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All the carbon compounds that we get from living body can be called
Biomolecules.
Amino acids
Amino acids are organic compounds containing an amino group and an acidic
group as substituents on the same carbon i.e., the - Carbon. Hence, they
are called
- amino acids.
There are four substituent groups occupying the four valency positions. These
are hydrogen, carboxyl group, amino group & a R group.
Based on nature of R group there are many amino acids. However, those which
occur in proteins are only of 20 types.
In glycine, R group is hydrogen, in alkine, R group is methyl, in serine it is
hydroxy methyl etc.
COOH
H C NH2
H
COOH
H C NH2
CH3
COOH
H C NH2
CH2 OH
Glycine
Alanine
Serine
The chemical and physical properties of amino acids are essentially of the amino,
carboxyl & the R functional groups.
Based on number of amino & carboxyl groups, there are acidic (glutamic acid),
basic (lysine) and neutral (valine) amino acids.
Similarly, there are aromatic amino acids like tyrosine, phenylalanine, tryptophan
etc.
A particular property of amino acid is the ionizable nature of NH 2 & -COOH
groups.
NH3+ - C COOH
Zwitter ionic form
Lipids
Lipids are generally water insoluble.
They are made up of fatty acids. A fatty acid has a carboxyl group attached to
an R group. (R is an alkyl group).
Eg: palmitic acid, Arachidonic acids.
Fatty acids can be saturated (C C) or Unsaturated ( C = C )
Another simple lipid is glycerol which is trihydroxy propane. Many lipids have
both glycerol & fatty acids. They can be monoglycerides, diglycerides &
triglycerides.
Lipids are categorised into oils & fats depending on their melting points. Fats
are solids at room temp & oil are liquids at room temp.
Some lipids are associated with phosphorus and are called phospholipids. They
are found in cell membrane. Eg. Lecithin.
Nitrogen bases
Nitrogen bases are organic compounds with heterocyclic rings and found in
nucleic acids. Eg: Adenine, guanine, cytosine, Thymine, Uracil.
Nitrogen bases when attached to sugar, are called nucleosides & when
nucleosides are attached to phosphate group, they are called as nucleotides.
Adenosine, guanosine, cytodine, thymidine, uridine are nucleosides.
Adenylic acid, Guanylic acid, Thymidylic acid, Guanylic acid, cytidylic acid &
ridylic acid are nucleotides.
DNA & RNA function as genetic material.
Adenine & guanine are called purines & cytosine, Thymine & uracil are called
pyrimidines.
Starch forms helical structure & thus, can hold I2 molecules. The starch I2 is
blue in colour. Cellulose does not contain complex helical structure & hence
cannot hold I2.
Plant cell wall, cotton fibre, paper contain cellulose.
There are more complex polysaccharides in nature. They have building blocks
like amino-sugar & chemically modified sugars.
(eg: glucosamine, N-acetyl galactosamine etc).
Exoskeleton of arthropuda has complex polysaccharides called chitin. These
complex polysaccharides are heteropolymers.
Nucleic Acids
It is another nacromolecule of acid insoluble fracton. They are oplymer of
nucleotides (polynucleotides)
A nucleotide has heterocyclic nitrogen bases, a monosaccharide & a phosphate
group(phospharic acid).
In DNA, deoxyribose sugar is present & in RNA, ribose sugar is present.
Structure of proteins.
The arrangement of amino acids in a sequence is called primary structure of
protein.
A protein is imagined as a line. The left end represented by the first amino acid
called N-terminal amino acid. The right end represented by the last amino acid
called C-terminal amino acid.
A protein chian does not exist as an extended rigid rod. It is folded in the form of
a helix. The folded form of helix forms secondary & teritiary structure, thus
it gives 3 dimensional view of protein.
Some proteins are an assembly of more than one poly peptide or subunits. This
is known as quaternary structure of protein.
Adult human haemoglobin consists of 4 subunits. Two of these are identical to
each other. Hence, two subunits of type & two subunits of type
together constitute the human haemoglobin (Hb).
Chemical reactions
A chemical reaction is a process in which reactants are converted into products.
Ba(OH)2 + H2SO4
BaSO4 + 2H2O
Reactants
Products
Rate of reaction refers to the amount of products formed per unit time.
p
p
Rate = t or t
As a general rule, rate of a reaction doubles for every 10oC rise in temperature
But, catalyzed reactions proceed at very high rate.
CO2 reacts with water to form carbonic acid. About 200 molecules of H2CO3is
formed in an hour but in presence of a catalyst carbonic anhydrase, 600000
molecules are formed in every second.
In different conditions different products are possible e.g.,
I. Glucose
lactic acid (Anaerobic)
II. Glucose
pyruvic acid (Aerobic)
III. Glucose
Alcohol (Fermentatics)
Mechanism of enzyme catalysis
A reaction takes place when the reacting molecules collide. However, products
are formed only if the colloiding molecules possess a definite amount of energy
called threshold energy.
In the reacting system, the difference between the threshold energy & the
average energy of the molecules is called activation energy.
If this difference (activation energy) is large an alternate path for the reaction
such that activation energy is lowered. Thus, the reaction becomes faster.
During enzyme catalysis, the substrate binds to the active site of the enzyme to
form a complex.
E+S
ES ( Enzyme substrate complex )
The enzyme-substrate complex breaks into products releasing the enzyme and
the free enzyme is ready to bind to another molecule of substrate.
ES
P+E
(Product)
Oxidoreductases (dehydrogenases)
Catalyse oxidation-reduction reactions
II.
Transferases
Catalyse transfer of a group between a pair of substrates Eg.- Kinase
III.
Hydrolases
Catalyse hydrolytic reactions. Eg.- Proteases
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IV.
V.
VI.
Lyases
Catalyse removal of group from substrate & leave double bonds.
X
XY+C=C
Eg.-Hydrases
Isomerases
Catalyseinterconversion of isomers. Eg.- epimerase
Ligases
Catalyse the linking together of two compound. Eg.-DNA ligase.
Nomenclature
Enzymes are named after the substrates on which these act, by adding the
suffix-asewith the substrate. Eg.- Lipase (lipid), sucrose (sucrose) ets.
Co-factors
For the proper functioning of certin enzymes, these must be associated with
small non protein compounds calledco-factors. Here, protein part of enzyme is
called apoenzyme. There are 3 kinds of co-factors.
I.
Prosthetic group
they are organic compounds that are tightly bound to the apoenzyme.
For e.g., In Peroxide, thatcatalyse breakdown of hydrogen peroxide,
haem is the prothetic group.
II.
Co-enzymes
They are organic compounds that bind to apoenzyme is only transient,
(association only during catalysis) E.G- Vitamins.
Co-enzyme nicotinamideaderisedisucleotide (NAD) & NADP contain the
vitamin niacin (B5)
III.
Metal ions
Metal ions form co-ordination bond with the active site of enzymes. E.gzinc is co-factor for carboxypeptidase.
Assignment
1. Describe the important properties of enzymes.
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