Biomolecules

SYNOPSIS

 All the carbon compounds which we get from living tissues can be called biomolecules.
MICROMOLECULES MACROMOLECULES
•Mol.wt. 18 to 800 Da •Mol.wt. 10,000 Da or above
•Present in acid soluble pool •Present in acid insoluble pool
•Glucose •Protein
•Ribose •Nucleic acid
•Amino acids •Polysaccharide
•Nitrogen bases •Lipid
•Nucleosides
•Nucloetides

 Macromolecules and their Functions

MACROMOLECULES DESCRIPTION FUNCTION
Polysaccharides  Mainly compounds of C, H and O.  Starch, glycogen -
 Homopolysaccharides: Made of only 1 type Storage food in plants
of monosaccharide monomer (e.g. starch, and animals.
glycogen, cellulose, chitin, insulin).  Cellulose, chitin -
 Heteropolysaccharides: Made of more than Provide a framework
1 type of monosaccharide monomer. to cells.
Lipids  Mainly fats and their derivatives.  Fats are oxidised to
 Simple lipids contain 1 molecule of glycerol obtain energy.
and 3 molecules of long chain fatty acids.  They also act as food
 Conjugated lipids contain other substances reserves.
such as a phosphate group, protein molecule
or carbohydrate molecule.
 Derived lipids are formed or derived by the
hydrolysis of simple or conjugated lipids.
Nucleic acids  Composed of polynucleotide chains -  DNA acts as the
pentose sugar, nitrogenous base, phosphoric genetic material
acid.  RNAs show
 DNA - Contains deoxyribose pentose sugar
enzymatic activities
 RNA - Contains ribose pentose sugar
Proteins  Folded linear heteropolymers of amino  Transport of
acids. nutrients across the
 Primary structure: Sequence of amino acids cell membrane
in a polypeptide chain of a protein.  Fighting infectious
 Secondary structure: Formation of agents
hydrogen bonds between carboxyl oxygen  Act as hormones and
and hydrogen atoms of other amino acids enzymes
belonging either to the same polypeptide
chain or to a different polypeptide chain.
 Tertiary structure: Long protein
polypeptide chains fold and bend on
themselves extensively.

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  Quaternary structure: Each polypeptide
chain is a subunit of the protein molecule.
 Anabolism is the process by which large, complex molecules are made of simpler molecules.
 Catabolism is the process by which large complex molecules are broken down into small, simpler
compounds.
 The rate of reaction refers to the amount of product formed
per unit.
Rate = p/t
 To initiate any chemical reaction, the substrate acquires
a certain amount of energy which is called energy of activation.
 When the substrate is bound to the enzyme’s active site,
a new structure called the transition state structure is formed.

 Mechanism of Enzyme Action

Substrate binds to the active site and fits itself perfectly into the active site.

The binding induces little alternation in the shape of the enzyme so that the substrate can
fit more tightly.

The active site once in close proximity of the substrate breaks the chemical bonds of the
substrate, and a new enzyme-product complex is formed.

Once the new bonds are formed, the enzyme releases the product molecule.

The free enzyme is again ready to bind to another molecule of the substrate.

 Factors Affecting Enzyme Activity

Substrate
Temperature pH Inhibitors
concentration

 Classification and Nomenclature of Enzymes

Oxido
Transferases Hydrolases Lyases Isomerases Ligases
reductases

 Some enzymes are associated with non-protein substances which make the enzyme catalytically
active. Such non-protein groups are called co-factors.
 Prosthetic group (e.g. peroxidase has haem as the prosthetic group)
 Co-enzymes (e.g. Coenzyme A)
 Metal ion (e.g. zinc associates with carboxypeptidases)

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