All the c copounds tht v gt frm lving tisu can b clled biomolecules.

living organims hv also got

inorganic elements and compounds in thm.
How do we know this? A slightly different but destructive experiment has to be done. One weighs a
small amount of living tissue(say leaf or liver and this is called wet wieght) and dry it. All the water
evaporates. Now if the tissue is fully burnt all the carbon compunds are oxidised to gaseous form
(co2,water vapour) and are removed. What is remaining is called ash. This ash contains inorganic
elements (like calcium, magnesium etc.). Inorganic compunds like sulphate, phosphate etc. Are also
seen in the acid soluble fraction.therefore elemental analysis gives elemental composition of living
beings in the form of hydrogen oxygen chlorine carbon etc.while analysis of compounds give idea
of organic and inorganic constituents present in living tissues.from chem. Point of view one can
identify functional groups like aldehydes ketone aromatic compounds . But from a biological view,
they can be classified into amino acids, nucleotide bases, fatty acids etc.

H
C
O earth<body(%)
N
S
---------
Na
Ca earth>body(%)
Mg
Si

O Si Ca Na Mg H C N – earth in decreasing order

O C N Ca H S Na Si – body in decreasing order

Amino Acid- acidic – glutamic acid

basic- lysine
neutral- valine
aromatic- tyrosine, phenylalanine, tryptophan

Lipid- water insoluble

palmitic acid- 16 carbon

arachidonic acid – 20 carbon
glycerol- trihydoxy propane
glycerides= glycerol + fatty acid
Oils have lower melting point
lecithin- present in cell membrane
– example of phospholipid
– neural tissues

DNA components-
(adenine, guanine, cytosine, uracil, thymine)nitrogen bases + sugar = nucleosides
(adenosine, guanosine, thymidine, uridine, cytodine)nucleosides + phosphate group + nucleotides
nucleotides -> nucleic acid (adenylic acid, thymidylic acid, guanylic acid, uridylic acid, cytodylic
acid)
secondary metabolites- alkaloids, flavonoids, rubber, essential oils, antibiotics, coloured pigments,
scents, gums, spices 9
useful secondary metabolites to humans- rubber, drugs, spices, scents and pigments 5
Pigments- carotenoids, anthocyanin etc.
Alkaloids- morphine, codeine
Terpenoids- monoterpenes, diterpenes etc.
Essential oils- lemon grass oil
Toxins- abrin, ricin
Lectins- concavalin A
Drugs- Vinblastin, Curcumin
Polymeric Substances- Rubber, gums, cellulose
BIOMACROMOLECULES-
Acid Soluble pool - 18 to around 800 Daltons
Acid Insoluble- only 4 types of organic compounds- proteins, polysachharides, lipids, nucleic
acids.
True Macromolecular fraction- Polypeptides, Polysaccharides, Nucleic acids
These classes of compounds with the excption of lipids have molecular weights in the range of
10,000 Da and above for this very reason biomolecules that is chemical compounds found in living
organism are of two type . One those which have molecular weight less than 1000 Da and are
usually referred to as micromolecules or simply biomolecules
while those whcih are acid insoluble fraction are called biomacromolecules.
The molecules in the insoluble fraction with the exception of lipids are polymeric subtances
whose molecular weights do not exceed 800 Da, come under acid insoluble fraction that is
macromolecular fraction. Lipids are indeed small Mw compounds and are present not only as such
but also arrange into structures like cell membranes and other membranes. When we grind a tissue
we are disrupting its structure. Cell mebrane and other membrane are broken into pieces, and form
vesicles which are not water insoluble. Therefore these membrane fragments in the form of vesciles
get separated along with the acid insoluble pool and hence in the macromolecular fraction. Lipids
are not strictly macromolecules.

The acid soluble- cytoplasmic composition

macromolecules from cytoplasm and organelles- acid insoluble
together they represent entire chemical composition of living tissues or organisms

W 70-90
P 10-15
N 5-7
C3
L2
I1
Water is the most abundant chemical in living organisms

PROTEINS
– polypeptides- linear chains of amino acids linked by peptide bonds.
– essential amino acids are obtained through diet only
– non ess. a.a are made by the body
– Functions – transport nutrients across cell membrane
– fight infectious organisms (antibodies)
– some are hormones (Insulin),
– some are enzymes( Trypsin)
– Collagen – Most abundant protein in animal world, Intercellular ground substance
– Ribulose bisphosphate Carboxylase-Oxygenase (RuBisCO) is most abundant
protein in the whole of the biosphere.
– Receptor- Sensory reception( smell, taste, hormone, etc.)
– GLUT-4 – Enables glucose transport into cells
– In a polypeptide or a protein, amino acids are linked by a peptide bond which is formed
when the carboxyl (-COOH) group of one amino acid reacts with the amino (-NH2)
group of the next amino acid with the elimination of a water moiety (the process of bond
formation is called dehydration).

POLYSACCHARIDES
 – Long chains of sugar with branches
– The right end is called the reducing end and left end is called non-reducing end
– Cellulose – homopolymer of glucose, Starch and glycogen are variants of cellulose
– Plant cell walls, Paper made from plant pulp, Cotton fibre
– Starch – storehouse of energy in plant tissues
– Starch forms helical secondary structures. Starch can hold I₂ molecules
whereas cellulose cannot (due to lack of complex helices)
– Starch-I₂ – blue colour
– Glycogen-I₂ – red colour
– Glycogen- storehouse of energy in animal tissues
– Inulin – Polymer of Fructose
– More complex polysaccharides have amino-sugars and chemically modified sugars (e.g.
Glucosamine, N-acetyl galactosamine). These complex polysachharides are mostly
homopolymers
– Exoskeleton of arthropods have a complex polysaccharide called chitin.
– In a polysaccharide the individual monosaccharides are linked by a glycosidic bond.
This bond is also formed by dehydration. This bond is formed between two carbon
atoms of two adjacent monosaccharides.
NUCLEIC ACIDS
– Polynucleotides
– building block is a nucleotide
– 1.heterocyclic compound
– Substituted purines - Adenine and Guanine
– Substituted pyrimidines- Uracil, Thymine, Cytosine
– 2.monosaccharide – Ribose(in RNA) or 2' Deoxyribose(in DNA)
– 3. phosphoric acid or phosphate
– In a nucleic acid a phosphate moiety links the 3’-carbon of one sugar of one nucleotide
to the 5’-carbon of the sugar of the succeeding nucleotide. The bond between the
phosphate and hydroxyl group of sugar is an ester bond. As there is one such ester bond on
either side, it is called phosphodiester bond
– Nucleic acids exhibit a wide variety of secondary structures. One of the secondary structures
exhibited by DNA is the famous Watson-Crick model. This model says that DNA exists as
a double helix. The two strands of polynucleotides are antiparallel. The backbone is
formed by the sugar-phosphate-sugar chain. A and G of one strand compulsorily base
pairs with T and C, respectively, on the other strand. There are two hydrogen bonds
between A and T and three hydrogen bonds between G and C. Each strand appears like a
helical staircase. Each step of ascent is represented by a pair of bases. At each step of
ascent, the strand turns 36°. One full turn of the helical strand would involve ten steps
or ten base pairs. The pitch would be 34Å. The rise per base pair would be 3.4Å. This
form of DNA with the above mentioned salient features is called B-DNA.

STRUCTURE OF PROTEINS
 – In inorganic chemistry, the structure invariably refers to the molecular formulae (e.g.,
NaCl, MgCl2 , etc.). Organic chemists always write a two dimensional view of the
molecules while representing the structure of the molecules (e.g., benzene, naphthalene,
etc.). Physicists conjure up the three dimensional views of molecular structures while
biologists describe the protein structure at four levels.
– The sequence of amino acids is called the primary structure.
– Left end represented by first a.a – called N-terminal a.a
– Right end represented by last a.a – called C-terminal a.a
– A protein thread does not exist throughout as an extended rigid rod. The thread is folded
in the form of a helix (similar to a revolving staircase). Of course, only some portions
of the protein thread are arranged in the form of a helix. In proteins, only right handed
helices are observed. Other regions of the protein thread are folded into other forms in
what is called the secondary structure
– In addition, the long protein chain is also folded upon itself like a hollow woolen ball,
giving rise to the tertiary structure. This gives us a 3-dimensional view of a protein.
Tertiary structure is absolutely necessary for the many biological activities of
proteins.
– Some proteins are an assembly of more than one polypeptide or subunits. The manner
in which these individual folded polypeptides or subunits are arranged with respect to
each other (e.g. linear string of spheres, spheres arranged one upon each other in the
form of a cube or plate etc.) is the architecture of a protein otherwise called the
quaternary structure of a protein. Adult human haemoglobin consists of 4 subunits.
Two of these are identical to each other. Hence, two subunits of α type and two
subunits of β type together constitute the human haemoglobin (Hb).

ENZYMES
– Almost all enzymes are proteins. There are some nucleic acids that behave like
enzymes. These are called ribozymes. An enzyme like any protein has a primary structure,
secondary and the tertiary structure. When you look at a tertiary structure you will notice
that the backbone of the protein chain folds upon itself, the chain criss-crosses itself and
hence, many crevices or pockets are made. One such pocket is the ‘active site’. An active
site of an enzyme is a crevice or pocket into which the substrate fits. Thus enzymes, through
their active site, catalyse reactions at a high rate.
– Enzyme catalysts differ from inorganic catalysts in many ways, but one major difference
needs mention. Inorganic catalysts work efficiently at high temperatures and high
 pressures, while enzymes get damaged at high temperatures (say above 40°C).
However, enzymes isolated from organisms who normally live under extremely high
temperatures (e.g., hot vents and sulphur springs), are stable and retain their catalytic power
even at high temperatures (upto 80°-90°C). Thermal stability is thus an important quality
of such enzymes isolated from thermophilic organisms.

– NOT MUCH IMPORTANT read 9.8.1, 9.8.2.(new ncert) 9.9,9.10(old ncert)

– read graph of activation energy
– blood conc.of glucose in a normal healthy individual is 4.5- 5.0 mM
– Each enzyme (E) has a substrate (S) binding site in its molecule so that a highly reactive
enzyme-substrate complex (ES) is produced. This complex is short-lived and dissociates
into its product(s) P and the unchanged enzyme with an intermediate formation of the
enzyme-product complex (EP). The formation of the ES complex is essential for catalysis.
E + S → ES → EP → E + P
– Steps: 1. First, the substrate binds to the active site of the enzyme, fitting into the active
site. 2. The binding of the substrate induces the enzyme to alter its shape, fitting more
tightly around the substrate. 3. The active site of the enzyme, now in close proximity of the
substrate breaks the chemical bonds of the substrate and the new enzyme- product
complex is formed. 4. The enzyme releases the products of the reaction and the free
enzyme is ready to bind to another molecule of the substrate and run through the catalytic
cycle once again.

FACTORS AFFECTING ENZYME ACTIVITY

– The activity of an enzyme can be affected by a change in the conditions which can alter the
tertiary structure of the protein. These include temperature, pH, change in substrate
concentration or binding of specific chemicals that regulate its activity. Temperature and
pH - Enzymes generally function in a narrow range of temperature and pH . Each enzyme
shows its highest activity at a particular temperature and pH called the optimum
temperature and optimum pH. Activity declines both below and above the optimum
value. Low temperature preserves the enzyme in a temporarily inactive state whereas
high temperature destroys enzymatic activity because proteins are denatured by heat.
Concentration of Substrate- With the increase in substrate concentration, the velocity of
the enzymatic reaction rises at first. The reaction ultimately reaches a maximum
velocity (Vmax) which is not exceeded by any further rise in concentration of the
substrate. This is because the enzyme molecules are fewer than the substrate molecules
and after saturation of these molecules, there are no free enzyme molecules to bind
with the additional substrate molecules.

– The activity of an enzyme is also sensitive to the presence of specific chemicals that
bind to the enzyme. When the binding of the chemical shuts off enzyme activity, the
process is called inhibition and the chemical is called an inhibitor.
 – When the inhibitor closely resembles the substrate in its molecular structure and inhibits
the activity of the enzyme, it is known as competitive inhibitor. Due to inhibitor's
close structural similarity with the substrate, the inhibitor competes with the substrate
for the substrate binding site of the enzyme. Consequently, the substrate cannot bind and
as a result, the enzyme action declines, e.g., inhibition of succinic dehydrogenase by
malonate which closely resembles the substrate succinate in structure. Such
competitive inhibitors are often used in the control of bacterial pathogens.

Classification and Nomenclature of Enzymes

Thousands of enzymes have been discovered, isolated and studied. Most of these enzymes have
been classified into different groups based on the type of reactions they catalyse. Enzymes are
divided into 6 classes each with 4-13 subclasses and named accordingly by a four-digit number.

Very Very Important-

Oxidoreductases/dehydrogenases: Enzymes which catalyse oxidoreduction between two
substrates S and S’ e.g., S reduced + S’ oxidised → S oxidised + S’ reduced.
Transferases: Enzymes catalysing a transfer of a group, G (other than hydrogen) between a pair of
substrate S and S’ e.g., S - G + S’  → S + S’ - G
Hydrolases: Enzymes catalysing hydrolysis of ester, ether, peptide, glycosidic, C-C, C-halide or P-
N bonds.
Lyases: Enzymes that catalyse removal of groups from substrates by mechanisms other than
hydrolysis leaving double bonds.
Isomerases: Includes all enzymes catalysing inter-conversion of optical, geometric or positional
isomers.
Ligases: Enzymes catalysing the linking together of 2 compounds, e.g., enzymes which catalyse
joining of C-O, C-S, C-N, P-O etc. Bonds.

Co-Factors
– non-protein constituents called cofactors are bound to the the enzyme to make the enzyme
catalytically active. In these instances, the protein portion of the enzymes is called the
apoenzyme.
– Three kinds of cofactors may be identified: prosthetic groups, co-enzymes and metal ions.
– Prosthetic groups are organic compounds and are distinguished from other cofactors in
that they are tightly bound to the apoenzyme. For example, in peroxidase and
catalase, which catalyze the breakdown of hydrogen peroxide to water and oxygen,
haem is the prosthetic group and it is a part of the active site of the enzyme.
– Co-enzymes are also organic compounds but their association with the apoenzyme is
only transient, usually occurring during the course of catalysis. Furthermore, co-
enzymes serve as co-factors in a number of different enzyme catalyzed reactions. The
essential chemical components of many coenzymes are vitamins, e.g., coenzyme
nicotinamide adenine dinucleotide (NAD) and NADP contain the vitamin niacin.
– A number of enzymes require metal ions for their activity which form coordination
bonds with side chains at the active site and at the same time form one or more
cordination bonds with the substrate, e.g., zinc is a cofactor for the proteolytic
enzyme carboxypeptidase.
– Catalytic activity is lost when the co-factor is removed from the enzyme which
testifies that they play a crucial role in the catalytic activity of the enzyme.