9.
Biomolecules
Chemical composition
All living organisms, from microbes to mammals, are composed of chemical
substances.
These chemical substances can be organic or inorganic. Chemical analysis is
performed to find out chemical composition of a living cell.
Water is the most abundant chemical compound in a living body.
Most of the organic compounds are found in acid-soluble fraction.
Inorganic compounds such as sulphate, phosphate, etc. are also found in acid-soluble
fraction.
Organic compounds
All carbon compounds obtained from living tissues are known as organic
biomolecules.
These are of two types:
(a) Micromolecules (biomolecules)
(b) Macromolecules (bio-macromolecules)
A. Micromolecules (Biomolecules)
These are organic compounds with molecular weights less than one thousand
Dalton.
Classified as amino acids, sugars, nucleotide bases, fatty acids, etc.
These are also known as primary metabolites.
Secondary metabolites on the other hand are compounds other than primary
metabolites. These are commonly found in plants, fungi, and microbes. For
example- Alkaloids, flavonoids, and essential oils etc. are secondary metabolites.
1. Amino acids
These are organic compounds containing an amino group, carboxyl group,
hydrogen, and a variable functional group (R).
Common structure of an amino acid is
Based on the nature of R group, there are many amino acids, but only 20 types
of amino acids constitute proteins.
Simplest amino acid is glycine that contains hydrogen as the R group.
Structure of glycine is
Amino acids can be acidic (when carboxylic group is more, e.g. glutamic acid),
basic (when amino group is more, e.g. lysine) or neutral (when both carboxylic
and amino group are same in number, e.g. Valine).
2. Fatty acids
Organic compounds containing a carboxyl group attached to an R group
R group is variable and contains 1 to 19 carbons.
Fatty acids can be saturated (without C=C double bond) or unsaturated (with
one or more C=C double bonds).
These are water insoluble compounds.
Structure of fatty acid (palmitic acid)
CH3 — CH2 14 — COOH
Fatty acids are esterified with glycerol to form monoglycerides, diglycerides,
and triglycerides.
Structure of triglycerides is
3. Nitrogen bases
These are organic compounds containing heterocyclic rings.
Adenine, guanine, cytosine, uracil, and thymine are nitrogen bases.
Structure of adenine is
When attached to sugar, these are known as nucleosides.
When a phosphate group is also attached along with sugar, these are known as
nucleotides.
B. Bio-macromolecules
Organic compounds with molecular weights in the range of ten thousand Daltons
and more are known as bio-macromolecules. Lipids are an exception.
These are found in acid insoluble fraction.
These are classified as proteins, polysaccharides, nucleic acids, etc.
1. Proteins
Proteins are linear chains of amino acids linked by peptide bonds, hence also
known as polypeptides.
A peptide bond is formed between the carboxyl group of one amino acid and the
amino group of next amino acid.
Structure of peptide bond-
Essential amino acids (obtained through diet or food) are part of dietary
proteins.
Functions of proteins:
1. To transport nutrients
2. Fighting infections
3. Act as hormones and enzymes
Collagen is the most abundant protein in the animals whereas RUBISCO
(Ribulose bisphosphate Carboxylase – Oxygenase) is the most abundant protein
universally.
Structures of proteins-
1. Primary structure is the linear chain of amino acids.
2. Secondary structure is the helical folded structure.
3. Tertiary structure is the three-dimensional view of protein.
4. Quaternary structure is the assembly of more than one polypeptide.
2. Polysaccharides
Polysaccharides are long chains of sugars (monosaccharides).
In a polysaccharide, the individual monosaccharides are joined by glycosidic
bonds.
Structure of glycosidic bond is
Cellulose is a polysaccharide consisting of only one type of monosaccharide –
glucose. Therefore, cellulose is a homopolymer or simple polysaccharides.
Similarly, insulin is a polymer of fructose.
Complex polysaccharides have building blocks, amino sugars, and chemically
modified sugars such as glucosamine, N-acetyl galactosamines, etc. Hence, they
are heteropolymers.
Chitin is an example of complex polysaccharide. It forms the exoskeleton of
arthropods and cell wall of fungi.
3. Nucleic acids
Nucleic acids are polynucleotides.
A nucleic acid containing deoxyribose sugar is DNA and that with ribose sugar is
RNA.
Bond formed between phosphate and hydroxyl group of sugar is known as
phospho-diester bond.
Metabolism
All chemical reactions occurring in a living organism are together known as
metabolism.
Biosynthetic pathways where simple structures form complex structures are known
as anabolic pathways.
Degradation pathways where complex structures break to form simple structures
are known as catabolic pathways.
Energy is liberated in the form of ATP (Adenosine triphosphate).
The rate of metabolic conversions (anabolism or catabolism) is affected by catalysts
called enzymes.
Enzymes
Enzymes are complex macromolecules with high molecular weight.
Almost all enzymes are proteins. Those RNA which can catalyze their own
biochemical reactions are called ribozymes.
The site of an enzyme at which a substrate fits is called its active site.
These can catalyze reactions at a high rate.
Example:
Activation energy is the energy required to achieve the transition state.
Enzymes are divided into 6 classes based on the type of reaction they catalyze -
oxidoreductases, hydrolases, transferases, lyases, isomerases, and ligases.
Properties of enzymes
Enzymes do not start a reaction, but help in accelerating it.
Enzymes affect the rate, but not the direction of a biochemical reaction.
Most of the enzymes have high turnover number. Turnover number of an
enzyme is the number of molecules of a substance that is acted upon by an enzyme
per minute. High turnover number of enzymes increases the efficiency of reaction.
Enzymes are specific in action.
Enzymatic activity decreases with increase in temperature.
The temperature and pH at which an enzyme shows the maximum activity is called
the optimum temperature and optimum pH respectively.
The activity of an enzyme declines both above and below the optimum value.
Enzymes show maximum activity at an optimum pH of 6 – 8.
The velocity of enzyme increases with increase in substrate concentration and then
ultimately reaches a maximum velocity.
A chemical that shuts the enzyme activity is called inhibitor.
When an inhibitor binds to the active site and competes with the substrate for
binding, it is called competitive inhibitor.
Nature of an enzyme action
The enzyme (E) first unites with the substrate (S) and forms an intermediate enzyme
substrate complex (ES).
Then it returns to its original form with an intermediate formation of enzyme
product complex (EP) after the reaction is concluded.
E+S ES EP E + P
Cofactors
The protein part of an enzyme is called apoenzyme.
Cofactors are non-protein constituents bound to the enzyme. These make the
enzyme catalytically active.
Cofactors can be classified in three categories.
Prosthetic groups – These are organic compounds which tightly bind to the
apoenzyme. Example: haem
Coenzymes – These are organic molecules which unite with the apoenzyme only
during the course of reaction. Example: NAD
Metal ions – Example: Zn acts as cofactor for carboxypeptidase.
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