SHAHINA AKHTER

XI A
GULF ASIAN ENGLISH SCHOOL
 1. ANALYSIS OF CHEMICAL COMPOSITION OF
LIVING ORGANISMS

• Take a living tissue, weigh & grind it in trichloroacidic acid

• Thick slurry is filtered through cheese cloth

Filtrate Retentate
• Inorganic compounds – ‘ash analysis’
• Living tissue is weighed to get wet weight
• This is dried dry weight
• C CO2 + H2O
• Ca, Mg, Na, K
 2.BIOMOLECULES OF CELLS

CHEMISTRY

MICROMOLECULES

BIOLOGICAL
MACROMOLECULES
M < 1000 MICROMOLECULES

(i)Amino acids
(ii)Sugars
(iii)Nucleotides
(iv)Lipids

M > 1000 BIOMACROMOLECULES

(i)Polysaccharides
(ii)Nucleic acids
(iii)Proteins
• Acid-soluble fraction cytoplasmic composition
• Acid-insoluble fraction macromolecules of
cytoplasm + cell organelles

COMPONENTS %

(i) Water 70 – 90
(ii) Proteins 10 – 15
(iii) Nucleic acids 5–7
(iv) Carbohydrates About 3
(v) Lipids About 2
(vi) Ions About 1
3. AMINO ACIDS
(i) Basic amino acids
Lysine

(ii)Acidic amino acids

Glutamic acid

(iii)Neutral amino acids

Alanine
Aromatic amino acids

Phenyl alanine
 4.SUGARS
• Monosaccharides : simplest sugars, which cannot be
hydrolysed further into smaller sugars
• Composed of 3-7 C atoms :
(i) Triose (3C) (Glyceraldehyde)
(ii) Tetrose (4C) (Erythrose)
(iii) Pentose (5C) (Ribose)
(iv) Hexose (6C) (Glucose)
(v) Heptose (7C) (Sedoheptulose)
Glucose

Galactose
• Monosaccharides have either a free CHO / CO
group reducing sugars
• Oligosaccharides : when 2/ few
monosaccharides are combined by glycosidic
bonds
• They are named as:
(i) Disaccharides (2) : Sucrose
(ii) Trisaccharides (3) : Arabinose
(iii) Tetrasaccharides (4) :Stachyose
(iv) Pentasaccharides (5) : Verbascose
Maltose
 5.LIPIDS
• Heterogenous group of organic compunds

• Water insoluble but soluble in non-polar

organic solvents
 Lipids

Straight chain compounds Fused hydrocarbon rings+ long

hydrocarbon chain e.g,
cholesterol

Simple lipids Compound lipids

Oil Fats Waxes Phospholipids Glycolipids Sphingolipids

CHOLESTEROL
• Lipids fatty acid
COOH – R ( -CH3 , -C2H5 , -CH2)
 Fatty acids

Saturated fatty acids Unsaturated fatty

– butyric acid acids – linoleic acid
Simple lipid – glycerol

Formed by esterification of glycerol with fatty acids –

monoglycerides , diglycerides , triglycerides

Fats – high m.p & remain soilds at room temp (Butter)

Oils – low m.p & remain liquids at low room temp (Sunflower
oil)
 • Phospholipids – when lipids have P & phosphorylated organic
compounds e.g. lecithin

• Brains have sphingolipids

PHOSPHOLIPID
- LECITHIN
 6.NUCLEOTIDES

Phosphorylated nucleosides – adenylic acid, guanylic acid,

thymidylic acid, cytidylic acid & uridylic acid

N base attached to pentose sugar – adenosine, guanosine,

thymidine, cytidine & uridine
• Purine + pyridimine monomers

• Higher nucleotides store energy in their high energy P

bonds

• Nicotinamide + riboflavin coenzymes

• Coenzymes : non – protein organic moiety of

holoenzyme
 7.PRIMARY & SECONDARY
METABOLITES

PRIMARY SECONDARY

IDENTIFIABLE PRDTS OF CERTAIN

FUNCTIONS METABOLIC PATHWAYS
• PRIMARY METABOLITES – amino acids, N bases,
proteins, nucleic acids, etc.
• SECONDARY METABOLITES
(i) Pigments : Anthocyanin, carotenoids
(ii) Drugs : Vinblastin, curcumin
(iii) Alkaloids : Morphine, codeine
(iv) Essential oils : Lemon grass oil
(v) Lectins : Concanavalin A
(vi) Terpenoids : Monoterpenes
(vii) Toxins : Abrin, Ricin
(viii) Polymeric Compounds : Rubber, cellulose, gums
 8.BIOMACROMOLECULES
• M > 1000 daltons
• Found in acid – insoluble fraction

POLYSACCHARIDES NUCLEIC ACIDS PROTEINS LIPIDS

 9. POLYSACCHARIDES

HOMOPOLYSACCHARIDES HETEROPOLYSACCHARIDES
(CELLULOSE , STARCH) (CHITIN)
 MONOMER GLUCOSE

PRESENT IN PLANT CELL WALL

Starch Glycogen Inulin

GLUCOSE GLUCOSE FRUCTOSE

PLANTS ANIMALS

STORAGE STORAGE
POLYSACCHARIDE POLYSACCHARIDE
Amylose
Amylopectin
 10.NUCLEIC ACIDS

DNA RNA
RIBONUCLEIC ACID (RNA)
 mRNA : Carries information from DNA to ribosome
Decides sequence of amino acids

tRNA: Carries an amino acid from cytoplasm to

r ibosome

rRNA: Forms parts of ribosomes

Forms part of seat of protein synthesis
 11.PROTEINS
• Heteropolymers containing string/strings
of amino acids
• Types of proteins result from 20 amino
acids
• Depending on
• (i) no. of amino acid residues
• (ii)sequence of amino acids
STRUCTURE OF PROTEINS
(i) Primary structure
(ii) SECONDARY STRUCTURE
(iii) TERTIARY STRUCTURE
(iv) QUARTERNARY STRUCTURE
 CLASSIFICATION
PROTEINS

FIBROUS GLOBULAR
Polypeptides arranged in parallel bundles Polypeptides become coiled &
(silk fibres, keratin & collagen) folded (albumin, globulin,
haemoglobin )
 PROTEINS

SIMPLE CONJUGATE
Composed of amino acids Peptide chain & cofactor
(histones, albumins)
 CONJUGATE PROTEINS
• Chromoproteins – pigments along with amino acids
(haemoglobin)
• Lipoproteins – lipids in their molecules (egg yolk)
• Phosphoproteins – phosphate grp with amino acids
(casein of milk)
• Metalloproteins – contain metallic ion with amino acids
(Zn carbonic anhydrase)
• Glycoproteins – contain carbohydrates with amino acids
• Nucleoproteins – contain nucleic acids with amino acids
(virus)
 PROTEINS FUNCTIONS

1. Collagen Intercellular/extracellular
ground substance

2. Trypsin Enzyme to digest protein

3. Insulin A hormone that regulates

glucose level

4.Gamma globulin Antibody, that fights against

infections
5.Receptors Proteins that receive
stimulus/substance
6.GLUT- T Regulates transport of
glucose into cells
12.CONCEPT OF METABOLISM
METABOLIC PATHWAYS – DYNAMIC STATE OF BODY CONSTITUENTS

LINEAR CIRCULAR
 METABOLISM

ANABOLISM CATABOLISM
More complex Complex substance is
compounds are formed broken into 2 / more
from simple ones smaller substances
(proteins synthesis) (Digestion of proteins
by peptides
 13. ENZYMES
CHARACTERISTICS OF ENZYMES
• Proteins that catalyse biochemical reactions in living
cells

• Each enzyme catalyses the reaction of 1 substrate

• Each enzyme requires a specific pH & temp

• They accelerate a reaction

SIMILARITIES BETWEEN ENZYMES
& INORGANIC CATALYSTS

• Catalysts remain unchanged at the end of the reaction

& they can be used again
• Required in far less quantities as compared to the
substrate
• Do not initiate a reaction, but rate of reaction by
lowering activation energy
• Do not alter eqm of a reversible reaction
• Form short-lived complexes with substrates
 DIFFERENCES B/W ENZYMES &
INORGANIC CATALYSTS
ENZYMES INORGANIC CATALYSTS

All enzymes are proteins & have complex Usually small & simple molecules
molecular organisation

An enzyme catalyses only a specific reaction They can catalyse a no. of reactions, hence
are not specific for any 1 reaction

Enzyme action can be regulated by specific Cannot be regulated by any other molecule
molecules

These are more sensitive to changes in pH & They are v.less affected by changes in pH &
temp of medium temp of medium
 NOMENCLATURE OF ENZYMES
• Adding suffix ‘ase’ to the substrate on which they act
e.g.,sucrase , protease etc.
• Acc. To physiological activity it catalyses e.g.,oxidase
, dehydrogenases, decarboxylase etc.
• Acc. To source from which they are obtained e.g.,
papain, bromelain etc.
• Some have been named like ptyalin, trypsin etc .
 CLASSIFICATION OF ENZYMES

• CLASS 1 : OXIDOREDUCTASES

• Catalyse oxidation /reduction of a substance

• Cytochrome oxidase oxidises cytochromes

• Glycolate oxidase oxidises glycolate

Sreduced + S’oxidised Soxidised + S’reduced

 CLASS 2 : TRANSFERASES
• They catalyse transfer of specific groups from 1
substrate to another

• Glutamate pyruvate transaminase

• S – G + S’ S + S’- G
 CLASS 3 : HYDROLASES
• Catalyse breakdown of larger molecules into smaller
molecules with addition of H2O

Amylase hydrolases starch

 CLASS 4 : LYASES
• Catalyse cleavage of specific covalent bonds &
removal of specific groups , without the use of H2O

Histidine decarboxylase cleaves histidine into histamine

& CO2
X Y

C–C X–Y +C=C

 CLASS 5 : ISOMERASES
• Catalyse rearrangement of atoms in a molecule to
form isomers

• Phosphohexose isomerase converts glucose 6-

phosphate into fructose -6-phosphate
 CLASS 6 : LIGASES
• Catalyse covalent bonding b/w 2 substrates to form a
large molecule, mostly involving utilisation of energy
by hydrolysis of ATP

RuBP carboxylase catalyses the joining of RuBP & CO2

in photosynthetic C fixation
MECHANISM OF ENZYME ACTION
(LOCK & KEY HYPOTHESIS)
 CATALYTIC CYCLE :
(i) Substrate binds to active site of enzyme
(ii) Binding of substrate induces the enzyme to alter its
shape & fit more tightly around substrate
(iii) Active site of enzyme, now in close proximity of
substrate breaks the chemical bonds of substrate &
an enzyme-product complex is formed
(iv) Enzyme releases the product of reaction & the free
enzyme is ready to take up another molecule of
substrate
 FACTORS AFFECTING ENZYME
ACTION
• Temperature
• Effect of pH
• Effect of substrate concentration
• Effects of chemicals
When binding of a chemical reduces / shuts off the enzyme
activity, the chemical is called inhibitor.
INHIBITORS

COMPETITIVE NON-COMPETITIVE
When inhibitor closely resembles substrate When inhibitor does not compete
in molecular structure & binds to active site with substrate for active site
of enzyme
• Feed back inhibition: Enzyme activity is inhibited
by prdt of same enzyme reaction

GLUCOSE-6-PHOSPHATE

INHIBITS ACTION OF HEXOKINASE

CATALYSES

PHOSPHORYLATION OF GLUCOSE
• Co-factors
ENZYMES

SIMPLE ENZYMES CONJUGATE ENZYMES

Made of 1/several polypeptide Has non-protein moiety + polypeptide chain

 COFACTOR

PROSTHETIC GROUP COENZYME METAL IONS

METAL IONS FORM CO-

TIGHTLY BOUND BOUND TO
ORDINATION BONDS
TO APOENZYME APOENZYME DURING
WITH SIDE CHAIN AT
COURSE OF CATALYSIS
ACTIVE SITE OF
ENZYME & SUBSTRATE

HAEM NAD & NADP Zn

I would like to express my special thanks of gratitude to
my teacher Mrs. Alarmelu Natchiar as well as our
principal Mrs Nasreen Banu who gave me the golden
opportunity to do this wonderful presentation on the topic
BIOMOLECULES, which also helped me in doing a
lot of Research and i came to know about so many new
things
I am really thankful to them.
Secondly I would also like to thank my parents and
friends who helped me a lot in finishing this presentation
within the limited time.

I am making this presentation not only for marks but to

also increase my knowledge .
THANKS AGAIN TO ALL WHO HELPED
ME.