amino acids is the ionizable nature

of NH2 and COOH groups. Hence in solutions of different
pH, the structure of amino acids changes
 Amino acids with alphabets: (R, F, Y, W, Q, N, E,
D, K)
 Proteins/ Hetero-polypeptides:
 They are linear chains of different amino acids linked by
peptide bonds (not a homopolymer, one type of monomer)

 Peptide bond: Amino acids are linked by a bond, which is

formed when the carboxyl (COOH) group of one amino
acid reacts with the amino (NH2) group (elimination of a
water molecule takes place)
Q. Which sugar does not give Benedict's test:

(1) Glucose
(2) Maltose
(3) Fructose
(4) Trehalose
Q. Which sugar does not give Benedict's test:

(1) Glucose
(2) Maltose
(3) Fructose
(4) Trehalose
Q. Sugar with five membered ring called -

(1) Pyranose
(2) Furanose
(3) Dextrorotatory
(4) Laevorotatory
Q. Sugar with five membered ring called -

(1) Pyranose
(2) Furanose
(3) Dextrorotatory
(4) Laevorotatory
 Collagen is the most abundant protein in animal world

 Ribulose bisphosphate Carboxylase-Oxygenase

(RuBisCO): Most abundant protein in the whole of the
biosphere

 Structure of proteins: 4 types

1. Primary structure:
 If a protein is imagined as a line, The left end represented
by the first amino acid (N-terminal amino acid) & Right
end represented by the last amino acid (C-terminal amino
acid)
 For example, the hormone insulin has two polypeptide
chains, A and B, shown in diagram below

 Both are linked by disulphide linkage

N-terminal aa C-terminal
aa
2. Secondary structure: 2 Types:
A. α-helix:
 The protein thread is folded in the form of helix (similar to
a revolving staircase)

 Only right handed helices are observed in proteins

 e.g. Keratin, Myosin, Tropomyosin proteins

B. β- Pleated sheets:
 Two or more segments of a polypeptide chain line up next
to each other, forming a sheet-like structure
 Bonding: Both structures are held in shape by hydrogen
bonds, which form between the carbonyl O of one amino
acid and the amino H of another

 However peptide bonds are always there

Q. Which sugar occurs only in mammals:

(1) Trehalose
(2) Galactose
(3) Lactose
(4) Mannose
Q. Which sugar occurs only in mammals:

(1) Trehalose
(2) Galactose
(3) Lactose
(4) Mannose
Q. Corbohydrate metabolism is controlled
by :-

(1) Parathormone
(2) Insulin
(3) Glucose
(4) Vitamin B12
Q. Corbohydrate metabolism is controlled
by :-

(1) Parathormone
(2) Insulin
(3) Glucose
(4) Vitamin B12
3. Tertiary structure:
 In addition, the long protein chain is also folded upon itself
like a hollow woolen ball

 This gives us a 3- dimensional

view of a protein

 Tertiary structure is absolutely

necessary for the many
biological activities of proteins

 For example: Majority of

proteins (e.g Myoglobin) and
 Bonding:
(i) Peptide bonds: strongest bond in proteins.
(ii) Hydrogen bonds
(iii) Disulphide bond: These bonds are second strongest bond
(iv) Hydrophobic bond:
(v) Ionic bond
Q. True statement for cellulose molecule:

(1) Beta - 1'- 4" linkage. unbranched

(2) beta - 1'- 4" linkage. branched
(3) Alpha - 1' - 4" linkage, branched
(4) Beta - 1' - 6" linkage unbranched
Q. True statement for cellulose molecule:

(1) Beta - 1'- 4" linkage. unbranched

(2) beta - 1'- 4" linkage. branched
(3) Alpha - 1' - 4" linkage, branched
(4) Beta - 1' - 6" linkage unbranched
Q. Which monosaccharide does not show
optical isomerism:

(1) Dihydroxy acetone

(2) Glyceraldehyde
(3) Erythrose
(4) Ribose
Q. Which monosaccharide does not show
optical isomerism:

(1) Dihydroxy acetone

(2) Glyceraldehyde
(3) Erythrose
(4) Ribose
4. Quaternary structure:
 Some proteins are an assembly of more than one
polypeptide or subunits

 Polypeptides or subunits are

arranged with respect to each
other (e.g. Linear string of
spheres, spheres arranged one
upon each other in the form of a
cube or plate etc)
 Adult human haemoglobin consists of 4 subunits (2
subunits of α- type and 2 subunits of β- type together
constitute the human haemoglobin (Hb)

Human
Haemoglobin
 Types of Proteins: On the basis of structure: 2 types

1. Simple proteins
2. Conjugated proteins

1. Simple proteins:
 Made up of amino acids only. It comprises of:

A. Fibrous proteins: Long, Coiled & Thread like. For example

(a). Collagen protein:

 1/3 part of total proteins
 Present in connective tissue
 Threads of collagen known as Tendon

(b). Elastin protein

 In connective tissue
 Threads of Elastin known as Ligament

(c). Keratin protein

B. Globular proteins: Spherical ("globe-like") proteins. For

example:

(a). Rubisco:

(b). Albumin:
 Maintain Osmotic balance (osmoregulation)
 In milk as Lacto-albumin
 In egg yolk as Ovalbumin
 In blood as Serum albumin

(c). Globin:
 Present in Haemoglobin.

(d). Histone protein:

 Basic protein Present with
eukaryotic DNA
(e). Prolamine:
 Present as store protein in cereal grains
 In Barley as Hordein
 In Maize as Zein
 In Wheat as Gladein, Gluten, Glutelline

2. Conjugated protein: It composed of protein & non

protein part (prosthetic group). It comprises of:

A. Nucleoprotein:
 Prosthetic group is nucleic acid. For example:
(a). Chromosome: DNA + RNA + Protein
(b). Ribosome: rRNA + Protein
(c). In Virus: Genetic material + protein coat
(d). Protamine: in nucleus of sperm (replace histones in later
haploid phase of spermatogenesis, are essential for DNA
stabilization and condensation)

B. Chromoprotein: Prosthetic group is Porphyrin pigment

(metal + porphyrin ring that contains 4 pyrrole rings, with 4
C and 1 N). For example:

 Haemoglobin (Fe) Red

 Cytochrome (Fe) Red
Q. Histone is a basic protein due to:

(1) Alanine & glycine

(2) Methionine & serine
(3) Tryptophan & tyrosine
(4) Lysine & Arginine
Q. Histone is a basic protein due to:

(1) Alanine & glycine

(2) Methionine & serine
(3) Tryptophan & tyrosine
(4) Lysine & Arginine
 Chlorophyll (Mg) Green
 Haemocyanin (Cu) Blue

C. Lipoprotein: Prosthetic group is lipid. For example:

 Chylomicron (helps absorption of fatty acids)

 Plasma membrane
 Vitelline membrane on egg surface

D. Phosphoprotein: Prosthetic group is phosphoric acid

(H3PO4). For example:
 Caseinogen in Milk
 Pepsin: Protein digesting emzyme.
Q. Which is very most structural part of the
body:

(1) Protein
(2) Carbohydrates
(3) Lipid
(4) Nucleic acid
Q. Which is very most structural part of the
body:

(1) Protein
(2) Carbohydrates
(3) Lipid
(4) Nucleic acid
Q. Which one of the following is
polysaccharide:

(1) Sucrose
(2) Lactose
(3) Glycogen
(4) Glucose
Q. Which one of the following is
polysaccharide:

(1) Sucrose
(2) Lactose
(3) Glycogen
(4) Glucose
E. Metalloprotein: Prosthetic group is metal. For example:
 Enzyme with its co-factor (metal ion)

F. Glycoprotein: Prosthetic group is carbohydrate (less than

4% carbohydrate). For example:

 Mucin in Saliva
 Erythropoetin hormone in Kidney (plays a key role in the
production of RBCs)
 A & B antigen of RBC
 α,β & γ globulin of blood
 FSH - Follicular stimulating hormone
 LH - Leutinizing hormone
 Functions:
 Some transport nutrients across cell membrane (carrier
proteins), also Haemoglobin transport O2 & Co2

 Some fight infectious organisms (e.g. Antibodies,

Lymphocytes)

 Some are hormones (e.g. Insulin

produced by β- cells in islets of
Langerhans of Pancreas)

 Some are enzymes (trypsin,

pepsin, amylase etc)
Q. Fattyness is due to the excess of:

(1) Connective tissue

(2) Blood
(3) Muscular tissue
(4) Adipose tissue
Q. Fattyness is due to the excess of:

(1) Connective tissue

(2) Blood
(3) Muscular tissue
(4) Adipose tissue
 Lipids:
 Are generally water
insoluble

 Lipids do not form polymer (Molecular weight.......)

 Lipid requires less space for storage as compare to

carbohydrate because lipid molecule is hydrophobic and
Condense

 Animals store maximum amount of food in the form of

lipid
1. Simple Lipids:

A. Neutral Fats or True fats:

 They could be simple fatty acids

 A fatty acid has a carboxyl group attached to an R group

 The R group could be a methyl (CH3), or ethyl (C2H5) or higher

 Types of Fatty acids:
(a). Saturated Fatty acids: without double bond. For example:

 Palmitic acid has 16 carbons (including carboxyl carbon)

 Stearic acid has 18 carbons

(b). Unsaturated Fatty acids: With one or

more C=C double bonds. For example:
 Oleic acid (18 C)
 Linoleic acid (18 C)
 Linolenic acid (18 C)
 Arachidonic acid (20 C)

 Another simple lipid is glycerol (Trihydroxy propane)

 Many lipids have both glycerol and fatty acids. Here the
fatty acids are found esterified with glycerol. These are
classified as:
(i). Monoglycerides: 1 fatty acid make ester bond with
glycerol

(ii). Diglycerides: 2 Fatty acids make

ester bond with glycerol

(iii). Triglycerides:.............................
Q. Fats in the body are formed when:

(1) Glycogen is formed from glucose

(2) Sugar level becomes stable in blood
(3) Extra glycogen storage in liver and muscles
is stoppped
(4) All of them
Q. Fats in the body are formed when:

(1) Glycogen is formed from glucose

(2) Sugar level becomes stable in blood
(3) Extra glycogen storage in liver and muscles
is stoppped
(4) All of them
Q. All lipids are:

(1) Composed of fatty acids

(2) Triglycerides
(3) Insoluble in water
(4) All the above
Q. All lipids are:

(1) Composed of fatty acids

(2) Triglycerides
(3) Insoluble in water
(4) All the above
 These are also called fats and oils based on melting point

 Oils have lower melting point (e.g. gingelly oil) and hence
remain as oil in winters

B. Waxes:
 These are monoglycerides with only one molecule of fatty
acid attached to a long chain of alcohol

 Waxes have an important role in protection

 They form water insoluble coatings on hair and skin in

animals and stem, leaves and fruits of plants.
 Examples:
 Bees Wax (Hexacosyl palmitate): mericyl alcohol
(C30H61OH) + palmitic acid

 Carnauba: occurs on leaves, stem and fruits

 Spermaceti: In skull of whale and Dolphin

 Cerumen or ear wax: occurs in external auditory meatus

 Lanoline or cholesterol ester or wool fat: occurs in blood,

sebum and gonadial ducts as lubricating agent. It is also
obtained from wool of sheep
2. Conjugated or Compound Lipids:

A. Phospholipid:
 2 Molecules of fatty acid + Glycerol + H3PO4 +
Nitrogenous compound

 Phospholipids are most abundant type of lipids in

protoplasm

 H3PO4 + Nitrogenous compound (hydrophilic polar end)

 Fatty acids (Hydrophobic polar end)

 Such molecules are called amphipathic
 Examples:
(a) Lecithin or Phosphatidyl choline:
 Nitrogenous compound in lecithin is choline
 Lecithin occurs in egg yolk, oil seeds and blood
 In blood lecithin functions as carrier molecule. It helps in
transportation of other lipid

(b) Sphingolipids or sphingomyelins:

 Similar to lecithin but in place of glycerol it contains an
amino alcohol Sphingosine
 Sphingolipids occur in myelin sheath of nerves

 Some tissues especially the neural tissues have lipids with

more complex structures

B. Glycolipid:
 2 fatty acid + sphingosine + galactose

e.g. Cerebroiside: which occurs in white matter of brain

 Gangliosides (more complex): These occur in nerve ganglia
and spleen
 These also contain N-acetyl neuraminic acid acid and
glucose beside other compounds.
C. Chromolipid:
 It is also called terpene

 Most complex lipid in protoplasm

 Chromolipids composed of repeated isoprene units

 Example : Carotenoids, vitamin A, E, K, Natural Rubber

(Polyterpene)
3. Derived Lipids:
 Lipid derived from simple or conjugated lipid

 Derived lipids are complex in structure

 They are insoluble in water and soluble in organic solvents

A. Steroids:
 Steroids exhibit tetracyclic structure called "Cyclo pentano
perhydrophenanthrene nucleus

 On the basis of functional group, steroids are of two types

(a). Sterols:
(i). Alcoholic steroids e.g. Cholesterol (abundantly occurs in
nervous tissue, Adrenal gland and skin).

 Cholesterol is a most abundant animal steroid (present in

animal fats & also synthesized
in liver)

 Several other biologically important steroids are derived

from cholesterol

 E.g. 7 - Dehydro cholesterol which occurs in skin is a

provitamin
Q. Which of the following fatty acid is not
synthesised in the human body

(1) Glycerol
(2) Cholesterol
(3) Linoleic acid
(4) Both 'a' and 'b'
Q. Which of the following fatty acid is not
synthesised in the human body

(1) Glycerol
(2) Cholesterol
(3) Linoleic acid
(4) Both 'a' and 'b'
 On exposure to ultraviolet radiation, it transforms in
cholecalciferol i.e. vitamin D

(ii). Ergosterol: It occurs in oil seed , fungi like ergot (group

of fungi of the genus Claviceps, that grows on Rye) and
yeast . Ergosterol is precursor of another form of Vitamin
D–Ergocalciferol

(b) Sterones:
 Ketonic steroids, for e.g.
(i) Sex hormones
(ii) Adreno-corticoids
(iii) Ecdyson hormone of insects
(iv) Diosgenin obtained from yam plant (Dioscorea), is used
in manufacture of Antifertility pills

 PROSTAGLANDINS:
 Group of hormones like unsaturated Fatty acids
 Acts as messenger b/w cells
 Derived from Arachidonic acid
 Nucleic acids/ polynucleotides:
 Friedrich Miescher discovered nucleic acid in nucleus of
pus cell and called it "nuclein“

 The term nucleic acid was coined by "Altman“

 2 types of Nucleic Acids: DNA (deoxyribonucleic acid) &

RNA (Ribonucleic acid)

 Nucleic acids are polymer of nucleotides = Nitrogen base

+ pentose sugar + phosphate
A. Nitrogen bases: Living organisms have a number of
carbon compounds in which heterocyclic rings can be
found

 Some of these are nitrogen bases:

1. Pyrimidines:
 Consist of one pyrimidine
ring (2 N + 4 C atoms)

 For e.g. Cytosine, Thymine, Uracil (substitute of thymine

in RNA)
2. Purines:
 Consist of two rings i.e. one Pyrimidine ring (2N + 4C) and
one Imidazole ring (2N + 3C)

 e.g. Adenine and Guanine

B. Pentose Sugar:
 Nitrogen base forms bond with first carbon of pentose
sugar to form a nucleoside

 In case of pyrimidines: Nitrogen of first place (N1) forms

bond with sugar
 In purines: nitrogen of ninth place (N9) forms bond with
sugar

 Nucleosides: When nitrogenous bases are found attached

to a sugar are called Nucleosides

 Adenosine, guanosine, thymidine, uridine and cytidine are

nucleosides

C. Phosphate: Forms ester bond (covalent bond) with fifth

Carbon of sugar to form a complete nucleotide
 Nucleotides: Adenylic acid (Adenosine monophosphate or
AMP), thymidylic acid, guanylic acid, uridylic acid and
cytidylic acid are nucleotides

 Nucleic acids like DNA and RNA consist of nucleotides

only.
 Nucleic acids/ polynucleotides: DNA and RNA
(function as genetic material)

 Nucleic acids exhibit a wide variety of secondary structures

1. DNA: Discovered by: F. Meischer

 In DNA pentose sugar is deoxyribose sugar and four types
of nitrogen bases A,T,G,C

 With the help of this study, Watson and Crick (1953)

proposed a double helix molel for DNA

 For this model Watson, Crick and Wilkins were awarded by

 Watson-Crick model says that DNA exists as a double helix
(secondary structure)

 According to this model B- DNA (present in our body)

comprises of:

1. The two strands of polynucleotides are antiparallel (run in

the opposite direction) & complementary

 If direction of phosphodiester bond in one strand is 3'-5'

then it is 5'-3' in another strand

2. The backbone is formed by the sugar-phosphate sugar chain

3. The nitrogen bases are projected more or less perpendicular
to this backbone but face inside

4. A of one strand compulsorily base pairs T of other strand

with 2 hydrogen bonds

5. G of one strand compulsorily base pairs C, of the other

strand with 3 hydrogen bonds

6. Each strand appears like a helical staircase. Each step of

ascent is represented by a pair of bases

7. At each step of ascent, the strand turns 36°. One full turn of
the helical strand would involve ten steps or ten base pairs
8. The pitch (1 full turn containing 10 bps) would be 34Å.
The rise per base pair would be 3.4Å (34 Å/10)

9. Polymerisation of nucleotides to form DNA takes place

10. In DNA strand, 3’ OH of one nucleotide make ester bond
with 5’ phosphate of another nucleotide and so on

11. 1 phosphate makes 2 ester bonds with 2 sugars, so that

linkage is called phosphodiester linkage
 Chargaff’ rule: In 1950, Erwin Chargaff found that in any
DNA molecule:

(i) The amounts of purines and pyrimidines are equal:

i.e. A + G : T + C

(1) The amount of adenine is always equal to that of thymine; and

the amount of guanine is always equal to that of cytosine

(ii) Tth base ratio (A + T)/(G + C) may vary flom one species to
another, but is constant for a given species

(iii) The deoxy-ribose sugar and phosphate components occur in

equal proportions
 RNA is usually single--stranded, but sometimes (as in
Reovirus and Rice dwarf virus), it is double-stranded

 RNA does not follow Chargaff's rules i.e., 1 : 1 ratio does

not exist between purines and pyrimidines bases due to
single-stranded nature and lack of complementarity
 Dynamic state of body constituents: concept of
metabolism:

 Biomolecules are present in certain concentrations (expressed as

moles/cell or moles/litre etc.)

 All these biomolecules have a turn over (they are constantly being
changed into some other biomolecules and also made from some
other biomolecules)

 This breaking (Catabolism, release energy) and making

(Anabolism, consumes energy) is through chemical reactions
constantly occuring in living organisms.

 Together all these chemical reactions are called metabolism

 A few examples for such metabolic transformations
are:

1. Removal of CO2 from amino acids making an amino acid

into an amine, removal of amino group in a nucleotide
base; hydrolysis of a glycosidic bond in a disaccharide etc.
2. Metabolic reactions are always linked to some other
reactions

3. There is no uncatalysed metabolic conversion in living

systems

 For e.g. Even CO2 dissolving in water, is however a

physical process, It is a catalysed reaction in living systems

 Proteins with catalytic power are named enzymes

4. Most important form of energy currency in living systems
is the bond energy in a chemical called adenosine
triphosphate (ATP)

5. the blood concentration of glucose in a normal healthy

individual is 4.2 mmol/L – 6.1 mmol/L, while that of
hormones would be nanograms/mL
6. All living organisms exist in a non-equilibrium steady state
characterised by concentrations of each of these
biomolecules. These biomolecules are in a metabolic flux

7. As living organisms work continuously, they cannot afford

to reach equilibrium

8. This is achieved by energy input Metabolism provides a

mechanism for the production of energy. Hence the living
state and metabolism are synonymous. Without metabolism
there cannot be a living state.
 Enzymes:
 Almost all enzymes are proteins except RNA containing
enzymes (ribozymes & ribonuclease P)

 An enzyme like any protein has the primary, secondary and

the tertiary structure

 When you look at a tertiary structure (with active site, a

crevice or pocket into which the substrate fits)

 Enzymes are different from Inorganic catalysts that work

efficiently at high temperatures and high pressures, while
enzymes get damaged at high temperatures (say above
40°C).
 However, enzymes isolated from Thermophilic organisms
who normally live under extremely high temperatures (e.g.,
hot vents and sulphur springs), are stable and retain their
catalytic power even at high temperatures (upto 80°-90°C)

 Chemical Reactions:
 When bonds are broken and new
bonds are formed during
transformation, this will be called
a chemical reaction

 Hydrolysis of starch into glucose

is an organic chemical reaction
 Rate of a physical or chemical process refers to the amount
of product formed per unit time

 Rate can also be called velocity if the direction is specified

 Consider a reaction given below:

 In the absence of an enzyme, Carbonic anhydrase, this

reaction is very slow, with about 200 molecules of H2CO3
being formed in an hour
 However, by using the enzyme present within the
cytoplasm called carbonic anhydrase, the reaction speeds
dramatically with about 600,000 molecules per second
formed (accelereated 10 million times)

 Our skeletal muscle, under anaerobic conditions, lactic acid

is formed. Under normal aerobic conditions, pyruvic acid is
formed

 In yeast, during fermentation, the same pathway leads to

the production of ethanol (alcohol). Hence, in different
conditions different products are possible.
Q. Translation refers to the process of:

(1) Polymerisation of nitrogen bases

(2) Polymerisation of nucleotides
(3) Polymerisation of nucleosides
(4) Polymerisation of amino acids
Q. Translation refers to the process of:

(1) Polymerisation of nitrogen bases

(2) Polymerisation of nucleotides
(3) Polymerisation of nucleosides
(4) Polymerisation of amino acids
 Factors affecting Rate of reaction:
1. Temperature: A general rule of thumb is that rate doubles
or decreases by half for every 10°C change in either
direction

2. pH: Every enzyme works at a specific pH (e.g Pepsin works

at ph 1.2- 2.0)

 MECHANISM OF ENZYME ACTION:

 The chemical which is converted into a product is called a

‘substrate’
 Hence enzymes, i.e. proteins with three dimensional
structures including an ‘active site’, convert a substrate (S)
into a product (P)

 Substrate ‘S’ has to bind the enzyme at its ‘active site’

within a given cleft or pocket

 Formation of an ‘ES’ complex takes place

 This complex formation is

a transient phenomenon
 During this, a new structure of the substrate called
Transition state structure is formed (unstable state, where
bond breaking/making is completed)

 Structure of substrate gets transformed into the structure of

product (s)

Nature of Enzyme Action:

 The y-axis represents the potential energy content

 The x-axis represents the progression of the structural

transformation or states through the ‘transition state’

 The energy level difference

between S and P. If ‘P’ is at a
lower level than ‘S’, the reaction
is an exothermic reaction
 The ‘S’ has to go through a much higher energy state or
transition state. The difference in average energy content of
‘S’ from that of this transition state is called ‘Activation
energy’(Ea)

 So enzyme works by lowering the Ea

 Factors Affecting Enzyme Activity:

1. Temperature:

 Each enzyme shows its highest

activity at a particular temperature
called optimum temperature
Q. Which element is not found in nitrogenous
base:

(1) Nitrogen
(2) Hydrogen
(3) Carbon
(4) Phosphorus
Q. Which element is not found in nitrogenous
base:

(1) Nitrogen
(2) Hydrogen
(3) Carbon
(4) Phosphorus
 Low temperature preserves the enzyme in a temporarily
inactive state whereas high temperature destroys enzymatic
activity because proteins are denatured by heat

2. pH: optimum pH is required

3. Concentration of Substrate:
 With the increase in substrate concentration, the velocity of
the enzymatic reaction rises at first.

 The reaction ultimately reaches a

maximum velocity (Vmax) which
is not exceeded by any further rise in
concentration of the substrate

 This is because the enzyme molecules are fewer than the

substrate molecules and after saturation of these molecules,
Q. Which of following base pair is wrong:

(1) A-T
(2) G-C
(3) A-C
(4) A-U
Q. Which of following base pair is wrong:

(1) A-T
(2) G-C
(3) A-C
(4) A-U
 There are no free enzyme molecules to bind with the
additional substrate molecules

 Km (Michaelis constant) is that concentration of substrate

where velocity reaches half of Vmax (i.e. Vmax /2)
 Two hypothesis to explain Mechanism of
Enzyme Action:

1. Lock and Key Hypothesis: Given by Emil Fischer

(1894). According to this:

 Both enzyme and substrate molecules have specific

geometrical shapes, similar to the system of lock and key

 The active sites contain special groups having –NH2, -

COOH, -SH for establishing contact with the substrate
molecules
 Just as a lock can be opened by its specific key, a subsbate
molecule (key) can be acted upon by a particular enzyme
(lock)

 This also explains the specificity of enzyme action

 This hypothesis explains how a small concentration of
enzyme can act upon a large amount of the substrate.

 It also explains how the enzyme remains unaffected at

the end of chemical reaction

 The hypothesis explains how a substance having a

structure similar to the substrate can work as
competitive inhibitor.
2. Induced Fit Hypothesis: This hypothesis was proposed by
Koshland (1960).

 According to this hypothesis the active site of the enzyme

does not initially exist in a shape that is complementary to
the substrate but is induced to assume the complementary
shape as the substrate becomes bound to the enzyme

 The active site is induced to assume a complementary

shape in much the same way as the hand induces a change
in the the shape of a glove
 According to this model, Active site contains 2 groups:

(a) Buttressing group: is meant for supporting the substrate

(b) Catalytic group: is meant for catalysing the reaction

 When substrate comes in contact with the buttressing

group, the active site changes to bring the catalytic group
opposite the substrate
 Enzyme inhibition:
 The activity of an enzyme is also sensitive to the presence
of specific chemicals that bind to the enzyme

 When the binding of the chemical shuts off enzyme

activity, the process is called inhibition and the chemical is
called an inhibitor

 Types of inhibitors:

A. Competitive inhibitor: This inhibitor closely resembles

the substrate in its molecular structure and inhibits the
activity of the enzyme
 Due to its close structural similarity with the substrate, the
inhibitor competes with the substrate for the substrate
binding site of the enzyme

1. Effect on Vmax:
 The effect of a competitive inhibitor is reversed by
increasing (S). At a suffciently high substrate concentration,
the reaction velocity reaches the Vmax
2. Effect on Km :
 A competitive inhibitor increases the apparent Km for a
given substrate.
 This means that in presence of a competitive inhibitor more
substrate is needed to achieve ½ Vmax
 EXAMPLES OF COMPETITIVE INHIBITION:
 Inhibition of alcohol dehydrogenase by ethanol in methanol
poisoning

 Inhibition of Succinic dehydrogenase by malonate &

oxaloacetate which closely resembles the substrate
succinate in structure
 Such competitive inhibitors are often used in the control of
bacterial pathogens:
 All cells require folic acid for growth. Folic acid cannot
cross bacterial cell walls by diffusion or active transport

 For this reason bacteria must synthesize folic acid from P-

aminobenzoic acid

 Sulpha drugs are inhibitor and

competes with the substrate
P-amino benzoic acid (PABA)
for the active site of enzyme
 This binding of inhibitor to the enzyme prevents the
synthesis of folic acid and thus bacterial pathogens are
controlled

B. NON COMPETITIVE INHIBITOR:

 Non competitive inhibition occurs when the inhibitor and
substrate bind at different sites on the enzyme
 The non competitive inhibitor can bind to either the free
enzyme or the ES complex, hereby preventing the reaction
from occurring

1. Effect on Vmax: Non-competitive inhibition cannot be

overcome by increasing the concentration of substrate.
Thus, non-competitive inhibitors decrease the Vmax
2. Effect on Km:
 Non-competitive inhibitors do not interfere with the
binding of substrate to enzyme

 Thus, the enzyme shows the same Km in the presence or

absence of the non-competitive inhibitor

 e.g. Cyanide kills an animal by inhibiting cytochrome

oxidase.
C. Allosteric Modulation or Feedback Inhibition:
 The activities of some enzymes, particularly those which
form a part of a chain of reactions (metabolic pathway), are
regulated internally

 Some specific low molecular weight substance, such as he

product(s) of another enzyme further on in the chain, acts
as the inhibitor

 Such a modulator substance binds with a specific site of the

enzyme different from its substrate-binding site.
 This binding increases or decreases the enzyme action.
Such enzymes are called Allosteric Enzymes

 Examples:
(a) Hexokinase which changes glucose to glucose-6-phosphate
in glycolysis, inhibited by glucose-6-phosphate
(b) Enzyme Phosphofructokinase is activated by ADP and
inhibited by ATP

(c) Inhibition of threonine deaminase by isoleucine. Amino

acid isoleucine is formed in bacterium Escherichia coli in
a 5 step reaction from threonine

 When isoleucine accumulates beyond a threshold value, its

further production stops
Q. If the sequence of bases in one strand of
DNA is known then the sequence in other
strand can be predicted on the basis of:

(1) Antiparallel
(2) Complementarity
(3) Polarity
(4) Coiling
Q. If the sequence of bases in one strand of
DNA is known then the sequence in other
strand can be predicted on the basis of:

(1) Antiparallel
(2) Complementarity
(3) Polarity
(4) Coiling
 Classification and Nomenclature of Enzymes:
 Enzymes are divided into 6 classes each with 4-13
subclasses and named accordingly by a four-digit number

1. Oxidoreductases/ Dehydrogenases: Enzymes which

catalyse oxidation & reduction between two substrates

2. Transferases: Enzymes catalysing a transfer of a group

(other than hydrogen). E.g Kinases
3. Hydrolases: Enzymes catalysing hydrolysis of ester, ether,
peptide, glycosidic, C-C, C-halide or P-N bonds.
E.g. All digestive enzymes

4. Lyases: Enzymes that catalyse removal of groups from

substrates by mechanisms other than hydrolysis leaving
double bonds. e.g. Decarboxylase

5. Isomerases: Includes all enzymes catalysing inter-

conversion of optical, geometric or positional isomers

6. Ligases: Enzymes catalysing the linking together of 2

compounds, e.g., enzymes which catalyse joining of C-O, C-
 Properties of Enzymes:

(i) Protein nature: Enzymes are generally proteins. They may

have additional inorganic or organic substances for their
activity.

(ii) Chemical reaction:

 Enzymes do not start a chemical reaction but increase the
rate of chemical reaction

 They do not change the equilibrium but bring about

equilibrium very soon.
(iii) Efficiency:
 The number of substrate molecules changed per minute by
a molecule or enzyme is called turn over number

 The higher the turn-over number, the more efficient an

enzyme is

(iv) Unchanged form: Enzymes are in no way transformed or

used up in the chemical reaction but come out unchanged at
the end of reaction

(v) Enzyme specificity: Enzymes are highly specific in their

action. For example, enzyme maltase acts
on sugar maltose but not lactose or sucrose
 Co-factors:
 there are a number of cases in which non-protein
constituents called cofactors are bound to the the enzyme to
make the enzyme catalytically active. In these instances, the
protein portion of the enzymes is called the Apoenzyme.

 Three kinds of cofactors may be identified:

1. prosthetic groups
2. co-enzymes
3. metal ions
1. PROSTHETIC GROUPS: Are organic compounds and are
distinguished from other cofactors in that they are tightly
bound to the apoenzyme

 For example, in Peroxidase and Catalase (catalyze the

breakdown of hydrogen peroxide to water and oxygen)
HAEM is the prosthetic group and it is a part of the active
site of the enzyme
2. CO-ENZYMES:
 Are organic compounds but their association with the
apoenzyme is only transient, usually occurring during the
course of catalysis

 The essential chemical components of many coenzymes are

VITAMINS, e.g., coenzyme nicotinamide adenine
dinucleotide (NAD) and NADP contain the vitamin Niacin
(vitamin B3)
3. Metal ions:
 They form Coordination bonds with side chains at the
active site and at the same time form one or more
coordination bonds with the substrate

 e.g. Zinc is a cofactor for the proteolytic enzyme

Carboxypeptidase, Alcohol dehydrogenase

 Cl- for Salivary amylase, Ni for Urease, Cu++ & Fe++ (Fe+++)
for Cytochrome oxidase etc.
Q. Which one of the following statements is
correct, with reference to enzymes?

1. Apoenzyme = Holoenzyme + Coenzyme

2. Holoenzyme = Apoenzyme + Coenzyme
3. Coenzyme = Apoenzyme + Holoenzyme
4. Holoenzyme = Coenzyme + Colactor
Q. Which one of the following statements is
correct, with reference to enzymes?

1. Apoenzyme = Holoenzyme + Coenzyme

2. Holoenzyme = Apoenzyme + Coenzyme
3. Coenzyme = Apoenzyme + Holoenzyme
4. Holoenzyme = Coenzyme + Colactor
Q. The essential chemical components of many
coenzymes are (NEET 2013)

1. Proteins
2. Nucleic acids
3. Carbohydrates
4. Vitamins
Q. The essential chemical components of many
coenzymes are (NEET 2013)

1. Proteins
2. Nucleic acids
3. Carbohydrates
4. Vitamins
Q. Identify the enzyme in : 3.1.2.1

(a) Dehydrogenase
(b) Ligase
(c) Dipeptidase
(d) Aldolase
Q. Identify the enzyme in : 3.1.2.1

(a) Dehydrogenase
(b) Ligase
(c) Dipeptidase
(d) Aldolase
Q. Enzymes used in feedback inhibition are
called:

(a) Allosteric enzymes

(b) Coenzymes
(d) Pro enzymes
(c) Holoenzymes
Q. Enzymes used in feedback inhibition are
called:

(a) Allosteric enzymes

(b) Coenzymes
(d) Pro enzymes
(c) Holoenzymes