SHAHINAAKHTER

XIA
GULFASIANENGLISHSCHOOL
 1. ANALYSIS OF CHEMICAL COMPOSITION OF
LItfING ORGANISMS

• Take a living tissue, weigh & grind it in

trichloroacidic acid
• Thick slurry is filtered through cheese cloth

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

CHEMISTRY

MICROMOLECULES

B I O L O G I C AL
MACROMOLECULES
M< MICROMOLECULES
1000
(i)Amino
acids
(ii)Sugars
(iii)Nucleotid
es (iv)Lipids
M> BIOMACROMOLECULES
1000
(i)Polysacchari
des (ii)Nucleic
acids
(iii)Proteins
• Acid-soluble fraction cytoplasmic
• Acid-insoluble fraction composition
cytoplasm + cell macromolecules of
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)
Glucos
e

Galacto
se
• 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) : tferbascose
Maltos
e
 5.LIPIDS
• Heterogenous group of organic
compunds

• Water insoluble but soluble in non-

polar organic solvents
 Lipids

Straight chain Fused hydrocarbon rings+

compounds long hydrocarbon chain
e.g, cholesterol

Simple Compound
lipids lipids

Oil Fats Waxe Phospholipids Glycolipids

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

Saturated fatty Unsaturated

acids fatty acids –
– butyric acid 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) Pigmen : Anthocyanin,
ts carotenoids
(ii)
(iii) Drugs
Alkaloids : tfinblastin, curcumin
(iv) Essential :: Morphine, codeine
Lemon grass
oils
(v) Lectins oil
(vi) Terpenoi : Concanavalin
ds A
(vii)
(viii) Toxins
Polymeric Compounds: Monoterpenes
: Rubber,
cellulose, gums : Abrin, Ricin
 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

Starc Glycoge Inulin
h n

GLUCOSE GLUCOSE FRUCTOSE

PLANTS ANIMALS

STORAGE STORAGE
POLYSACCHARIDE POLYSACCHARIDE
Amylos
e
Amylopect
in
 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 Polypeptides become
bundles (silk fibres, keratin & coiled & folded (albumin,
collagen) globulin, haemoglobin )
 PROTEINS

SIMPLE CONJUGATE
Composed of amino Peptide chain &
acids (histones, cofactor
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. Intercellular/extracellu
Collage lar
n ground substance
2. Enzyme to digest
Trypsi protein
n3. A hormone that
Insuli regulates
n glucose level
4.Gamma Antibody, that fights
globulin against
5.Recepto infectio
rs ns Proteins that
6.GLUT- T receive
stimulus/substance
Regulates
transport
of glucose into cells
12.CONCEPT OF METABOLISM
METABOLIC PATHWAYS – DYNAMIC STATE OF BODYCONSTITUENTS

LINEAR CIRCULAR
 METABOLISM

ANABOLISM CATABOLISM
More complex Complex
compounds are substance is
formed from broken into 2 /
simple ones more smaller
(proteins synthesis) substances
(Digestion of
 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, rate of reaction
but lowering activation by
energy
• Do not alter eqm of a reversible
reaction
 DIFFERENCES B/W ENZYMES &
INORGANIC CATALYSTS
ENZYMES
All enzymes are proteins & have
complex
molecular organisation
An enzyme catalyses only a specific
reaction
Enzyme action can be regulated by
specific molecules
These are more sensitive to changes
in pH & temp of medium
INORGANIC CATALYSTS
Usually small & simple molecules
They can catalyse a no. of reactions,
hence are not specific for any 1
reaction
Cannot be regulated by any other
molecule
They are v.less affected by changes in
pH & 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 + Soxidised +
S’oxidised 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
• Temperatu
re
• 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
• F e e d b a c k i n h i b i t io n : E n z y m e a c t i v i t y is i n h i b i t e d
b y p r d t of s a m e e n z y m e re a c t i o n

GLUCOSE-6-PHOSPHATE

INHIBITS ACTION OF HEXOKINASE

CATALYSES

PHOSPHORYLATION OF GLUCOSE
• Co-
ENZYMES
factors

SIMPLE ENZYMES CONJUGATE ENZYMES

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

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
ACTItfE SITE OF ENZYME
& SUBSTRATE

HAEM NAD & NADP Zn