BIOMOLECULES

• These are elements of which living organisms are made up of. It is somewhat similar

to the earth's crust components.

• The study of various organic and inorganic molecules in a cell and their role in the

physiological process of the cell is called biochemistry.

This table depicts the comparison between elements present in living and nonliving

matter.

Elements % in Earth's crust %in the Human body

Hydrogen 0.14 0.5

Carbon 0.03 18.5

Oxygen 46.6 65.0

Nitrogen Very Little 3.3

Sulphur 0.03 0.3

Sodium 2.8 0.2

Calcium 3.6 1.5

Magnesium 2.1 0.1

Silicon 27.7 Negligible

How to analyze chemical composition?

Trichloroacetic acid is used to fractionate Biomolecules. We get 2 fractions after

treatment.

Acid soluble fraction:- In the filtrate

• Contain all micro molecules except lipids.

Acid insoluble fraction

• Contain macromolecular and lipids.

Primary and secondary metabolites

Primary Metabolites - These are the metabolites that have direct involvement in

growth, development, and reproduction.

Example:- Amino acid

Secondary Metabolite - They are not directly involved in growth and development.

Example:- Alkaloids, Toxins, Drugs

Biomolecules are of 2 types

Biomicromolecules:- Compounds having a molecular weight of less than 1000

dalton are called biomicromolecules.

Example:- Amino acid

Biomacromolecule: Compounds having a molecular weight of range of 10 thousand

daltons ( except lipids ) are called biomacromolecules.
 Example:- carbohydrates

Type of Biomolecule

Carbohydrates:-

• They are the biomacromolecules made up of C, H, O

• Commonly called saccharides.

• It can be monosaccharides, oligosaccharides, polysaccharides

Monosaccharides Oligosaccharides Polysaccharides

They are made up of a single They are made up of 2 -10 units. They are made up of more than 10 units.

unit.

Sweet in taste. Sweet in taste. Not sweet in taste.

They are sugar. They are sugar They are non-sugar.

Example - Example- Example -

Triose - Glyceraldehyde Disaccharides - Maltose, Lactose, Starch -

Tetrose - erythrulose Sucrose • Stored food in plants.

Pentose - Ribose ,xylose • Homopolymer of alpha D glucose.

Hexose - Glucose, Fructose, Insulin

galactose Trisaccharides - Raffinose • Polymer of fructose

• It is used to check GRF( glomerular

filtration rate).

Heptose - sedoheptulose Tetrasaccharides - Stachyose

 Lipids

• They are micromolecules that yield high energy.

Simple Compound Derived

It includes: Triglycerides It includes:- Phospholipids It includes:- Steroids

• Glycerol+2 fatty acid + • It is a cyclopentano

H3Po4 perhydro phenanthrene

• Example - Lecithin ring.

• Example:- Cholesterol,

Cortisol, Testosterone

Monoglycerides - Monohydroxy Glycolipids Terpenes

alcohol + Fatty acid • Sphingosine + 2 fatty acid • Its unit is isoprene.

• Example:- Bee wax, WaxD, + glucose/galactose • Example:- Camphor,

Ear wax • Example- Cerebroside Menthol

Cutin Chromolipids Prostaglandins

• Formed by cross • Lipid +Pigment • Derived from Arachidonic

esterification of hydroxy • Example:- Rhodopsin acid.

fatty acid.
 • Present in plant cuticles. • They help in smooth

muscle contraction.

• Found in semen,

Menstrual fluid

Suberin Lipoproteins

• Glycerol + suberin Acid • Lipids + Proteins

• Present in root • Example:- Chylomicrons

endodermis.

• Triglycerides are composed of Glycerol + 3 Fatty acid

Fatty Acids are further classified as

Saturated and unsaturated Fatty Acids:

Saturated Unsaturated

CnH2nO is a general formula. CnH2n-2xO2 is a general formula.

n = number of carbon n = no of C

x = no of the double bond

n= 16 Palmitic Acid n =18 ,x=1 ,Oleic, Also called MUFA

n= 18 Stearic Acid ( mono unsaturated fatty acids)

n= 20 Arachidic Acid n= 18, x=2. , Linoleic

n= 18,x =3, Linolenic

Examples of Triglycerides are:-

Fat

• It contains saturated fatty acid.

• Remain solid at room temperature

• Tripalmitin, Tristeric are examples of fat.

Oil

• It contains unsaturated fatty acids.

• Remain liquid at Room temperature.

• Triolein , Gingelly seed are examples of oil

Amino Acid

• They are micromolecules.

• It has 3 groups- R group, COOH, NH2 attached to the alpha carbon.

• All amino acids are optically active except glycine.

• They are small, colorless crystalline solids

They are soluble in water, insoluble in organic solvents. There are 20 amino

acids.

Function

• Glycine is the precursor of Haeme.

• Tyrosine is the precursor of Thyroxine, Melanin

• Tryptophan is the precursor of Niacin.

• Some amino acids act as neurotransmitters. Eg: GABA

Protein

• They are Heteropolymer.

• 2 Amino acids are linked by peptide bonds.

• The most abundant protein in the animal world is Collagen.

• Most abundant protein in the biosphere is - RUBISCO.

• They are classified into 4 types on the basis of folding complexity.

 Primary Structure Secondary Structure Tertiary Structure Quaternary

Structure

• It is a chain of amino • If the primary • When a long When different

acids having many structure shows peptide chain polypeptides with

peptide bonds. folding in some folds upon itself their own level

• It does not show any regions due to H to form a woolen arrange with respect

folding bond formation ball-like to each other it gives

called sec. structure, it is rise to the quaternary

structure called a tertiary structure.

• It is of 2 types:- structure.

alpha-helix and

beta-pleated

sheet.

It tells us about the position It gives a 3D structure

of different amino acids in a to a compound.

chain.

Example:- Found in the keratin of Found in each chain of Found in

Cysteine...Alanine...serine skin, hair haemoglobin haemoglobin.

It is a hypothetical example All chains are

of a primary chain. connected together

to form haemoglobin.
Functions

• Glycoprotein is present in cell membranes.

• Phloem protein is involved in the transportation of nutrients.

• Helps in storage of oxygen . example - Myoglobin

• They act as a regulatory protein in muscle.

• Streptokinase is a clot buster.

• Fibrinogen helps in blood clotting.

Nucleic Acid

• They are composed of Nitrogenous bases + pentose sugar + phosphate

Nitrogenous bases are of 2 type

• Purine:- double-ringed

o Example- Adenine, Guanine

• Pyrimidine:- They are single-ringed.

o Example:- Thymine, Uracil, cytosine

Pentose sugar
• Ribose

• Deoxyribose

Nucleoside= Sugar + Base

Nucleotide = Sugar + Base + phosphate

Examples of nucleic Acids are DNA, RNA

DNA( Deoxyribose Nucleic Acid)

 • Double Helix Structure of DNA cis described by Watson and Crick.

• Bases are attached to sugar N- glycosidic bond in 3' to 5' direction.( 3' C of

nucleotide to 5'C of sugar)

• Phosphates are attached to sugar by phosphodiester bonds.

RNA (Ribonucleic Acid)

• RNA is the genetic material of viruses.

• In cellular organization, it helps in protein synthesis.

• In RNA, uracil is found instead of cytosine.

Metabolic Basis for living

Metabolism = Catabolism + Anabolism

• Catabolic pathway - Pathways that lead to degradation of compounds.

• Anabolic pathway - pathway which leads to the formation of compounds.

Enzyme
• Term enzyme was given by Kuhne.

• Enzymes are bio catalysts made up of protein ( exception -Ribozyme).

• Enzymes are thermolabile..ie..they degrade at high temperature.

Chemical Reactions

• Enzymes are used to catalyse inorganic reactions.

Example:- Carbonic amylase accelerate the reaction by 10 million times

How do Enzymes bring about such a High rate of Chemical

conversations.?
 • Enzymes have active sites..ie..sites for holding the substrate.

• Then convert that substrate into a product by different transition states.

S-P

S ...> ES ....> P+ E Action of enzyme

S= substrate P= product

• Enzymes lower the activation energy.

• Maximum Binding energy is released due to maximum interaction between

enzyme and substrate, which ultimately lowers the activation energy.

Nature of enzyme action

E = enzyme P = product
S = substrate

• Substrate get bind to the active site of an enzyme to form ES complex

ES = enzyme-substrate complex

• This binding leads to shape alteration of active sites.

E + S forms ES COMPLEX..and then EP complex

• Then, enzymes get separated out leaving the product.

Factors affecting enzyme activity

Temperature

• At optimum temperature, the enzyme shows maximum binding.

• The optimum temperature of enzymes is 25°C - 40°C.

• Enzyme activity varies with temperature as shown in the graph.

PH

• Each enzyme has its optimum ph for its maximum functioning.

• Example:- pepsin has an optimum ph of 1.5 - 2.5

• Trypsin has an optimum ph of 7.5 - 8.5

Substrate concentration

• With the fixed molecules of an enzyme, the rate of reaction or velocity

increases with the increase of substrate up to a particular limit.

• Km value - It is the substrate concentration at which enzymes attain half of

their max velocity.

• Km is inversely proportional to the affinity of the enzyme with its substrate.

Inhibitors

• They are the structure resembling the substrate

• Enzymes are sensitive to these inhibitors, thus they affect binding.

• They are of many kinds: Example; Competitive inhibitors, non-competitive

inhibitors, Allosteric inhibitors

Classification and Nomenclature of Enzyme

• Enzyme commission has developed a rule for naming enzymes.

• Enzymes are classified according to the chemical reaction it catalyses.

EC numbers are 4 digit numbers given to each enzyme.

• 1st no. denote - major class

• 2 nd number denote- sub class
 • 3 rd no. denote - sub sub class

• 4 th no. denotes - the serial number in sub sub class .

• The first number, denoting class can be classified into 6 groups

EC1

• OXIDOREDUCTASE

• Example- oxidases, oxygenases

EC2

• TRANSFERASES

• Example:- Kinases

EC3

• HYDROLASES

• Example - Peptidases

EC4

• LYASES

• Example - Aldolases

EC5

• ISOMERASES

• Example - Mutase

EC-6

• LIGASES
 • Example- Carboxylases

Co- factors

Enzymes are of 2 type

• Simple

• Conjugate

The conjugate enzyme has 2 parts

• Protein part called Apoenzyme

• Non-protein part called Cofactors.

• These cofactors can be organic and loosely bound called Coenzyme.

Example- NAD has vitamin niacin

• Cofactors that are organic and tightly bound are called a prosthetic group.

Eg- Haeme in peroxidase.