The document provides details about biomolecules found in living organisms. It discusses the chemical composition of tissues and cells, including micro and macromolecules. Specific biomolecules covered include amino acids, sugars, lipids, nucleotides, and proteins. The roles and structures of these biomolecules are described. Additionally, the document outlines metabolic pathways and explains the role of enzymes in catalyzing biochemical reactions. In summary, the document is a comprehensive overview of the major biomolecules found in living organisms, their structures and functions, as well as enzymatic processes and metabolism.

1. SHAHINA AKHTER
XI A
GULF ASIAN ENGLISH SCHOOL

3. 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

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

5. 2.BIOMOLECULES OF CELLS
CHEMISTRY
MICROMOLECULES
BIOLOGICAL
MACROMOLECULES

6. M < 1000 MICROMOLECULES
(i)Amino acids
(ii)Sugars
(iii)Nucleotides
(iv)Lipids
M > 1000 BIOMACROMOLECULES
(i)Polysaccharides
(ii)Nucleic acids
(iii)Proteins

7. • 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

8. 3. AMINO ACIDS

9. (i) Basic amino acids
Lysine
(ii)Acidic amino acids
Glutamic acid
(iii)Neutral amino acids
Alanine

10. Aromatic amino acids
Phenyl alanine

11. 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)

12. Glucose
Galactose

13. • 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

14. Maltose

15. 5.LIPIDS
• Heterogenous group of organic compunds
• Water insoluble but soluble in non-polar
organic solvents

16. Lipids
Straight chain compounds Fused hydrocarbon rings+ long
hydrocarbon chain e.g,
cholesterol
Simple lipids Compound lipids
Oil Fats Waxes Phospholipids Glycolipids Sphingolipids

17. CHOLESTEROL

18. • Lipids fatty acid
COOH – R ( -CH3 , -C2H5 , -CH2)

19. Fatty acids
Saturated fatty acids Unsaturated fatty
– butyric acid acids – linoleic acid

20. 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)

21. • Phospholipids – when lipids have P & phosphorylated organic
compounds e.g. lecithin
• Brains have sphingolipids
PHOSPHOLIPID
- LECITHIN

22. 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

24. • Purine + pyridimine monomers
• Higher nucleotides store energy in their high energy P
bonds
• Nicotinamide + riboflavin coenzymes
• Coenzymes : non – protein organic moiety of
holoenzyme

25. 7.PRIMARY & SECONDARY
METABOLITES
PRIMARY SECONDARY
IDENTIFIABLE PRDTS OF CERTAIN
FUNCTIONS METABOLIC PATHWAYS

26. • 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

27. 8.BIOMACROMOLECULES
• M > 1000 daltons
• Found in acid – insoluble fraction
POLYSACCHARIDES NUCLEIC ACIDS PROTEINS LIPIDS

28. 9. POLYSACCHARIDES
HOMOPOLYSACCHARIDES HETEROPOLYSACCHARIDES
(CELLULOSE , STARCH) (CHITIN)

29. MONOMER GLUCOSE
PRESENT IN PLANT CELL WALL

30. Starch Glycogen Inulin
GLUCOSE GLUCOSE FRUCTOSE
PLANTS ANIMALS
STORAGE STORAGE
POLYSACCHARIDE POLYSACCHARIDE

33. Amylose

34. Amylopectin

35. 10.NUCLEIC ACIDS
DNA RNA

38. RIBONUCLEIC ACID (RNA)

40. 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

41. 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

42. STRUCTURE OF PROTEINS
(i) Primary structure

43. (ii) SECONDARY STRUCTURE

44. (iii) TERTIARY STRUCTURE

45. (iv) QUARTERNARY STRUCTURE

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

47. PROTEINS
SIMPLE CONJUGATE
Composed of amino acids Peptide chain & cofactor
(histones, albumins)

48. 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)

49. 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

50. 12.CONCEPT OF METABOLISM
METABOLIC PATHWAYS – DYNAMIC STATE OF BODY CONSTITUENTS
LINEAR CIRCULAR

51. 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

52. 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

53. 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

54. 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

55. 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 .

56. 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

57. CLASS 2 : TRANSFERASES
• They catalyse transfer of specific groups from 1
substrate to another
• Glutamate pyruvate transaminase
• S – G + S’ S + S’- G

58. CLASS 3 : HYDROLASES
• Catalyse breakdown of larger molecules into smaller
molecules with addition of H2O
Amylase hydrolases starch

59. 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

60. CLASS 5 : ISOMERASES
• Catalyse rearrangement of atoms in a molecule to
form isomers
• Phosphohexose isomerase converts glucose 6-
phosphate into fructose -6-phosphate

61. 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

62. MECHANISM OF ENZYME ACTION
(LOCK & KEY HYPOTHESIS)

63. 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

65. FACTORS AFFECTING ENZYME
ACTION
• Temperature

66. • Effect of pH

67. • Effect of substrate concentration

68. • 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

70. • Feed back inhibition: Enzyme activity is inhibited
by prdt of same enzyme reaction
GLUCOSE-6-PHOSPHATE
INHIBITS ACTION OF HEXOKINASE
CATALYSES
PHOSPHORYLATION OF GLUCOSE

71. • Co-factors
ENZYMES
SIMPLE ENZYMES CONJUGATE ENZYMES
Made of 1/several polypeptide Has non-protein moiety + polypeptide chain

72. 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

73. 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.