Biomolecules Theory (PDF - Ai)

Chapter 2
Biomolecules
e How to Analyse Chemical All living organisms are made up of the same chemicals i.e., elements
Composition? and compounds. If we analyse a plant tissue, animal lissue or a microbial
* Primary and Secondary paste, we obtain elements like carbon, hydrogen, oxygen etc.
Metabolites
» Carbohydrates T N L CONT e
* Amino Acids . While performing a chemical analysis, when a living tissue is grinded
o e in trichloroacetic acid (C1,CCOOH), a thick slurry is formed. This slurry
o Lipids when strained through cheese cloth or cotion gives two fractions, one
is the filtrate which is called acid-soluble pool where thousands of
Dl organic compounds are found. The other fraction is called the retentate
* Dynamic State of Body or the acid-insoluble pool where compounds like proteins, nucleic
Constituents - Concept of .
Metabolism acids, polysaccharides etc. are found.
The Living State . All the carbon compounds that we get from living tissues can be called
o Engymes ‘biomolecules’
. However, inorganic elements and compounds are also presentin the living
organisms, which can be identified with the help of a technique called
‘ash’ analysis. A small amount of a living tissue (say a leaf or liver) is
weighed (wet weight) and dried. All the water evaporates. The remaining
material gives dry weight
. When this tissue is fully burnt, the carbon compounds are oxidised to
gaseous forms like COQ ‘and water vapour that are lost and the remnant
is called ‘ash’. This ash contains many inorganic elements like calcium,
magnesium etc
. In the acid-soluble fraction, inorganic compounds like sulphate,
phosphate etc. are also present.
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32 Biomolecules NEET
The most abundant element in celllliving matter is oxygen.

Table : A comparison of elements present in non-living and living matter®
Hydrogen (H) 014 05

Carbon (C) 0.03 185
Oxygen (O) 46.6 65.0
Nitrogen (N) Very little 33
Sulphur (S) 0.03 03
Sodium (Na) 28 0.2
Calcium (Ca) 386 15
Magnesium (Mg) 21 0.1
Silicon (Si) 27.7 Negligible
* Adapled from CNR Rao, Understanding Chemistry,
Universities
Press, Hyderabad.
Fe** and Cu** are found in cylochromes.
The concentration of the cations inside the cell is K> Na > Ca.
Table : A list of inorganic constituents of living tissues
Sodium Na’
Potassium K
Calcium Ca™
Magnesium Mg™
Water H.0
Compounds NaCl, CaCO,,
PO}, SO}
. From a biological point of viewwe can classify the biomolecules into micromolecules and macromolecules.
. Biomolecules
Micromolecules Macromolecules
(acid soluble fraction) (acid inscluble fraction)
T, A
Amino acids Simple sugars Nucleotides
Polysaccharides %im Nucleic acid

. The acid soluble pool contain chemicals with small molecular mass of 18 - 800 daltons approximately.
They are called micromolecules or biomicromolecules. They include amino acids, sugar, nucleotides etc.
while those which are found in the acid insoluble fraction are called macromolecules or biomacromolecules.
. Lipids are not strictly macromolecules. Their molecular weight does not exceed 800 Da, but they are obtained
in the acid insoluble fraction because when we grind a tissue, cell membrane and other membranes are broken
into pieces and form vesicles which are not water soluble (lipids are also present in structures like cell
membrane and other membranes). Therefore, these membrane fragments in the form of vesicles
get separated
along with the acid insoluble pool.
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NEET Biomolecules 33
+ The acid-soluble fraction represents roughly the cytoplasmic composition (without organelles), while the acid-
insoluble fraction represents the macromolecules of the cytoplasm and cell organelles. The two fractions
together represent the entire chemical composition of living tissues or organisms.
Table : Average composition of cells

% of the total
cellular mass
Water 70-90
Proteins 10-15
Carbohydrates 3
Lipids 2
Nucleic acids 57
lons 1
Note: Water is the mast abundant chemical in living organisms.
PRIMARY AND SECONDARY METABOLITES

. Living organisms produce thousands of organic compounds (biomolecules) including amino acids, sugars,
chlorophyll, haem etc. These are required for their basic or primary metabolic processes like photosynthesis,
respiration, protein and lipid metabolism etc. These organic compounds are called primary metabolites.
Primary metabolites have identifiable functions and play known roles in normal physiological processes.
. Many plants, fungi and microbes of certain genera and families synthesize a number of organic compounds
(biomolecules) which are not involved in primary metabolism and seem to have no direct function in growth
and development of organisms. Such compounds are called secondary metabolites.
. The functions or role of secondary metabolites in host organisms are not understood. However, many of them
are useful to human welfare (e.g., rubber, drugs, spices, scents and pigments).
. Some secondary metabolites have ecological importance.
Table : Some secondary metabolites

Pigments Carotenoids, Anthocyanins, etc.
Alkaloids Morphine, Codeine, etc.
Terpenoides Monoterpenes, Diterpenes etc.
Esseniial oils Lemon grass oil, etc.
Toxins Abrin, Ricin
Lectins Concanavalin A
Drugs Vinblastin, Curcumin, efc.
Polymeric substances | Rubber, Gums, Cellulose
CARBOHYDRATES
Carbohydrates are mainly compounds of carbon, hydrogen and oxygen. These are also known as saccharides
because their basic components are sugars. They are of two types: small and large (complex). Small
carbohydrates (biomicromolecules) are further divided into monosaccharides, derived monosaccharides and
oligosaccharides. Large carbohydrates (biomacromolecules) are called polysaccharides.
1. Monosaccharides : They are those sugars or simple carbohydrates which cannot be hydrolysed further into
smaller components. These are composed of 3-7 carbon atoms and are biomicromolecules.
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Example - Ribose, glucose, fructose efc.

. H I—C =0
H—C—OH H—C=0
] CH,OH I
HO — CI —H H—C—OH
HOCH,
H— ‘i— OH Hot—on
H—C—OH HON, on H= é, OH o
s
H— . OH H )
y—Cc—OoH OH OH
Open chain of Glucose C.H,0, (Glucose) ‘Open chain of Ribose C.H,0, (Ribose)
s Glucose, fructose, mannose, galactose are hexoses. These are white, sweet-tasting, crystalline and
exiremely, soluble in waler.
« Glucose is the universal sugar. It is also known as dextrose or grape sugar or corn sugar.
# Fructoseis called fruit sugar. It is also knownas levulose. It is the sweetest
among naturally occurring
sugars.
® Monosaccharides have ‘free’ aldehyde or ketone group which can reduce Cu™ to Cu®. Hence, these are
also called reducing sugars.
2. Derived monosaccharides : Monosaccharides are modified variously to form a number of different substances.
* Deoxy sugar : e.g. Deoxygenation (removal of oxygen at 2'¢ carbon) of ribose produces deoxyribose,
a constituent of DNA.
) <) 0,
5 5
H,COH Deorygenaton
H,COH
d 1 Decwetn d b
H\H H¥H H\H H/H
3 3 2
OH OH HO H
Ribose (C.) Deoxyribose (C.)
= Amino sugar : e.g. glucosamine
e Sugar acid : e.g. glucuronic acid, ascorbic acid
« Sugar alcohol : e.g. mannitol (present in brown algae)

3. Oligosaccharides : They are small carbohydrates which are formed by condensation of 2-9 monosaccharides.
The monosaccharide
units are joined together
by glycosidic bond, formed
by dehydration. It is nommally formed
between carbon atoms 1 and 4 of neighbouring unit (1, 4 bond). Depending upon the number of
monosaccharide molecules condensed to form oligosaccharides, they can be disaccharides (e.g., sucrose,
maltose, lactose, trehalose (present in haemolymph of insects), trisaccharides (e.g., raffinose - made up of
glucose, fructose and galactose), tetrasaccharides (e.g., stachyose) etc.
CH,OH CH,OH
0 H H Q
H/H H H
d b 0 d b
OHN oHB H
2}/
aid
Giycosidic bond
OHo 2
H/OH
M Gucoss Maltose " Glucoss H
‘ SfHOH .iu,on H,OH

Hi 3c—0, C—0, —q, HOGH H,
;{a RN SO H
T S H
NS i/fl
H
AVS ,i{n
H
; bH [, H "/ouon
H
H H H H Z H
PGALACTOSE gwvepomry F-GLUCOSE 1+ GLUCOSE PFRUCTOSE
Fig. : Structural formulae of common disaccharides
s Reducing sugars : They are those sugars which can reduce Cu®* ions to Cu* ions. This property is the
basis of Benedict's and Fehling's
test to detect
the presence of glucosein urine. The property is found in all
those saccharides which possess free aldehyde or ketone groups. All monosaccharides have this ability.
« Amongst disaccharides, sucrose (glucose + fructose) is non-reducing because both aldehyde group of
glucose and ketone group
of fructose participate in formationof glycosidic bond between the two. However,
some other disaccharides like, lactose, maltose possess reducing groups.
4. Polysaccharides : These are polymers or chains of monosaccharides and are macromolecules. They are
threads containing different monosaccharides as building blocks and are branched or unbranched. The right
end of a polysaccharide is the reducing end while the left end is the non-reducing end. Depending upon the
composition, polysaccharides are of two types. homopolysaccharides and heteropolysaccharides.
(i) Homopolysaccharides : They consist of only one type of monosaccharide monomer. Starch and
glycogen both are polymers of glucose and serve as a storage form in plants and animals respectively.
(a) Glycogen: Glycogen is made up of about 30,000 glucose residues. It is a branched structure having
(ct1,4) linkage at unbranched part and the branching points have (a1, 6) linkage. It gives red colour
with iodine. It is stored as reserve food in liver and muscles in man.
o
% \
- 0,
\% 1 OH H
o 0 OH
o. OH OH
CH,
Fig. : Diagrammatic representation of a portion of glycogen
(b) Starch is a polymer of glucose. It is the major reserve food in plants. It forms helical
secondary structure ie., the chain of glucose molecules folds in the form of a helix. Starch gives
a characteristic blue colour with iodine (I;) molecules due to the ability of the latter to occupy a
position in the interior of a helical coil of glucose units.
Starch has two components that includes amylose (an unbranched polymer) and amylopectin
(a branched polymer).
Amylopectin : Consists of 2000 - 200,000 glucose molecules forming straight chain and branches
(after
25 glucose units). Branching point has a, 1-6 glycosidic linkage.
Amylose : Consists of &, 1-4 glycosidic linkage between oD glucose molecules. It is a straight chain
of 200 - 1000 glucose units. It is helical and each tum consists of 6 glucose units.
(c) Inulin is a polymer of fructose. It is a storage polysaccharide found in roots and tubers of Dahlia
and related plants. Inulin is not metabolised in human body and is readily filtered through the kidney.
It is therefore used in testing of kidney function.
(d) Chitin : It is the second most abundant organic substance. In chitin, the basic unit is a nitrogen
containing glucose derivative known as N-acetyl glucosamine. The exoskeletons of arthropods have chitin,
(e) Cellulose (Hexosan polysaccharide) : Cellulose is an unbranched homopolysaccharide of f-glucose

with ({1, 4) linkages between glucose molecules. One molecule of cellulose has about 6000 -glucose
residues. Cotton fibres contain the largest amount (90 percent) of cellulose among natural materials.
It is produced by plants and is used for building cell walls. It is the most abundant organic
compound in the biosphere. Wood and cotion contain large quantities of cellulose. Paper made from
plant pulp is cellulose. Cellulose does not contain complex helices and hence cannot hold I,.
(ii) Heteropolysaccharides : Heteropolysaccharides consist of more than one type of monosaccharide
monomers i.e., they are heteropolymers and are more complex polysaccharides. Some of the
heteropolysaccharides are :
(a) Peptidoglycan : In peptidoglycans the heteropolysaccharide chains are made up of two alternate
amino-sugar molecules i.e., N-acetyl glucosamine and N-acetyl muramic acid. Peptidoglycan is
present in bacterial cell wall which is degraded by the enzyme lysozyme, which hydrolyses the
glycosidic bond, killing bacterial cells.
(b) Hyalurenic acid : It is a heteropolymer composed of D-glucuronic acid (a carboxylic acid) and
D-N-acetyl glucosamine (a monosaccharide derivative of glucose). Hyaluronic acid accounts for the
toughness and flexibility of cartilage and tendon.
(c) Agar is a type of mucopolysaccharide and is obtained from red algae. It is used as culture
medium in laboratory.
Note:
e Carbohydrates like glycogen and starch (polysaccharide) are relatively easy to store because
of the
following advantages :
(i) They are stored in bulk.
(i) They are chemically nonreactive.
(ii) They are osmotically inactive.
e When necessary
these polysaccharides are broken down by enzymes for the release of energy.
1. Glucose is
(1) Cane sugar (2) Grape sugar
(3) Malt sugar (4) Triose sugar
2. Pentoses and hexoses are common
(1) Oligosaccharides (2) Disaccharides
(3) Monosaccharides (4) Polysaccharides
3 Which of the following is present in acid insoluble fraction?
(1) Glucose (2) Fructose
(3) Alanine (4) Lipids
4. Secondary metabolite that is a polymeric substance
(1) Ricin (2) Monoterpenes
(3) Curcumin (4) Rubber
5. Choose a secondary metabolite that is a drug as well
(1) Concanavalin A (2) Vinblastine
(3) Diterpenes (4) Ricin
6. Inulin is a polymer of
(1) Fructose (2) Glucose
(3) Mannose 4) Ribose
7. Structural polysaccharide among following is
(1) Glycogen (2) Starch
@ Inuin @) Cellulose
8 Select the mismatch
(1) Chitin - Polymer of glucosamine
(2) Glycogen - Polymer of glucose
(3) Cellulose - Heteropolysaccharide
@) Inulin = Homopolysaccharide
9. Unbranched polymer
of glucose is
(1) Starch (2) Glycogen
@) Celulose @) Chitin
10. The most abundant carbohydrate in biosphere is
(1) Starch 2) Glycogen
(3) Cellulose (4) Hemicellulose
AMINO ACIDS
« Amino acids are organic compounds, having amino group (-NH,) and carboxylic group (~COOH) attached to
the same carbon ie., the a-carbon (a-carbon is the carbon to which functional groups are attached). The
a-carbon
also bears hydrogen and a variable
‘R’ group.
. They are substituted methanes as there are four substituent groups occupying the four valency positions
of carbon. Since both the functional groups are attached to the a-carbon so they are called a-amino acids.
. Based on the nature of ‘R’ groups there are many amino acids.
* Amino acids which occur in proteins in man are of twenty types. The ‘R’ group in these proteinaceous amino
acids could be a hydrogen (glycine), a methyl group (alanine), hydroxy methyl (serine), efc.
. Humans are incapable of synthesizing nearly half of the 20 standard amino acids and these are known as
essential amino acids. They must be obtained from food. e.g., Lysine, methionine, phenylalanine, tryptophan,
wvaline, isoleucine, leucine, threonine.
. ‘Semi essential amino acids : They can be synthesised very slowly by a human beings. e.g., Arginine and
histidine.
. The amino acids that are synthesized in our body are called non-essential amino acids to denote the fact
that they are not needed in diet.
e.g., Alanine, cysteine, glutamate, glycine, proline etc.
) fi;oou O0H FOoH
H—?—NH, H—(IL—NHI H—‘C’NH;
[
Glycine Alanine Serine
. Physical and chemical properties of amino acids are mainly due to the amino, carboxyl and ‘R’ functional groups.
Based on comparative number of amino and carboxyl groups, amino acids can be acidic, basic and neutral.
() Acidic amino acids : The amino acids have an exira carboxylic group.
Example - Glutamic acid (glutamate), aspartic acid (aspartate).
HN-C-H
J:H,—COOH
Aspartic acid
(i) Basic amino acids : They have an additional amino group.
Example - Lysine, arginine etc.
. CI:OOH
H;Hl‘rH
(fH:h
H,C-NH,
Lysine
(iii) Neutral amino acids : Amino acids have one amino group and one carboxylic group.
Example - Valine, alanine, glycine, leucine, isoleucine.
(iv) Sulphur containing amino acid : Have sulphur.
Example - Cysteine, methionine.
(v) Alcoholic amino acid : Have ~OH group.
Example - Serine, threonine
(vi) Heterocyclic amino acid : ‘N’ is present in ring.
Example - Proline, histidine, hydroxyproline.
(vii) Aromatic amino acids possess cydic structure with a straight side chain bearing carboxylic and amino
group.
Example - Tyrosine, phenylalanine, tryptophan.
@—CH,—CHNHFCOOH
Phenylalanine
. A particular property of amino acids is the ionizable nature of NH, and COOH groups. At isoelectric point,
an amino acid exists as a dipolar ion, called a Zwitterion.
A zwitterion is compound that has a negative charge
‘on one atom and a positive charge on a non-adjacent atom. Hence, in solutions of different pHs, the structure
of amino acid changes.
[lHN-CH-COOH ==
T
HN-CH-COO ==
T
HN-CH-COO"
(A (B) (C)
. Two amino acids can join through amino group of one and carboxylic group of the other forming a peptide
bond by loss of a water molecule. When a few amino acids are joined in this fashion, the structure is called
an oligopeptide. When many amino acids are joined, the product is called a polypeptide.
GO
[=]
NH e g
OH
——
Peptide bond
PROTEINS
. Proteins are large-sized macromolecules having one or more polypeptides (chains or polymers of amino
acids linked by peptide bond).
. As there are 20 types of amino acids, a protein is a heteropolymer and not a homopolymer.
A homopolymer has only one type of monomer repeating ‘n’ number of times.
+ Collagen is the most abundant protein in animal world. It is the main component of connective tissue of
animals.
. Ribulose bisphosphate carboxylase-oxygenase (RuBisCO) is the most abundant protein in the whole of
the biosphere.
Structure of Proteins
Biologists describe the protein structure at four levels - primary, secondary, tertiary and quatemary.
(a) Primary structure
The sequence in which amino acids are arranged in a polypeptide chain of a protein is called its primary
structure. It gives the positional information of amino acids in a protein ie., which is the first amino acid,
which is the second, and so on.
(=) Primary
Polypeptide
{b) Secondary / \
5 oy
o
Alpha- Helox Beta—pieated shest
(c) Tartiary
Disuifide bond
R \@
Fig. : Structure of a protein
« In this, chains of amino acids which constitute a protein, the amino acid present at the left end is
the first amino acid, whereas the one at the right end is the last amino acid of the protein. The first
amino acid is known as N-terminal amino acid and the last is known as C-terminal amino acid.
(b) Secondary structure
* Some portion of the protein thread are folded either in the form of a helix (similar to a revolving
staircase) or i-pleated sheet. The u-helix and (-pleated sheet are two types of secondary structures.
In o-helix, there is interaction between every fourth amino acid by the formation of intramolecular
hydrogen bond. The polypeptide gets a helical shape (u-helix). The intramolecular hydrogen bond
is a bond formed between the hydrogen
atom and the highly electronegative
atom such as nitrogen,
oxygen and fluorine of the same molecule.
= In proteins, only right-handed helices are observed.
Example - Keratin protein present in hair.
Fig. : Cartoon showing : Secondary structure (a-helix) of protein

* When two or more polypeptide chains are held together by intermolecular hydrogen bonds, the
structure is described as p-pleated sheet. The intermolecular hydrogen bond is the bond formed
between the hydrogen atom of the molecule and the highly electronegative atom (such as nitrogen,
oxygen, fluorine) of the other molecule.
Example - Fibroin protein of silk
Hydrogen bond
Polypeptides
Fig. : p-pleated
o Collagen helix : The polypeptide coil of collagen helix is strengthened by establishing hydrogen
bond and locking effect also occurs with the help of amino acids proline and hydroxyproline.
(c) Tertiary structure

e The long protein chain or the polypeptide chain usually folds upon itself like a hollow woollen ball.
This is termed as the tertiary structure. This structure gives a 3-dimensional view of a protein.
* Tertiary structure is absolutely necessary for the many biological activities of proteins for example,
this structure brings distant amino acid side chains closer forming the active site (the site fo which
a substrate gets attached) of proteins Le., enzymes.
Example - Myoglobin (protein found in muscle cells)
u [
Hydrogen | .o lonic
Bond Bond
l-D
Hydophtic,
¢ (@, Y CH.OH Van
e iaals
- i E:. | Covalent Interacton
',m,%} -] Bond
N S ' [
A B
Fig. : A. Various types of bonds formed during coiling of polypeptide,
B. Cartoon showing tertiary structure of protein
(d) Quaternary structure
Quaternary structure is formed when a protein has more than one subunits (individual polypeptide chains
of a quatemary protein are called subunits) or polypeptide chains and each polypeptide has a primary,
secondary or tertiary structure of its own. The way in which these individually folded polypeptides are
arranged with respect to each other gives the architecture of the quaternary structure of a protein.
For example, haemoglobin has such structure. Haemoglobin has four helical polypeptide chains, two
a-chains and two fi-chains.
Functions
Proteins perform many functions in living organisms, some of the functions are as follows :
1. Enzymes : Al enzymes (except a few) are built up of proteins alone or in conjugation with some non-protein
materials called cofactors.
Table : Some proteins and their functions
Collagen |Intercellular ground substance

Trypsin Enzyme
Insulin Hormone
Antibody |Fights infectious agents
Receptor |Sensory reception (smell,
taste, hormone, etc.)
GLUT-4 |Enables glucose transport into
cells
2. Defence proteins : Immunoglobulins or antibodies are proteins that fight infectious agents. They are
produced by a type of white blood cell called B-lymphocytes.
3. Hormone : Some hormones are proteinaceous in nature, for example insulin. It is secreted by the
f-cells present in the islets of Langerhans of pancreas. It regulates the sugar metabolism.
4. Receptor
: Receptors are protein molecules which bind to specific information
molecules like hormones.
5. Transport proteins : Protein like haemoglobin present in the RBC transports oxygen from lungs to various
part of the body.
6. Simple and Conjugated Protein: On the basis of structure, proteins are classified as simple or
conjugated. Simple Proteins are composed of amino acids only. For example, egg albumin, serum
globulins, glutelins of wheat or rice, keratin of skin and hair and collagen of connective tissues.
Conjugated Proteins are formed by the binding of a simple protein with a non-protein part called the
prosthetic Group.
The conjugated proteins are of following types:
(a) Nucleoproteins (prosthetic group—nucleic acid) e.g., Protamines
(b) Metalloproteins (prosthetic group-metals) e.g., Ferritin
(c) Chromoproteins (prosthetic group—pigment) e.g. Cytochromes
(d) Phosphoproteins (prosthetic group—phosphoric acid) e.g., Casein of milk.
(e) Lipoproteins (prosthetic group-lipids) e.g., Chylomicron.
() Glycoproteins (prosthetic group—carbohydrates) e.g., Mucin.
LIPIDS
Lipids are all made of carbon, hydrogen and little oxygen and are water insoluble. The lipids are not
polymers but they are assembled from smaller molecules by dehydration. Their general formula in C H,,0,.
Lipids could be simple fatty acids or glycerol. Many lipids have both glycerol and fatty acids. Some lipids
have phosphorus and a phosphorylated organic compound in them. Some lipids have more complex structures.
Classification
The lipids are classified into sub-groups as follows :
i Classification of Lipids
Lipids
Simple lipids Cqmpound or Dar_M;d

conjugated lipids lipids
Neutral or Waxes Cutin

true fats
Phospholipids ~ Glycolipids Lipoproteins ~ Chromolipids
A. Simple lipids : These are esters (organic acids and alcohols react to form esters) of fatty acids with
various alcohols. They are of two types :
() Neutral or true fats : These are esters of fatty acids with glycerol. They are also called glycerides.
A fat molecule consists of one molecule of glycerol and one to three molecules of the same or
different long-chain fatty acids.
(a) Glycerol : A glycerol molecule has 3 carbons, each bearing a hydroxyl (-OH) group. Hence
called trihydroxypropane.
CH,-OH
+MH
CH,-OH
Glycerol
(b) Afatty acid molecule is an unbranched chain
of carbon atoms having a carboxylic group attached
toan ‘R’ group(1 carbon to 19 carbons). For example, palmitic acid has 16 carbons including
carboxyl carbon. Arachidonic acid has 20 carbon atoms including the carboxyl atom.
Fatty acids are of two types :

1. Saturated fatty acids : Fatty acids without double bond.
Example - Palmitic acid, Stearic acid
CH,~CH,),,~COOH CH,~CH,),;~COOH
Palmitic acid Stearic acid
2. Unsaturated fatty acids : Fatty acids with one or more double bonds.
Example - Oleic acid, linoleic acid, linolenic acid, arachidonic acid
CH,(CH,), CH = CH (CH,), COOH
Oleic acid
CH,(CH,), CH = CH CH, CH = CH(CH,), COOH
Linoleic acid
« Neutral or true fats may be monoglyceride if there is only one molecule of fatty
acid attached to a glycerol molecule. If the number of fatty acids attached to a
glycerol happens to be two, it is called diglyceride, or triglyceride if the number of
fatty acids is three.
. im—on HOOC-R, E:,-o—oc—fl,
H-OH + HOOCR, — CH-O-OCR, +3H0O
éH,-OH HOOC-R, J:H-o-oc-n,
Glycerol Fatty acid Triglyceride
(1 molecule) (3 molecules) (1 molecule)
= Based on the melting point triglycerides can be called fats or oils. Fats have high
meilting point and remain as solids at room temperature. e.g., butter, ghee while
oils have low melting point and remain as liquids/oil at room temperature. e.g.,
gingelly oil. sunflower oil, etc.
() Waxes : These are esters of fatty acids with alcohol of high molecular weight instead of glycerol.
e.g., beeswax, lanolin etc. They have an important role o play in protection. They form water-
insoluble coating on hair and skin in animals and stems, leaves and fruits of plants.
Beeswax is formed from palmitic acid and myricyl alcohol and secreted by worker bees.
B. Compound or conjugated lipids : These are esters of fatty acids with alcohol, but contain some other
substances also. They are :
() Phospholipids : The phospholipids are composed of a molecule of glycerol or other alcohol having
(a) a phosphate group joined to one of its outer -OH groups, (i) two fatty acid molecules linked
to the other two ~OH groups, and (iii) a nitrogen-containing choline molecule, bound to the
phosphate group. Phospholipids are found in cell membranes. Lecithin is one example of
phospholipid.
: o -
Choline
Pol )
[¢] CH,-O-E-H, head group
! osphate
" of CH
CH,-o-P-O-CH,-CH,-fi-@H,
Y
Glygerol
b o
Non-polar tails
Phaospholipid (lecithin)
(i) Glycolipids : Glycolipids contain fatty acids, alcohol (sphingosine) and sugar can be galactose or
other. The sugar replaces one fatty acid molecule. These
are present in myelin sheath
of nerve fibres
and in the outer surface of cell membrane of chloroplast.
(iii) Lipoproteins : Lipoproteins contain lipids (mainly phospholipids) and proteins in their molecules.
Membranes are composed of lipoproteins.
(iv) Chromolipids : These contain pigments such as carotenoids e.g. Carotene, vitamin A
C. Derived lipids
Steroids : The steroids do not contain fatty acids, but are included in the lipids because they have fat-
like properties. The most common steroids are sterols. A common sterol is cholesterol.
= Cholesterol is the most abundant steroid in the animal tissues. Food rich in animal fats contain
cholesterol. It is also synthesised in the liver.
« Cholesterol is an essential component of animal plasma membrane
mfil
Cholesterol
» Prostaglandins : It is a group of hormone like unsaturated fatty acids which function as messenger
substance between cell. They are derived from arachidonic acid and related C,, fatty acid.
NUCLEIC ACIDS
Nucleic acids are polymers of nucleotides and are macromolecules. There are two types of nucleic acids
namely - deoxyribonucleic acid (DNA) or ribonucleic acid (RNA). Nucleotides serve as the building block of
nucleic acids. A nucleotide is composed of :
(i) A phosphate group :
N
H-0-P-O-H
£
0-P-0O
| |
OH o
Phospharic Acid Phosphate ion
(ii) A five-carbon sugar or pentose sugar (monosaccharide) : In RNA, the sugar is ribose (thus the
name ribonucleic acid) and in DNA the sugar is deoxyribose (thus deoxyribonucleic acid).
ZEaN AN
CHOHO, OH CH,0H.0, OH
KN of Kl
R
OH O] oH [H
[hribose f-decxyribose
(iii) A heterocyclic nitrogen-containing compound called base : There are four different bases commonly
found in DNA : adenine (A), guanine (G), thymine (T) and cytosine (C). RNA also contains adenine,
guanine and cytosine but instead of thymine it has uracil (U). Adenine and guanine are double-fing bases
called purines. Cytosine, thymine and uracil are single-ing bases called pyrimidines.
TONM, [+] NH, o
NF N HN' HN ra
@E N NH
N
.
T I N N
N
O
I T i
-
TH "
]
H H H H
Adenine Guanine Uracil Cytosine Thymine
s The nitrogenous base is joined to the sugar molecule by a glycosidic bond and forms a structure
called nucleoside. The nucleoside combines with a phosphate group by an ester bond to form a
nucleotide.
Nitrogenous | Nucleoside | Nucleotide

Base
1. Adenine |Adenosine |Adenylicacid
2. Guanine |Guanosine | Guanylicacid
3. Cytosine | Cytidine Cytidylic acid
4. Thymine | Thymidine | Thymidylic
acid
5. Uraal Uridine Uridylic acid
+ In anucleic acid, a phosphate moiety (moiety is a part of a larger molecule or siructure) links the
3’ carbon of one sugar of one nucleotide to the 5" carbon of the sugar of the succeeding nucleotide.
The bond formed 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 for example, one of the secondary
structure exhibited by DNA is the famous Watson-Crick model.
: s
5 3
g o]
\
o
|
h. Thymi
ymine sz Adeni
Adenine
o 1"
[e]
_ |
> o] —FI‘—O
9 H H o
o= I;-‘— o
9
HC R,=22 Cylosine
Guanine L ™\ g
|CH’
& k3 ?
Fig. : Diagram indicating secondary structure of DNA
Watson-Crick Model of DNA

e According to this model, DNA exists as a double helix. A DNA molecule has two unbranched
polynucleotide strands. Each polynucleotide strand or chain consists of a sequence of nucleotides linked
together by phosphodiester bonds. The polynucleotide strands are antiparallel, i.e., run in the opposite
direction.
e The two strands are not coiled upon each other but the double strand is coiled upon itself around a
common axis like spiral staircase with base pairs forming steps while the backbones of the two strands
form railings. The backbone of DNA is formed of sugar and phosphate.
s The nitrogen bases are projected more or less perpendicular to the sugar phosphate backbone but face
inside.
# The base-pairing is specific. Adenine is always paired with thymine and guanine is always paired with
cytosine. Thus, all base-pairs consist of one purine and one pyrimidine. Once the sequences of
bases in one strand of a DNA double helix is known, the sequence of bases in the other strand is also
known because of the specific base pairing. The two strands of a DNA double helix are thus said to
be complementary (not identical). This is known as complementary base pairing.
e The two polynucleotide strands are held together in their helical structure by hydrogen bonding between
bases in opposing strands. Adenine and thymine are linked through two hydrogen bonds while guanine
and cytosine are linked through three hydrogen bonds.
e One
end of the strand
is called 5 end where the fifth carbon
of the pentose
sugar is free and the other
end is called 3’ end where the third carbon of pentose sugar is free.
= Ateach base pair, the strand tums 36°. One full turn of the helical strand (360°) involves ten base pairs
ie., one turn of 360° of the helical strand has about 10 nucleotides on each strand of DNA. The base-
pairs in DNA are stacked 3.4 A apart. Thus, pitch of the DNA is 34 A as ten base pairs occupy a
distance of about 34 A.
e This form of DNA with the above mentioned salient features is knownas B-DNA.
3 End @ & End
2 OSER=(g0
$ —
=e o ®
=G OYEI=C30,
Trm
034 nm 221
L T "
e ¥ :
o7 ® ®
Mo -'
SN
OUE=EN20
S~ 5 © ® ¥
=
=\
T iy, OSH=RNp0
DG
® (®
® 4
(a) 5 End L} 3 End
Fig. : DNA double helix
e The DNA is mostly right handed (DNA with right handed coiling). It exists in many forms such as,
() B-form : The usual DNA, having 10 base pairs per tum.
(i) A-form : Having 11 base pairs per tum, the base pairs are not perpendicular to the axis, but are
tilted.
(ili) C-form : Like B form but having 9 base pairs per turn.
(iv) D-form
: Like B form, but have 8 base pairs per tum.
Note: DNA with left handed coiling is called Z-DNA, with 12 base pairs per turn.
Chargaff’ rule :
In 1950, Erwin Chargatf concluded that in any DNA molecule :
(i) The amounts of purines and pyrimidines are equal e, A+ G=T+C.
(i) The amount of adenine is always equal to that of thymine and the amount of guanine is always equal
to that of cytosine (ie., A=Tand G = C).
(i) The base ratio (A + TY(G + C) may vary from one species to another, butis constant
for a given species.
(v) The deoxyribose sugar and phosphate components occur in equal proportions.
RNA : (Ribonucleic acid)
® RNA s usually single—stranded, but sometimes (asin Reovirus and Rice dwarf virus), it is double—stranded
RNA does not follow Chargaff's rules ie., 1: 1 ratio does not exist between purines and pyrimidines
bases due to single—stranded nature and lack of complementarity.
e There
are three types of RNAs:
(i) Messenger RNA (m-RNA): This constitutes nearly 5% of total cellular RNA
(i) Ribosomal RNA (--RNA) :(about 80% of total cellular RNA).
(iii) Transfer RNA or Soluble RNA or adaptive RNA (s—RNA, I-RNA) : (about 10-15% of total cellular RNA).
II
omp—d
| ~on
et
| g Uracil
H H
pmmam, O
Fo==Pmouon,
b ':i::'_rdfi'é'ffi_;:g?\‘:lf_ofinmlaa
st
B { R oy
ol |
L et Sors aami]
e
AL P
W |
omp—p ~Euriin)
| ~on
W&
| _o._ Cviosine
CHE)
" "
e oH
Fig. : A polynucleotide strand of RNA
11. Which of the following amino acid is basic in nature?

(1) Glutamic acid (2) Lysine
(3) Valine (4) Tyrosine
12 Select the false statement regarding proteins.
(1) A protein is a heteropolymer
and not a homopolymer
(2) Collagen is the most abundant protein in the animal world
(3) RuBisCO is the most abundant protein in the whole biosphere
(4) The first amino acid in the polypeptide chain is called C-terminal amino acid and the last amino acid
is called N-terminal amino acid.
13. Mark the incorrect statement about adult human haemoglobin
(1) Itis made up of four sub-units
(2) Two sub-units are of u-type and two sub-units of [i-type
(3) It has quatemary structure w.rt. level of organisation
(4) Itis a simple protein
4. Structural level of organisation in a protein absolutely necessary for the many biological activities is
(1) Primary @) Secondary
(3) Tertiary (4) Quatemary
15. Antibodies that help o fight infectious agents are
(1) Polysaccharides (2) Amino acids
(3) Proteins (4) Glucose
16. Arachidonic acid has
(1) 20 carbons excluding carboxyl carbon (2) 20 carbons including carboxyl carbon
(3) 16 carbons excluding carboxyl carbon (4) 16 carbons including carboxyl carbon
17. Lecithin is
(1) Simple lipid ) Derived lipid
(3) Phospholipid (4) Steroid
18 Which of the following statements is incorrect?
(1) Lipids are strictly macromolecules
(2) Palmitic acid has 16 carbons including carboxyl carbon
(3) Oils have low melting point and hence remain as oil in winters
(4) Arachidonic acid is an unsaturated fatty acid
19. Which one is correct base pairing found in DNA molecules?
(1) Cytosine - Uraci
(2) Thymine — Guanine
(3) Thiamine - Adenine
(4) Cytosine — Guanine
20. Which of the following is not a salient feature of B-DNA?
(1) One full tum of helical strand involves 10 base pairs
(2) Pitch of helix would be 34 A
(3) Diameter of double helix would be 20 A
{4) This DNA exhibits left handed coiling
DYNAMIC STATE OF BODY CONSTITUENTS - CONCEPT OF METABOLISM

# Living organisms contain thousands of organic compounds or biomolecules (also known as metabolites)
that are presentin certain concenirations (expressed as molesflitre etc.) All these biomolecules havea
turnover which means they are constantly being changed into some other biomolecule and also being
made from some other biomolecules. Through chemical reactions, this breaking and making occurs
constantly in living organisms. Together all these chemical reactions are called metabolism.
« Biomolecules get transformed due to metabolic reactions that occur in a living cell/organism.
e Metabolites are converted into each other in series of linked reaction called metabolic pathways.
« Flow of metabolites through metabolic pathway has a definite rate and direction like automobile traffic.
This metabolic flow is called the dynamic state of body constituents.
s In metabolic reactions, every chemical reactions that occurs is a catalysed reaction (reactions that occur
in the presence of a catalyst). Catalyst which accelerates the rate of a given metabolic conversations
(reactions) are known as enzymes. Almost all enzymes are proteins
with catalytic power. Thus, enzymes
are biocatalyst which accelerates the rate of a given metabolic reactions.
s Al chemical reactions occurming in the living systems are mediated through the biocatalysts called enzymes.
Metabolic Basis for Living
* Metabolic pathways can lead to a more complex structure from a simpler structure for example, acetic
acid becomes cholesterol. Such metabolic pathways are called biosynthetic pathways or anabalic
pathways. Another example is formation of proteins from amino acids. Anabolic pathways consume
energy.
e Metabolic pathways can also lead to a simpler structure from a complex structure for example glucose
(6 carbon compound) becomes lactic acid (3 carbon compound) such pathways are called catabolic
pathways. Catabolic pathways leads to release of energy.
e Adenosine triphosphate (ATP) a nucleotide, is called universal energy carrier as well as energy
currency of the cell. ATP is composed of an adenine (a purine), a ribose (pentose sugar) and a row
of three phosphate atlached lo ribose. ATP is found in all living cells.
THE LIVING STATE

e The most important fact of biological systems is that all living organisms exist in a steady state. Steady
state is a non-equilibrium state in which all the biomolecules remain at constant concentration. These
biomolecules are in a metabolic flux.
* Metabolic flux is the rate of turn over of molecules through a metabolic pathway.
® Any chemical or physical process moves spontaneously to equilibrium but at equilibrium no work can
be done. Living organisms cannot afford to reach equilibrium as they work continuously. Therefore, the
living state is a non-equilibrium steady-state to be able to perform work
ENZYMES
® Almost all enzymes are proteins that catalyse the biochemical reactions in living cells, hence called
biocatalysts.
s« Enzymes are proteinaceous in nature (Sumner 1926) with the exception of recently discovered two RNA
enzymes
() Ribozyme : Cech et al, 1981 isolated ribozyme from Tetrahymena
(i) Ribonuclease - P discovered by Altman from bacteria.
s An active site of an enzyme is a crevice or pocket into which the substrate fits. A substrate is a specific
compound acted upon by an enzyme. Thus enzymes, through their active site, catalyse reactions at a
higher rate.
» Enzymes are organic catalysts, there are inorganic catalysts also, which do not occur in living cells.
Table : Differences between enzymes and inorganic catalysts
(i) |Almost all enzymes are proteins and | They are usually
small and simple
have a complex molecular organisation. | molecules like nickel, platinum ete.
cells.
(ii) | They occur inliving They do not occur in living cells.
(iiij|An enzyme catalyses only a specific | They are not specific
for any one reaction
reactions. Y and can catalyse a number of reactions.
(iv)| They get damagedat hightemperatures | They work efficiently at high temperatures
(above 40°C). and pressures.
{v) | Theyare highly efficient. They are less efficient.
e Enzymes isolated from thermophilic organisms who normally live under extremely high temperatures (e.g.,
hot vents and sulphur springs), are thermally stable and retain their catalytic power even at high
temperatures (upto 80°-90°C). Thus thermal stability is an important quality of such enzymes isolated
from thermophilic organisms.
How do enzymes bring about such high rates of chemical conversions?

e The chemical which is converted into a product is called a ‘substrate’. Thus, enzymes i.e., proteins with
three dimensional structures including an active site are capable of converting a substrate (S) into a
product (P). This can be shown as :
s
I Submpane
— P
{Proguct)
e When substrate binds to the active site of enzyme a new structure of the substrate called transition
state structure is formed. There could be many more ‘altered structural states’ between the stable
substrate and the product. In this formation of substrate into product, all other intermediate structural
states are unstable.
« The molecules of the substrate undergo chemical changes i.e., breaking or making of bonds finally the
product is formed and is released from the active site. Hence, enzyme transformes the structure of
substrate into product.
= For a reaction to start, an external supply of energy is needed. It is called activation energy.
s Activation energy required for such a large number of reactions cannot be provided by living systems.
Enzymes lower the activation energy required for a reaction.
: Transition state
Activation energy
without enzyme
g Activation energy with enzyme

g e
z
o
roduct (P)
Progressof reaction
Fig. : Concept of activation energy
* In the given graph, Y-axis represents the potential energy content. Potential energy of a body is its
stored energy. The X-axis represents the progression of the structural transformation of substrate into
product or states through the ‘transition state’, or we can say it represents the progress of reaction.
e If the energy level difference between S and P is such that P is at a lower level than 'S, the reaction
is exothermic. In exothermic reactions, the energy content of the product is lower than that of the
substrate as heatis released. External supply
of energy is not required to form the product.
* When ‘S is at lower level than P, the reaction is endothermic. In endothermic reactions, the energy
content of products is higher. As, heat is absorbed in this reaction.
e The difference in the energy level of substrate (S) and transition state is the activation energy required
to start the reaction.
Nature of Enzyme Action

The catalytic cycle of an enzyme action can be described as follows :
(i) The substrate binds to the active site of the enzyme.
(i) The binding of the substrate induces the enzyme to alter its shape and fit more tightly around the
substrate.
(i) The active site of the enzyme which is in close proximity of the substrate breaks the chemical bonds
of the substrate and an enzyme-product complex is formed.
) The enzymes releases the product(s) of the reaction and the free enzyme is ready to take up another
molecule of the substrate.
Factors Affecting Enzyme Activity
Enzymes are proleins with tertiary structures. Any change in the tertiary structure would affect the activity/
action of enzymes. Factors which can affect the enzyme action are as follows :
(i) Temperature
* The temperature
at which the enzyme shows its highest activity is known as its optimum tem perature.
e« Enzyme activity declines both below and above the optimum temperature.
z
2
H
:
)
Temperature
Fig. : Effect of change in temperature on enzyme activity
(i) Hydrogen ion concentration (pH)
A rise or fall in pH reduces enzyme activity. Some enzymes act best in an acidic medium, others in
an alkaline medium. For every enzyme there is an optimum pH where its action is maximum.
£
H
]
o
w
pH
Fig. : Effect
of change in pH on enzyme activity
(iii) Concentration of substrate
Increase in substrate concentration, increases the velocity of the enzymatic reaction. The reaction
ultimately reaches a maximum velocity (V,,..,) which is not exceeded by any further rise in concentration
of the substrate. This is because, at this stage the enzyme molecules become fully saturated and no
active site is left free to bind additional substrate molecules.
BV,
B2
£ Voo
L
k] ]
= '
82 i
'
K8
Fig. : Effect of change in : Concentration of substrate on enzyme activity
* K (Michaelis constant) is a mathematical derivation or constant which indicales the substrale

concentration at which the chemical reaction catalysed by an enzyme attains half its maximum
velocity.
Mechanism of Enzyme Action :
Two hypothesis have been put forward to explain the mode of enzyme action.
1. Lock and Key Hypothesis : This hypothesis was given by Emil Fischer (1894).
This theory explains how a small concentration of enzyme (lock) can act upon a large amount of the
substrate (key). It also explains how the enzyme remains unaffected at the end of chemical reaction. The
theory explains how a substance having a structure similar to the subsirate can work as a competitive
inhibitor.
2. Induced Fit Hypothesis : This hypothesis was proposed by Koshland (1960). According to this model,
the enzyme (or its active site) is flexible. The active site of the enzyme contains two groups-
(a) Buttressing group is meant for supporting the substrate.
(b) Catalytic group is meant for catalysing the reaction. When substrate comes in contact with the
butiressing group, the active site changes to bring the catalytic group opposite the substrate for bonds
to be broken or formed.
Inhibition of Enzyme Activity

Any substance that can diminish the velocity of an enzyme-catalyzed reaction is called an inhibitor. The two
most commonly encountered types of inhibition are competitive and noncompetitive.
A. Competitive inhibition :This type of inhibition occurs when the inhibitor binds reversibly to the same site
that the substrate would normally occupy and therefore, competes with the substrate for that site
1. EffectonV,,, : The effect of a competitive inhibitor is reversed by increasing [S].

2. Effect on K, : A competitive inhibitor increases the apparent K,, for a given substrate. This means
that in the presence of a competitive inhibitor more substrate is needed to achieve 12 V.. eg.,
Inhibition of alcohol dehydrogenase by ethanol in methanol poisoning, sulpha drugs for folic
acid synthesis in bacteria and Inhibition of succinic dehydrogenase by malonate and
oxaloacetate.
. | I
(I:Hl Clfla
CH, coo
Succinate Malonate
) 1‘ Malonic acid (competitive inhibitor)
' ' .
Succinic Succinic acid Active centre Substrate

dehydrogenase (substrate) of enzyme unused
blocked by inhibitor
Fig. Competitive inhibition of enzyme action
Competitive inhibitors are frequently used in the control of bacterial pathogen. All cells require folic acid
for growth. Folic acid cannot cross bacterial cell walls by diffusion or active transport. For this reason
bacteria must synthesize folic acid from P-aminobenzoic acid. Sulpha drugs act as inhibitors and
compete with the substrate P-amino benzoic acid (PABA) for the active site of the enzyme. This
binding of inhibitor to the enzyme prevents the synthesis of folic acid and thus growth of bacterial
pathogens is controlled.
. SO.NH, COOH
NH, NH,
Sulphanilamide PABA
o Ve [T s
2 Inhibitor F.\
58' =" Wit competiiive
vl /. Inhibitor
ey ¥
vl
3
g 4 (apparent K, in presence
. [} ot a competitve inhibitor)
I N
K, Michaelis constant, K. is increased
in the presence of a competitive inhibitor
Fig. Effect of a competitive inhibitor on the reaction velocity (V) versus substrate [S] plot.
B. Non-competitive inhibition : This type of inhibition is recognized by its characteristic effect on Vg,
Noncompetitive inhibition occurs when the inhibitor and substrate bind at different sites on the enzyme.
The noncompetitive inhibitor can bind to either the free enzyme or the ES complex, thereby preventing the
reaction from occurring.
1. Effect on V,,: Noncompetitive inhibition cannot be overcome by increasing the concentration of
substrate. Thus, noncompetitive inhibitors decrease the V,,, of the reaction.
2. Effect on K, : Noncompetitive inhibitors do not interfere with the binding of substrate to enzyme. Thus,
the enzyme shows the same K, in the presence or absence of the noncompetitive inhibitor. e.g.,
cyanide kills an animal by inhibiting cytochrome oxidase.
z Inhibitor
g N
F-J ~ S ——
T Vo . / With noncompetitive
§ 2 4 ~ Inhibitor
1 of
74 ¢
sl
K, \ Michaelis constant, K., is unchanged
in the presance of a noncompetitive inhibitor
Fig. : Effect of a noncompetitive inhibitor on the reaction velocity (V,) versus substrate [S] plot.
C. Allosteric Modulation or Feedback Inhibition: The activities of some enzymes, particularly those which
form a part of a chain of reactions (metabolic pathway), are regulated internally. Some specific low
molecular weight substance, such as the product(s) of another enzyme further on in the chain, acts as
the inhibitor. Such a modulator binds with a specific site of the enzyme different from its substrate-binding
site. This binding increases or decreases the enzyme action. Such enzymes are called Allosteric
Enzymes.
Examples :
(a) Hexokinase changes the substrate glucose to product glucose-6-phosphate in glycolysis. Decline in
its enzyme activity by the allosteric effect of the product is called Feedback Inhibition, e.g., allosteric
inhibition of hexokinase by glucose-6-phosphate.
(b) Enzyme phosphofructokinase is activated by ADP and inhibited by ATP.
(c) Ancther example is inhibition of threonine deaminase by isoleucine. Amino acid isoleucine is formed
in bacterium Escherichia coli in a 5-step reaction from threonine. When iscleucine accumulates
beyond a threshold value, its further production stops.
Classification and Nomenclature of Enzymes

Enzymes are divided into six classes :
(i) Oxidoreductases / dehydrogenases : Enzymes which catalyse oxidation-reduction reactions involving
transfer of electrons/H* from one molecule to ancther. In these reactions one compound is oxidised and
other is reduced.
Example - dehydrogenase, oxidases, reductases, calalase, peroxidase.
(i) Transferases : These enzymes catalyse the transfer of specific groups other than hydrogen from one
substrate to another.
Example - Transaminase (transfers amino group), Kinase (catalyse the phosphorylation of substrate by
transferring phosphate group usually from ATP).
(iii) Hydrolases : These enzymes catalyse the breakdown of larger molecules into smaller molecules with
the addition of water. They catalyse hydrolysis of ester, ether, peptide, glycosidic, C-C, C-halide or
P-N bonds.
Example - Proteases, amylases, lipases, maltase, nucleases and other digestive enzymes.
(iv) Lyases : These enzymes catalyse the cleavage of substrate into two parts, without the use of water
or removal of groups without hydrolysis. A double bond is formed at the place of removal of group.
Example - Aldolase, decarboxylase, carbonic anhydrase etc.
(v) Isomerases : These enzymes catalyse the rearrangement of molecular structure to form isomers. Isomers
are molecules or molecular compounds that are similar in that they have the same molecular formula
however have different arrangements of the atoms or group of atoms involved. They catalyse inter-
conversion of optical, geometric or positional isomers.
Example - Isomerase
(vi) Ligases : These enzymes catalyse covalent bonding of two substrates to form a large molecule. They
catalyse joining of C-O, C-S, C-N, P-0 etc. bonds by using energy of ATP
Example - RUBP carboxylase, ligase, Phosphoenol pyruvate (PEP carboxylase) etc.
« Intemational Union of Biochemistry (JUB) appointed an Enzyme Commission (EC) in 1961 which devised
some basic principles for classification and nomenclature of enzymes. IUB system has divided enzymes
into six major classes. Each class in turn is subdivided into many subclasses which are further divided.
A four digit enzyme commission (EC) number (e.g., 5.2.1.7) is assigned to each enzyme represents :
@M Fdigit ~ Class
(i) I digit — Subclass
(i) medigt - Sub-subclass
(v) Iv= digit — Individual enzyme
Properties of Enzymes
« Protein nature: Enzymes are generally proteins. They may have additional inorganic or organic
substances for their activity.
* Chemical reaction: Enzymes
do not start a chemical reaction but increase the rate of chemical reaction
They do not change the equilibrium but bring about equilibrium very soon.
« Efficiency: The number of substrate molecules changed per minute by a molecule or enzyme is called
turnover number. The higher the tum-over number, the more efficient an enzyme is
* Unchanged form: Enzymes are in no way transformed or used up in the chemical reaction.
s Enzyme specificity: Enzymes are highly specific in their action. For example, enzyme mallase acts
on sugar maltose but not on laciose or sucrose.
Co-factors
Many enzymes exhibit the catalytic activity only in association with certain non-protein substances. Such
substances are called co-factors. In these .enzymes the protein portion is known as apoenzyme.
Holoenzyme = Apoprotein + Cofactor
Three types of co-factors are identified :
() Prosthetic group : They are organic compounds and are tightly bound to the apoenzyme. For example,
haem is the prosthetic group in peroxidase and catalase enzymes that catalyze the breakdown of
hydrogen peroxide to water and oxygen. Haem (prosthetic
group) is a part of the active site of the enzyme.
(ii) Co-enzymes : They are also organic compounds but their association with the apoenzyme last for a
short period of time, usually occurring during the course of catalysis. The essential chemical components
of many coenzymes are vitamins, e.g., coenzyme nicotinamide adenine dinucleotide (NAD) and NADP
contain the vitamin niacin.
(iii) Metal ions : 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 coordination bonds with the
substrate. Example, zinc is a co-factor for the proteolytic enzyme carboxypeptidase.
Note: Catalytic
activity is lost when the co-factoris removed from the enzyme which lestifies that they
playa crucial role in the catalytic activity of the enzyme.
Fe™, Fe™ Cytochrome oxidase, catalase, aconitase, peroxidase
Ca* Lipase, Succinic dehydrogenase
Mg™ Hexokinase, pyruvate kinase, DNA polymerase, enolase, phosphotransferase
Zn** Alcohol dehydrogenase, Carbonic anhydrase, LDH, carboxypeptidase
cr Salivary amylase
21. Al the following statements are correct about enzymes, but one is wrong. Select the incorrect statement.
(1) Almost all enzymes are proteins
(2) There are some nucleic acids which behave like enzymes and are called ribozymes
(3) Enzymes obtained from thermophilic organisms retain their catalytic power even at high temperatures
up to 80-90°C
(4) Ribozyme was discovered by Altman et al.
22, Study the reaction given below
€O, +H,0—2™ 1,co,

In absence of any enzyme this reaction is very slow, with 200 molecules of H,CO, being formed in an hour.
In presence of enzyme the reaction speeds up dramatically with about 600,000 molecules formed every
second. Select the enzyme which has accelerated up the reaction by 10 million times.
(1) Ribozyme
(2) Carbonic anhydrase
(3) Catalase
(4) Peroxidase
23. Which of the following is not an example of competitive inhibition?
(1) Inhibition of succinic dehydrogenase by malonate
(2) Sulpha drugs used to control bacterial pathogens

(3) Inhibition of alcohol dehydrogenase by ethanol in methanol poisoning
(4) Inhibition of hexokinase by glucose-6-phosphate
24, Set of coenzymes that are nucleotides of vitamin niacin is
(1) NAD, NADP
(2) FMN, FAD
(3) ATP, ADP
(4) ATP, FAD
25. A cofactor for the proteolytic enzyme carboxypeptidase is
() Znc (2) Copper

@) Calcium @) Magnesium
26. Group of enzymes that helps in catalysing a transfer of a group (other than hydrogen) between a pair of
substrates is
(1) Oxidoreductases
(2) Transferases
(3) Lyases
(4) Isomerases
27. Factor(s) which can influence enzyme activity is/are
(1) High temperature @

(3) Substrate concentration (4) Al of these
28. What would happen to V___ in presence
of a competitive inhibitor?
(1) Decreases
(2) Increases
(3) Remains the same
(4) First increases then decreases

29. Study the following graph of concept of activation energy given below. Select the correct option for stages
labelled A to D.
B
(=
D X AN
Substrate (s)
uct (P)
Progressof reaction
A B c D
(1) Transition State Potential energy Activation energy Activation energy
without enzyme with enzyme
(2) Kinetic energy Potential energy Activation energy Activation energy
(3) Potential energy Transition state Activation energy Activation energy
(4) Potential energy Transition state Activation energy Activation energy
without enzyme: without enzyme
30. Enzymes work at optimum temperature.
Over a range of 5 — 40°C, what would happen to the rate of enzyme
controlled reactions for every 10°C rise in temperature?
(1) The rate doubles itself (2) Decreases by half
(3) No effect (4) First increases than decreases
m -
-
ssignm
= >
L
B 6. Dehydration synthesis during peptide bond

SECTION -A formation involves loss of which molecule?
NCERT Based MCQs [NCERT Pg. 151]
1. A six carbon sugar with aldehydeINCERT
group isPg, 145] "
(1) Amino acids ) co,
) (3) NH, (4) Water
; 7. Hydroxymethyl is the side chain of which amino
{2) Deoxyribose acid? [NCERT Pg. 144)
(3) Glucose (1) Tyrosine
(4) Fructose (2) Serine
2. Monomeric unit is not available for @ Cysteine
[NCERT Pg. 143] @ T
(1) Proteins (4) Tryptophan
L 8. Sugars such as glycogen are characterized by
@) Lipids presence of which set of functional groups?
(3) Polysaccharides [NCERT Pg. 148]
(@) Nucleic acids (1) Hydroxyland amino
3. Phosphodiester bond is characteristically found in Sulthydryl and phosphats
[NCERT Pg. 151] @ yant
; . (3) Carbonyl and hydroxyl
(1) Deoxyribonucleic acid )
@) Chitin (4) Carbonyl and amino
o 9. A molecule of ATP bears maximum resemblance
(3) Phospholipid o [NCERT Pg. 153]
) Celulose (1) Palmitic acid
4. Catalytic activity of carboxypeptidase is lost upon (2) Amino acid
removal of cofactor [NCERT Pg. 159] .
(1) Coenzyme (@) Prosthetic group @ DNA nucleotide
(4) RNA nuclectide
©) o o 2" 10. Biocatalysts [NCERT Pg. 154]
5. Read the given statements [NCERT Pg. 151] ‘ ) )
Statement-A : If the total amount of adenine in (1) Hasten the rate of a given metabolic conversio
eukaryotic ds DNA is 30% then total pyrimidine @) Are mostly nucleic acils
content is 50%. (3) Work at similar temperature and pH optima
Statement-B : Nitrogenous bases do not form part (4) Act by altering the equilibrium of the reaction
of backoone in DNA. 11. Monomer of the most abundant biomolecule on
Select the correct option. earth is [NCERT Pg. 148]
(1) Statement A is incorrect (1) Glycine
(2) Statement B is incorrect (2) N-acetylglucosamine
(3) Both statement
A & B are incorrect (3) Glucose
{4) Both statement A & B are correct @) ATP
‘Aakash Educational Services Limited - Regd. Office : Aakash Tower, 8, Pusa Road, New Delhi-110005 Ph. 011-47623456
12. Select the correct match between column | and 16, Which of the following statements is wrong?
column Il [NCERT Pg. 146]
Column | Column I (1) Hydrogen bonds are crucial for stabilising the
a. Cellulose (i) Storage homo- alpha helical structure in a given protein
polysaccharide (2) Transient state structure of the substrate
b. Chitin (i) Structural homo- formed during an enzymatic reaction is high
polysaccharide energy and unstable
c. Inuini ii Branched polymer

(iii)
of glucose
¢ 3) Complementary
i
RNA if needed
base pairing is applicable to
(4) Concanavalin A is a lectin which is

d. Glycogen (iv) Exoskeleton of N . "
arth categorised as a primary metabolite
) Cannot
zp 1, 17. Which
i of the following
i is not a fatty acidid?
molecules [NCERT Pg. 144]

Choose the correct option. [NCERT Pg. 149] (1) Uridylic acid (2) Paimitic acid
(1) a(v). blv), c(i), d(iii) (2) afii), biii), c{i), d(iv) (3) Stearic acid {4) Arachidonic acid
" . A& bl & i 18. Select the correct set w.r.t essential amino acids
(3) a(v). biiv), cfii), ?‘l) (4] a(ii), bliv), cfiii), d(i)
(4) for an adult man. [NCERT Pg. 147]
13, Select the non-reducing sugar among the following. (1) Glycine, jonine, cystine
[NCERT Pg. 161] (2) Glutamic acid, histidine, serine

(1) Galactose (2) Fructose () Tyrosine, lysine, proline
(3) Glucose (4) Sucrose (4) Leucine, valine, phenylalanine
4. Select the incorrect match. [NCERT Pg. 145] 19, Substitution of methane can result in formation of
(1) Lecithin — Phosphoglyceride [NCERT Pg. 143]
(2) Competitive inhibition — Decrease in K, and (1) Monosaccharides
Vi, Value (@) Amino acids
(3) Heterocyclic ring — Adenine and (3) Glycerol
geanine ) Nucleic acids

4 oenzy| - Vitamin derival
“e mes B m 20. Competitive inhibitor of an enzyme
15. Select the correct maich based on graph given INCERT Pg. 158]
1 (1) Increases K, value of substrate for that

K enzyme
g3
® g E (2) Decreases K, value of substrate for that
£E2 enzyme
T
HE .
§=2 (3) Decreases V,, value of the enzymatic
A B C D E F 4) Increases V,_, value of the enzymatic reaction

Companent — - o .
21. Biomicromolecule present in acid soluble
pool is a
[NCERT Pg. 147]
D A- . [NCERT Pg. 143]
(1) A - Proteins (1) Nucleic acid
2) E - Lipids (2) Nucleotide
(3) B - Nucleic acids @) Protein
) C-lons (4) Polysaccharides
22. Choose
the odd one w.rt homopolymers 26. Select the correct option which shows the
[NCERT Pg. 149] structure of a zwitterion. [NCERT Pg. 144]
(1) Peptidoglycan (2) Chitin E R - R
(3) Starch (4) Cellulose (U] H‘,'N—éH—CDOH @ I-QN—'&H—CDO'
23. The nitrogenous base not present in DNA is -
IHCERT o161 (3) H.N jrkcoou @) H,N —CH-CO00"
(1) Adenine (2) Thymine
(3) Cylosine ) Uraci 27. Factor which does not affect the enzymatic action
24. Select the option which is mismatched. of ic anhydrase is INCERT Pg. 157]
[NCERT Pg. 158] (1) Temperature
(1) Transferases — Transfer
of specific groups. @) pH
other than hydrogen from (3) Concentration of substrate
one substrate to another s
(4) Activation energy
(2) Isomerases - Catalyse the - . ) .
rearrangement of 28 A’ and B’ constitute sucrose which is a
molecular structure to ‘C’ sugar A, B and C in the above stalement
form isomers represent [NCERT Pg. 161]
(3) Ligases — Catalyse the cleavage of (1) Glucose, fructose, reducing
substratehydrolysis
without into two parts, (2) Gl Glucose, galactose, non-reducing
i
(3) Galactose, glucose, reducing

(4) Dehydrogenases — Catalyse oxidation-
reduction reaciion involving 4) Glucose, fructose, non-reducing
transfer of electrons. 29. Biomolecule which cannot be considered as a
25. The graph given below is showing the concept of polymer is [NCERT Pg. 144]
activation energy. Identify A and B in options given (1) RuBisCO (2) Gingelly oil
below.
. (3) Glycogen @) Cellulose
A
SECTION - B
I s Obijective Type Questions

sififiéf' ———— 1 Vér::h of the following amino acid is represented by
(1) Tyrosine (2) Glutamic acid

(3) Cysteine (4) Tryptophan
Broduct (P) 2. Given below is a list of some fatty acids.
Progress of raction (a) Stearic acid (b) Oleic acid
[NCERT Pg. 156] (c) Linoleic acid (d) Linolenic acid
A B (e) Arachidic acid
(1) Transition state Potential energy How many of them are unsaturated essential fatty
(2) Potential energy Transition state acids?
(3) Activation energy Activation energy (1) Two
without enzyme with enzyme (2) Three
{4) Activation energy Activation energy (3 Four
with enzyme without enzyme (4) Fre
3. Mark the incorrect match w.rt protein and their 9. Which of the following factor affecting enzyme
corresponding function activity is depicted in the given graph?
(1) GLUT4 ~ Enables glucose
transport into cells TV
@) Indin _ s
c
(3) Rennin - Enzyme v,
@) Coliagen — inkrcollular ground g A
substance T
4. Inhibition of succinate dehydrogenase is caused by E :
malonate. What will happen to the K of the £ H
enzyme when excess of succinate is added? K,
(1) K, will increase and V, _, constant
(2) K, will decrease and V,,, constant (1) pH
(3) K, constant and V,_ decreases (2) Temperature
) K constant and V,__ increases (3) Product concentration
5. InB-DNA, what will be the number of nitrogenous (4) Substrate concentration
bases per helical tumn? 10. Mark the odd one w.r.t. the component in given
(1) 10 struciures
@ 20 (1) Cytosine (2) Guanosine

@ 40 (3) Adenosine (4) Uridine
@) 60 11. Identify the amino acids A and B given below.
6. An enzyme obtained from a plant source has been A B

classified by enzyme commission and allocated its . R
unique four digit number 1.2.1.4. To which of the T‘ '\1
following class does it belong? NH, - C — COOH NH, - C - COOH
| |
(1) Ligase CH, CH,
(2) Oxidoreductase ‘SH
(3) Hydrolase
(4) Isomerase oH
7. Given below is list of some biomolecules.
(@) Keratin {b) Nuclease Choose the correct option.
(€) Insulin (d) Glucose A 8

. 1) Serine Phenylalanine
(e) Glycine o o . e
How many of them are macromolecules and are @ ne yrosine
present in retentate during analysis of (3) Cysteine Tyrosine
biomolecules? (4) Cysteine Phenylalanine
(1) Two (2) Three 12. Which of the following is the prosthetic group in
(3) Four (4) Fve enzyme in peroxidase and catalase?
8 Which of the following secondary metabolites (1) Znc

belong to toxin category? (2) Haem
(1) Codeine (2) Concanavalin-A (3) NAD
(3) Anthocyanin (4) Ricin (4) NADP
13. is the most abundant chemical in .

living organisms. NH,
(1) Protein (2) Water @ ] "> — Ademiceisa
(3) Glucose (4) Sucrose H pyrimidine present
14. Sugars are commonly called carbohydrates and inRNA
hexoses are the sugars having six carbons, twelve
hydrogen and six oxygen atoms. Mark the odd one . (l?,OOH
w.rt. hexose sugar. @ H- ? ~NH, - Glycine provides
(1) Glucose (2) Lactose H nitrogen and carbon
®3) Galactose (4)(4) Man Mannose atoms for the

synthesis of haem
15. Choose the incorrect statement w.rt B-DNA.
(1) At each step of ascent, the strand tuns 36° 19. Which of the following statements is incorrect
2) The pitch would be 34 A wrt starch?
(3) The rise per base pair would be 3.4 nm (1) Starch is a stored food of plants
(4) There are two hydrogen bonds between (2) Starch is a polymer
of a-glucose units
adenine and thymine (3) Amylose and amylopectin are two types of
16. Find out the correct option where both the given components of starch
secondary metabolites belong to the same (4) Amylose is linear branched structure
category. consisting of glucose units joined by o (1, 4)
(1) Vinblastin and rubber glycosidic and « (1, 6) glycosidic linkages
(2) Gums and cellulose 20. Which one is the most abundant protein in the
(3) Morphine and carotencid animal worid?
(4) Abrin and curcumin (1) Insulin (2) Collagen
17. Al of the following statements are comect w.rt the (3) Haemogiobin (4) Myosin
structure of polysaccharides, except 21, Mark the wrong statement.
(1) Inulin is a polymer of fructose (1) Zinc is a cofactor for proteclytic enzyme
(2) The right end of polysaccharide chain is carboxypeptidase
nonrecuing end and belt sad i reducing and 2) K, (Michaelis constant) is numerically
(3) Starch is a branched homopolymer of glucose equivalent to %2 V,
and‘ can hold iodine molecules in the helical (3) Both strands of B DNA together appear ke a
helical staircase
(4) Plant cell walls are made up of cellulose and ~
cellulose does not contain complex helices @) Tymsmle, Ph‘enyda%a-\r\e and Tryptophan are
and hence, cannot hold iodine Momac smino scuis
18, Which of the following is a correct description of ~ 22, u-keratin protein assumes secondary structure
the given biomolecules? through the formation of
. (1) Intrachain hydrogen bonds
HOCH, Adenil
o ine (2) Interchain hydrogen bonds
m — Adenosine, found in (3) Peptide bonds
DNA () Interchain disulphide bonds
23. Cholesterol is a
(2) CH,CH,),~COOH — Palmitic acid is P
unsaturated essential (1) wax @) Trigyceride
fatty acid (3) Steroid (4) Phospholipid
24. Which of the following glycosidic bond is found in R

sucrose? SECTION - C
M) at, 4 Previous Years Questions
@p14 1. Prosthetic groups differ from co-enzymes in that
@ 1' . [NEET-2019 (Odisha]
al,
(1) They can serve as co-factors in a number of
) a-1,p-2 enzyme - catalyzed reactions
25. Protein part of conjugated enzyme is known as (2) They require metal ions for their activity
(1) Holoenzyme (3) They (prosthetic groups) are tightly bound to
@ c apoenzymes.
@ s . ”(4) Their A . .
association with apoenzymes is tfament
2. “"Ramachandran plot” is used to confirm the
(4) Prosthetic group structure of [NEET-2019 (Odiisha)]
26. Allosteric modulation is due to the inhibitory action (1) DNA (2) RNA
faced by an enzyme due to @ ins @) Triacylglycerides
(1) Compelitive reversible inhibition 3. Which of the following organic compounds is the
(2) Non-competitive irreversible inhibition main constituent of Lecithin?
(3) Accumulation of products [NEET-2019 (Odisha)]
(4) Accumulation of substrate (1) Phosphoprotein
27. Which are structural polysaccharides? (2) Arachidonic acid
(1) Starch and cellulose (3) Phospholipid
(2) Chitin and cellulose ) Chol .
N . 4. Concanavalin A is [NEET-2019]
(3) Inulin and chitin i
(1) an alkaloid
@) VGIyeogen and starch ) ) @ ane: il oil
28. Which are not the examples of derived lipids? @) a lectin
(1) Estrogen, progesterone, vitamin A (4) a pigment
(2) Carotenoids, bile acids 5. Consider the following statement :
(3) Waxes, fats, oils (A) Coenzyme or metal ion that is tightly bound to
(4) Diosgenin, prostaglandin, cortisone enzyme prolein is called prosthetic group.
. . (B) A complete catalytic active enzyme with its
29. Find the incorrect statement about chitin. bound prosthetic is called apor
4] mfinexmlemnofa‘mmpodsflmngal Salect the comect oplion. [NEET-2019)
@ F of N A (1) Both (A) and (B) are true.

ormec -H.B'y lucosamine monomer
o E o v o (2) (A)is true but (B) is false.
(3) Formed (1-4), glycosidic bond between
monomers (3) Both (A) and (B) are false.
) ) (4) (A) s false but (B) is true.
(4) Itis a heteropolymeric polysaccharide
# 6. Purines found both in DNA and RNA are
30. The helical structure of a protein is stabilized by [NEET-2019)
(1) Peptide bond (1) Adenine and thymine
(2) Hydrogen bond (2) Adenine and guanine
(3) Ether bond (3) Guanine and cytosine
(4) lonic bond (4) Cytosine and thymine
7. The two functional groups characteristic

of sugars (1) Endothermic reaction with energy A in
are [NEET-2018] presence of enzyme and B in absence of
(1) Hydroxyl and methyl anzyma
(2) Carbonyl and methyl (2) Exothermic reachun with energyA in presence
@ c i and hydroxyl of enzyme and B in absence of enzyme
{4) Carbonyl and phosphate (3) Endothermic reacmn with energyA in absence
of enzyme and B in presence of enzyme
8. Which of the following are not polymeric? )
[NEET-2017) (4) Exothermic reaction with energy A in absence
(1) Nuciic acids of enzyme and d BB in presence of enzyme
@) Proteins 13. Atypical fat molecule is made up of [NEET-2016]
(3) Polysaccharides (1) Three glycerol and three fatty acid molecules
) Lipids (2) Three glycerol molecules and one fatty acid

9. Which one of the following statements is correct,
with reference to enzymes? [NEET-2017] (3) One glycerol and three fatty acid molecules
(1) Apoenzyme = Holoenzyme + Coenzyme (4) One glycerol and one fatty acid molecule
(2) Holoenzyme = Apoenzyme + Coenzyme 14, Which one of the following statements is wrong?
(3) Coenzyme = Apoenzyme + Holoenzyme [NEET-2016]
{4) Holoenzyme = Coenzyme + Cofactor (1) Glycine is a sulphur containing amino acid
10. A non-proteinaceous enzyme is @ s is a disaccharide
[NEET (Phase-2) 2016] ) )
M (3) Cellulose is a polysaccharide
ysozyme
i (4) Uracil is a pyrimidine
(2) Ribozyme
@ L 15. Which of the following biomolecules does have a
" ) Ligase ] phosphadiester bond? [Re-AIPMT-2015]
“) D " (1) Nucleic acids in a nucleotide
1. Which of the following is the least likely to be . .
involved in stabilizing the three-dimensional folding (2) Fatty acids in a diglyceride
of most proteins? [NEET (Phase-2) 2016] (3) Monosaccharides in a polysaccharide
(1) Hydrogen bonds (4) Amino acids in a polypeptide

@) Electrostatic interaction 16, The chitinous exoskeleton of arthropods is formed
(3) Hydrophobic interaction by the polymerisation of : [Re-AIPMT-2015]
{4) Ester bonds (1) Lipoglycans
12. Which of .the following describes the given graph " -
o [NEET (P 2016) (2) Keratin sulphate and chondroitin sulphate
(3) D-glucosamine
- (4) N-acetyl glucosamine
I 17. Which one of the following is not applicable to
B RNA? [Re-AIPMT-2015]
E " (1) Chargaffs rule
o e (2) Complementary base pairing
i (3) 5 phosphoryl and 3 hydroxyl ends
Product -
P (4) Heterocyclic nitrogenous bases
18. In sea urchin DNA, which is double stranded 17% 23, The essential chemical components of many
of the bases were shown to be cytosine. The coenzymes are: [NEET-2013]
percentages of the other three bases expected to o
be present in this DNA are [AIPMT-2015] {1} iciato acsis (2) Carbohydrates
(1) G 85%, AS50%, T 24.5% (@) Vitamins ) Proteins
24, Transition state structure of the substrate formed
(2) G 34%, A24.5%, T 24.5% during an enzymatic reaction is: [NEET-2013]
(3) G 17%, A 16.5%, T 32.5% (1) Permanent
but unstable
(4) G 17%, A 33%, T 33% (@) Transientand unstable
19. Which one of the following statements is
Incomect? [AIPMT-2015] @ Permanent
and stable
(1) The presence of the competilive inhibitor () Transient but stable
decreases
the K,, of the enzyme for the substrate ~ 25. Macromolecule chitinis [NEET-2013)
(2) A competitive inhibitor reacts reversibly with the (1) Phosphorus containing polysaccharide
enzyme to form an enzyme-inhibitor complex (2) Sulphur containing polysaccharide
(3) In competitive inhibition, the inhibitor molecule Simple polysaccharid
is not chemically changed by the enzyme @ ,mp . ° R
o (4) Nitrogen containing polysaccharide
(4) The competitive inhibitor does not affect the .
rate of breakdown of the enzyme-substrate 26 Whichoneoutof
A D given below correctly represents
complex the structural formula of the basic amino acid?
20, Seectthe opton which s netcomrtwitrespect

to enzyme action: [AIPMT-2014]
[ NA [ 8N [ cHon
© | 5 |
. NH,
1)
(1) Substrate
Sul binds
inds with enzyme atits active sifsite I
He—o— L
H— Gt coom| !
cH, i
(2) Addition of lot of succinate does not reverse the | ] ] c‘:H
inhibition of succinic dehydrogenase by malonate CH, CH, CH, M
(3) A non - competitive inhibitor binds the enzyme ‘cu, [ INH, CH,
at a sile distinct from that which binds the | !:H,
substrate
T Mon
C,
{:H,
(4) Malonate is a competitive inhibitor of succinic [s] NH.
dehydrogenase -
21. Which one of the following is a non - reducing [AIPMT (Prelims)-2012]
carbohydrate? [AIPMT-2014] 1) A @ 8B
(1) Maltose (2) Sucrose @ c 4) D
(3) Lactose (4) Ribose 5-phosphate 27. Given below is the diagrammatic representation of one
22 Aphosphog
e
ide is always mad of:
of the categories of small molecular weight organic
. fyceri b i o P compounds in the living tissues. Identify the category
[NEET-2013) shown and the one blank component “X" in it
(1) Only an unsaturated fatty acid esterified 1o a HOGH, O_"X"
glycerol molecule to which a phosphate group
is also attached
(2) A saturated or unsaturated fatty acid esterified
to a glycerol molecule to which a phosphate
group is also attached [AIPMT (Prelims)-2012]
(3) A saturated or unsaturated fatty acid esterified Category Component
to a phosphate group which is also attachedto (1) Nucleotide Adenine
a glycerol molecule @ N cide Uracil
(4) Only a saturated fatty acid esterified to a glycerol N
molecule to which a phosphate group is also (3) Cholesterol Guanin
attached (4) Amino acid NH,
28. For its activity, carboxypeptidase requires (1) A: Lecithin — a component of cell membrane
[AIPMT (Mains)-2012] (2) B: Adenine — a nucleotide that makes up
(1) Copper (2) Znc nucleic acids
(3) lron (4) Niacin (3) A: Triglyceride — major source of energy
29. Which one of the following biomolecules is (4) B: Uracil — a component of DNA
orrectly clerised? [AIPMT
« ’ Chafi_‘ i k ‘ (Malnf)-ZtHZ] 32, The figure given below shows the conversion of a
(1) Alanine amino acid — Contains an amino group substrate into product by an enzyme. In which one
and an acidic group anywhere in the molecule of the four options (1-4) the components of reaction
(2) Lecithin — a phosphorylated
glyceride found in labelled as A, B, C and D are identified correctly?
cell membrane . N
(3) Palmitic acid - an unsaturated fatty acid with
18 carbon atoms c
(4) Adenylic acid — adenosine with a glucose
phosphate molecule
30. The curve given below show enzymatic activity with o
relation to three conditions (pH, temperature and BT T
substrate concentration)
@
E Product )
Frogress
of rescton
x-axis [AIPMT (Mains)-2010]
What do the two axes (x and y) represent? )
X-axis
et praimeyoy || A | 8 | ¢ [ © |
y-axis Potential Transition | Activation |Activation
N o 1) |energy state energy with| energy with-|
(1) Enzymatic activity Temperature M enzyme |outenzyme
(2) Enzymatic activity MH 2 Transiion | Potential | .- : tio ficm?m
(3) Temperature Enzyme activity state energy erzyae

oiva
{4) Subsrate concentration Enzymatic activity 3) |Acivaton | rensiton |ooaea on, | Potential
i . ) energywi st RO ) ey
31. Which one of the following structural formulae of two out enzyme enzyme
oorganic compound is correctly identified along with 4) | Activation ctivation
its related function 4) | anergy with T':’;t‘:“' energy wil :flm'flflhl'
enzyme lout enzyme oy
CH,—O—E—R 33. Three of the following statements about enzymes

? 1 are correct and one is wrong. Which one is
A m+o_?4 o wrong? [AIPMT (Mains)-2010]
CHZ—O—!—O—CH,—?HZ (1) Enzymes require optimum pH for maximal
bk ity
CHnéHCHS (2) Enzymes are denatured at high temperature
NH, N but in certain exceptional organisms they are
effective even at lemperatures 80°-90°C
(3) Enzymes are highly specific
[AIPMT (Prelims)-2011] (4) Most enzymes are proteins but some are
lipids
34. Whichoneofthe
following pairsiswronglymatched? 40, Carbohydrates,
the mostabundant biomolecules on
[AIPMT (Prelims}-2009] earth, are produced by [AIPMT (Prelims)-2005]
) A _ Nitrogenase (1) All bacteria, fungi
and aigae
@) Fruitjuice - Pectinase (2) Fungi, algae and green plant cells
(3) Textle — Amylase (3) Some bacteria, algae and green plant cells
@) De nts — Lk 4) Viruses, fungi and bacteria
. 41, Which of the following statements regarding enzyme
35. Carbohydrates are commonly found as starch in ;
plant s e organs. Which of the following five inhibition is correct 7 [AIPMT (Prelims)-2005]
properiies of starch (a - e) make it useful as a (1) Non-competitive inhibition of an enzyme
can be
storage material? [AIPMT (Prelims)-2008] overcome by adding large amount of substrate
a. Easily translocated (2) Competitive inhibition is seen when a substrate
b C ical nol ive competes with an enzyme for binding
to an
3 inhibitor protein
c. Easily digested by animals (3) Competitveinhibitionis sean the
d. Osmotically inactive and the inhibitor compete
e. Synthesized during photosynthesis (4) Non-competitive inhibitors often bind to the
The useful properties are enzyme ireversibly
42, Thecatalyticefficiency
of two differentenzymes can
(1) Botha & e @) Bothb & be comparedbythe [AIPMT (Prelims)-2005)
(3) Bothb & d 4) a,cle (1) TheK, value
36. An organic substance bound to an enzyme and N
essen?ialk)rfls iv ty is called (2) The pHoptimum
value
[AIPMT (Prelims)-2006] (3) Formation of the product
@ c @ nzyme (4) Molecular size of the enzyme
(3) Apoenzyme (4) Isoenzyme Questions asked Prior to Medical Ent. Exams. 2005
37. Telomerase is an enzyme which is a 43, The four elements that make up 96% of all the
0 (Prelims)-2005] elements found in a living system are
(1) RepettiveDNA ) RNA (1) C.H OandP 2) C,N.Qand P
@ si protein @ toin (3) H, H,O,Cand N 4)
(4] C,H H, OandS
44 cholesterol patients advisedto
38. Which of the following is the simplest amino acid? High chole pat i ae use
0 (Prelims)-2005] (1) Ghee, butter and oils
R (2) Groundnut oil, margarine and vegetable oils
@ ‘ (3) Fatty oil and butter
Asparagine
@ G (4) Cheese, dalda and ghee
@) Aani 45. Essential amino acid is
ine
(1) Phenylalanine
39. Enzymes, vitamins and hormones can be classified v
into a single category of biological chemicals, (@) Giycine
because all of these [AIPMT (Prelims)-2005] (3) Aspartic acid
(1) Enhance oxidative metabolism (4) Serine
(2) Are conjugated proteins 46. Lipids are insoluble in water because lipid
(3) Are exclusively synthesized in the body of a molacules e
living organism as at present (1) Hydrophilic (2) Hydrophobic
(4) Help in regulating metabolism (3) Neutral (4) Zwitter ions
1 - 1.1 |11 R
47. The major role of minor elements inside living 54. Which of the following is the diagrammatic
organisms is to act as representation
of phospholipid lecithin?
(1) Co-factors of enzymes . o
(2) Building blocks of important amino acids CH,-0- é_ R,
(3) Consttuents of hormones | i
{4) Binders of cell structure m TH—O—O-R.
48. Nucleotides are building blocks of nucleic acids. L N
CH,-O-P-0- —CH, —NH;
Each nucleolide
is a composite molecule formed by ‘ 6H CH—CH-NH,
(1) Base-sugar-phosphate .
(2) Base-sugar-OH fi
@) (Base-sugar-phosphate), ‘l’“*‘ 0-&-Ri
() Sugar-phosphate @ CH-0-8-R,
49. About 98 percent of the mass of every living T o
organism is composed of just six elements CH,—O—!‘.—R,
including carbon, hydrogen, nitrogen, oxygen and i
(1) Sulphur and magnesium i’
(2) Magnesium and sodium H, '0'0 -R
(3) Calcium and phosphorus @) H—O-!!—E
(4) Phosphorus and sulphur ‘I:l, ?H,
50. Which of the following
is a neutral amino acid? CH,—O0-P-0-CH,-CH,“N-CH,
(1) Glutamine (2) Arginine (BH J:H,
(3) Valine (4) Asparagine = o
51. The most unsaturated
fatty acid is CH,—O—{':—R'
(1) Linoleic acid i‘ L
(2) Oleic acid @) R-C-0- |H o
(3) Linolenic acid CH,—O-H—DH
{4) Arachidonic acid i
52. Which of the following is a nucleotide? 55. Which of the following is not a secondary
(1) Thymidine metabolite of plant cell?
(2) Cylosine (1) Rubber (2) Chiorophyll
(@) Thiamine (3) Essential oi ) Tannins
(4) Uridylic acid 56. The most abundant molecule in cell is
53. Which of the following is incomrect regarding the 1) Wal Carbohydrate
amino acids and their functions? (1) Water @
. f . (3) Lipid (4) Protein
(1) Tyrosine : Converted into epinephrine . .
hormone and used in the 57 Which are the most diverse molecules in the cell?
synthesis of melanin pigment (1) Lipids (2) Mineral salts
(2) Glycine : Involved in the formationof heme (@) Proteins 4) Carbohydrates
(3) Tryptophan : Helps in the synthesis of auxin 58. The nt organic compound on is
hormone
() Histdine : Can be converted info histamine (1) Protein @ Celulose
Iby the removal of amino group (3) Lipids (4) Steroids
59. Haemoglobin is a type of 67. Which of the following is a reducing sugar?

(1) Carbohydrate (2) Respiratory pigment (1) Galactose
(3) Vitamin (4) Skin pigment (2) Gluconic acid
60. Collagen is (3) p-methyl galactoside
(1) Fibrous protein (2) Globular protein (4) Sucrose
(3) Lipd (4) Carbohydrate 68. Animportant step in the manufacture of pulp for paper
61. Maltose is formed of two molecules of indusiry s the
) F @ se (1) Preparation
of pure cellulose
(2) Treatment of wood with chemicals that break
(3) Glucose (4) Sucrose cellulose
62 A polysaccharide which is synthesized and stored
in 'I)':ercelsi: © ands (3) Removal of oils present in the wood by
) treatment with suitable chemicals
m @ aen (4) Removal
of water from the wood by prolonged
(3) Lactose (4) Galactose heating at approximately 50°C
63. Agar is commercially obtained from 69. [1-4 linkages are present in
(1) Red algae (1) Cellulose
(2) Blue-green algas (2) Chitin
(3) Brown algae (3) Starch
{4) Green algae (4) Both (1) & (2)
64. Which of the following groups consists of 70, Which of the following statements is false?
polysaccharides only? (1) Cellulose is the most abundant organic
(1) Sucrose, glucose and fructose compound in the biosphere
(2) Maltose, lactose and fructose (2) Celluloseis an unbranched polymer with
(3) Glycogen, sucrose and maltose £-1.4 glycosidic bonds
{4) Glycogen, cellulose and starch (3) Rayon and cellophane are chemically similar to
cellulose xanthate
65. Lactose i posed of
ose 1= com (4) Cellulose can be digested by the herbivoresby
(1) Glucose + galactose p-amylase, produced by the glandular cells of
(2) Fructose + galactose their alimentary canal
(3) Glucose + fructose 71, If the total amount of adenine and thymine in a
G double-stranded DNA is 60%, the amount of
() Glucose + glucose guanine in this DNA will be
66. Cellulose, the most important constituent of plant 1) 15% 2) 20%
cell wall is made up of ()3]% e o
3 [4) 40
(1) Branched chain of glucose molecules linked by @ “ ) ‘
a1, 4 glycosidic bond in straight chain and 72, DNA has equal number of adenine and thymine
«1, 6 glycosidic bond
at the site of branching residues
(A = T) and equal number of guanine
and
) cytosine (G = C). These relationships are known
(2) Unbranched chain of glucose molecules linked as
by fi1, 4 glycosidic bond
{3) Branched chain of glucose molecules inked by o1) Chargaff's
‘ rule
a1, 6 glycosidic bond at the site of branching law
(2) Coulomb's
(4) Unbranched chain of glucose molecules linked (3) Le Chatelier's principle
by a1, 4 glycosidic bond {4) Van't Hoff plot
73. Which of the following pairs of nitrogenous bases ~ 81. The role of an enzyme in a reaction is to/as
of nucleic acids is mismatched with the category 1) Decrease activation energ
mentioned against it? o B "
(2) Increase activation energy
(1) Adenine, Thymine - Purines
) (3) Inorganic catalyst
(2) Thymine, Uracil — Pyrimidines
. N . (4) None of these
(3) Uracil, Cytosine — Pynmidines
82. Which of the following factor(s) do(es) not affect
() Guanine, Adenine — Purines enzyme activity?
74. In a DNA molecule A Temperature
(1) There are two strands which run antiparallel- B. pH
one in 5" — 3’ direction and other in 3" — 5
. y C. Enzyme concentration
(2) The total amount of purine nucleotides and )
pyrimidine nucleotides is not always equal D. Product concentration
{3) There are two strands which run parallel
in the i
§ — 3’ direction F. Activation energy
(4) The proportion of adenine in relation to thymine (1) Conly
varies with the organism @ c&D
75. Which pI.I'I'Ie base is found in W? (3) Donly
(1} Thyine @) Ureci @) Fonly

(3) Cytosine (4) Guanine 83. A competitive inhibitor of succinic dehydrogenase
76. Similarity in DNA and RNA is that is
(1) Both are polymers of nucleotides (1) Malate (2) Malonate
(2) Both have similar pyrimidines (3) Oxaloacetate (4) Both (2)& (3)
(3) Both have similar sugar 84. Which of the following is a typical example of
(4) Both are genetic material in man fleedback inhibition'?
77. Length of one loop of B-DNA is (1) Cyanide and cytochrome reaction
(1) 34nm (2) 0.34 nm (2) Sulpha drugs and folic acid synthesizer
bacteria
(3) 20 nm (4) 10 nm
. . . o (3) Allosteric inhibition of hexokinase by glucose
78. Which of the following enzymesis used
to join bits 6-phosphate
of DNA?
. (4) Reaction between succinic dehydrogenase and
(1) Ligase @) Primase succinic acid
() DNA polymerase (4) Endanuclease 8. Which factor is responsible for inhibition of
79. The 3'-5° phosphodiester linkages inside a enzymatic process
during feedback?
polynucleotide chain serve to join (1) Substrate (2) Enzyme
(1) One DNA strand with the other DNA strand (3) End product (4) Temperature
(2) One nucleoside with another nucleoside 86. Which of the following is true for competitive
(3) One nuclectide with another nucleotide enzyme inhibition?
(4) One nitrogenous base with pentose sugar (1) Decrease in V,,, and K
80. ATPis (2) Unchanged V, _ and decrease in K
(1) Nucleotide @) Nucleoside (3) Unchanged V, and increase in K,_
(3) Nucleic acid (4) Vitamin (4) Increase in V,,, and K,
87. The Michaelis constant K _ is 2. Which of the following is not a function of
(1) Numerically equal to % V.__, polysaccharides?
(2) Dependent on the enzyme concentration (1) Energy source
(3) Numerically equal to the substrate (2) Energy storage
concentration that gives half maximal velocity (3) Structural support
@) In.(‘zi::ed in the presence of non-competitive (4) Storage of genetic information
- 3. Which of the following statement is false?

88. If an enzyme has been given the EC code 5.2.1.7,
itis likely to be involved in (1) Glycogen and cellulose both are
homopolymers of glucos
(1) Digestion (2) Redox reaction kansend
(2) The amino group identifies the specific amino
(3) Isomerization (4) Molecular breakdown acid and determines its shape
89. Prosthetic group is a part of holoenzyme. It is @) Indinisa of fru
(1) Loosely attached organic part @) A protein is a heteropolymer not a

(2) Loosely attached inorganic part homopolymer
(3) Non-protein organic part firmly atiached with 4. Haem is the prosthetic group and it is the part of
apoenzyme the active site of which of the following enzymes?
{4) None
of these (1) Pepsin and trypsin
90. Which of the following has carbohydrate as (2) Carboxypeptidase
and aminopeptidase
prosthetic group? Perard d
(1) Glycoprotein (2) Chromoprotein @) Peraxidasa end catalass
@ Li in @ N _ (4) Amylase and maltase
91. Mark the mismatched pair 6 e the class

cf orzyms iniohied i e iclowing
(1) Cellulose : Unbranched polymer with Xy
f.,1-4 glycosidic linkage 1
(2) Cellophane : Cellulose xanthate C-C—> X-Y +C=C.
(3) Carboxypeptidase : Exopeptidase, Mg acts They catalyse removal of groups from subslrates
as a co-factor by mechanism other than hydrolysis leaving double
(4) Aminopeptidase : Exopeptidase, cleaves )

the peptide bond at (1) Oxidoreductases (2) Transferases
N-terminal end (3) Hydrolases (@) Lyases
92. Apoenzyme is 6. False statement about the coenzyme NAD and

(1) Always
a protein NADP is that they
(2) Often a metal (1) Contain the vitamin niacin
(3) Always an inorganic compound (2) Act as coenzymes of oxidising enzymes
(4) Often a vitamin (3) Participate in the formation of nucleic acid
(4) Contain adenine, phosphate and ribose sugar
SECTION -D 7. Food proteins should include sufficient amounts of
animal proteins such as milk, egg, fish and meat
NEET Booster Questions proteins, because they are nuiritionally superior
1. Coenzyme is and rich in
(1) Always a protein (1) Al the twenty amino acids
(2) Often a metal (2) All essential amino acids
(3) Always an inorganic compound (3) Aromatic amino acids
(4) Often a vitamin (4) Polypeptides
8. Select the option which is not correct with respect 14. Identify the organic compound illustrated and its
1o enzyme action. component ‘X'
(1) Inhibition of succinic dehydrogenase by . o
malonate can be reversed by addition of lot of Il
succinate HO—PI —OCH, b’
(2) In non-competitive inhibition substrate does not OH
bind with substrate binding site but binds at
some other site of enzyme
(3) Sulpha drugs are competitive inhibitors of folic
acid synthesis in bacteria, they substitute for (1) Undine : Uracil
p-amino benzoic acid (@) Nucleoside : Adenosine
(4) Cyanide kills an animal by inhibiting cytochrome (3) Adenylic acid . Adenine
oxidase, its effect can be overcome by B ~
increasing substrate concentration (4) Amino acid © NH,
9. Complete the following analogy 15. Select the incorrect statement.
RNA - uracil :: DNA 1) Ce_llagen is the most abundant protein in
1 Guark animal world
M (2) RuBisCO is the most abundant protein in the
(2) Thymine whole of biosphere
(3) Adenine (3) Ribozymes are nucleic acids with catalytic
@) Cytosine property
10. Within organism, which nitrogenous bases @) Adul!"hamoglnhm has tertiary structure of
are found in similar percentage? 16 Cont . i s

3 it ucleic acids i I i
(1) AandT,GandC (2) Aand C,Gand T e
(1) 15-20% 2) 10-15%
(3) AandC,GandU (4) Aand G Tand U
1. catalysed reaction, refers to
N The effect
e of enend product
uct on on thethe rate
ral of enzyme & ’ 57of th folowing
17, Which . @ 2o melabolies
secondary " are
(1) Feedback inhib¥or (1) Morphine, Codeine (2) Abrin, Ricin

(2) Competitive '"hi’,m,", ) ) (3) Concar A @) Vi in, Cu .
@) Non-competitive inhibition (smeversible) 18, Identify the molecules (A) and (B) illustrated below,
(4) Lock and key mechanism along with their reducing ends.
12. Plant proteins like those of pulses are deficient in " CHOH
i of the followit
which lowing amino
ino acids’
acids? " " . ] "
(1) Lysine and tryptophan
(2) Cysteine and methionine OH oH
(3) Alanine and glycine
(4) Tyrosine and tryptophan OH OH
13. Which of the following statement is false? (A) B)
(1) Wax is a simple lipid (5] ()
(2) Arachidonic acid has 20 carbon atoms (1) Galactose, rightend Ribose, right end
excluding the carboxyl carbon (2) Glucose, right end Ribose, right end
(3) Gingelly oil has lower melting point hence (3) Glucose, left end Ribose, left end
remains as oflin winter (4) Mannose, right end Deoxyribose right
(4) CH,;~CH,),,~COOH, is palmitic fatty acid end
19. Which of the following are correct set of o

nucleosides? Il
(c) O—p—0
(1) Cytidylic acid, Uridylic acid |
(2) Uridine, Cytosine ©
) ) (@) HO-CH—CH,—N._
(3) Thymidine, Uridine CH/I 'CH,
(4) Uridylic acid, Thymidyiic acid " CH,
20. Which of the following is a storage protein? (1) (a). (b) and (c)
(1) Collagen (2) (a)and (b)
@) Starch (3) (a). (b), (c) and (d)
@) Glutetn @) (o) and (d)
) Keratin A bt i
23. Which of the following is correct identification of
21. The structure of uracil is given below. molecules illustrated below?
. ° i o
Il
HN; H ‘I? ?H,—O—D— R,
A Fh-C*U—?H (fi
X CH,—Ofli-’—D —CH,—C:-'.
H OH Mgy
To which of the following will uracil have to bind ’ (‘:H
(directly or indirectly) to form a RNA nucleotide? . :
fi 'HO—CH, OH
() o—p—0 (b) B
& § '
OH
. HO'
NH, . :
N HO—CH, H T'
© Os @ R
H
N H ?H'
(I.‘vH.
(1) (b} and (c)
CH,
(2) (a) and (b) |
@) (c)and (d) Gt
4) (a)and (d) NH,
22, Which of the following are required for the formation D. CH,—CH,),—COOH
of o molss? I TS N O T
(@ CH{CH,),,-COOH 1 N I (e R
oH-on @ [frgeerie fcrmesaralvaine_[swmrc_|
oo |
Ie s Phospholipid |Cholesterol | Lysine | Stearic
CH~OH lecithin fatty acid
Aakash Educational Services Limited - Regd. Office : Aakash Tower, 8, Pusa Road, New Delhi-110005 Ph.011-47623456
24, Which of the following statements is false? 28. The given structure represents a monosaccharide
(1) K, is a measure of the affinity of the enzyme known as
for its substrate .
(2) K, value of the protease enzyme will vary with HOCH.
the type of protein
(3) K, value represents concentration of substrate M H
at which half the maximum velocity of the
enzyme reaction is attained H
4) K is increased in the presence of a non-
compelitive inhibitor (1) Ribose (2) Glucose
25. The skin pigment melanin is synthesized from
which of the following amino acids? (3 Fructose 4) Rafinces
(1) Glycine (2) Tyrosine 29. Chitin present in the exoskeletons of arthropods is
(3) Tryptophan (4) Alanine (1) Protein

26. Primary structure of a portion of a hypothetical (2) Polysaccharide
protein is given with labelled parts as A, B, C and @ Lipid
D. Choose the false option.
(4) Derived monosaccharide
- oH 30. One of the following is correct sequence of
COOH carbohydrales in the order of increasing complexity
| of chemical structure
SH CH,
| | (1) Sucrose, starch, oligosaccharide, maltose,
[ S
~HN-CH-CO-NH-CH-CO-NH-CH-CO-NH-CH-CO-
o .
(@) Triose, maltose, sucrose, oligosaccharide,
A B c D starch
(1) A is an alcoholic amino acid — Serine. The (3) Triose, glucose, maltose, oligosaccharide,
three lelter abbreviation is Ser and single letter starch
code is § (4) Oligosaccharide, triose, starch, sucrose,
(2) B is sulphur containing amino acid — Cysteine. maltose
The three letter abbreviation
is Cys and single 44 Glucose is stored as glycogen in
letter code is C
(3) C is aromatic amino ackd — Tyrosine. The three (1) Pancreas @) Bone
letter abbreviation is Tyr and single letter code (3) Kidney 4) Liver
is ¥ 32. A cellulose molecule is formed by the
(4) D is acidic amino acid — Glutamate. The three polymerisation of glucose. The number of glucose
!amec abbreviation is Glu and single letter code molecules present in a cellulose is
=G ) @
27. | ltose,
" metess, ghee °
glycosidic bond is formed betwee
" ®) 60000 @) 60
(1) Carbon 1 of one glucose molecule and carbon .
4 of second glucose molecule 33. The structure of protein which gives a three
dimensional view is
(2) Carbon 2 of one glucose molecule and carbon ‘
3 of second glucose molecule (1) Primary structure
(3) Carbon 3 of one glucose molecule and carbon (2) a-helix
4 of second glucose molecule (3) P-pleated sheet
(4) Carbon 1 of one glucose molecule and carbon
6 of second glucose molecule (4) Tertiary structure
34. The product of the given reaction would be a 41. In DNA, cytosine
pairs with
‘CH.OH (1) Guanine
, HOOC-R, .
éHOH 4+ HOOC-R, —* e (? M’ ‘m
CH,OH HOOC-R, @ Adarine
Glycerol Fatty acid ) Urscl
42, The given amino acid is in nature
(1) Monoglyceride (2) Diglyceride i
(3) Triglyceride (4) Both (1) & (3)
H,N—(l)—H
35. The given fatty acid is known as |
CH,.COOH
CH,(CH,), CH = CH (CH,), COOH
(1) Paimitic acid (1) Acidic
(2) Oleic acid (2) Basic
(3) Stearic acid (3) Neutral
(4) Arachidonic acid (4) Aromatic
36. Nucleic acids, as described by Watson and Crick ~ 43. Which of the following are basic amino acids?
exhibit (1) Glycine and Alanine
(1) Secondary structure (2) Lysine and Arginine
(2) Tertiary structure (3) Glutamic acid and Aspartic acid
(3) Quatemnary structure (4) Histidine and Proline
(4) Both
(2) & (3) 44, Which of the following aminoacids
is involved in the
37. The backbone of a DNA molecule is made up of formation
of Heme?
(1) Adenine and guanine (1) Tryptophan () Tyrosine
(2) Sugar-phosphate-sugar chain (3) Glycine (4) Histidine
(3) Cylosine and thymine 45, mfl one of the following is alcoholic amino acid
@) All of tese (1) Tyrosine and serine

3B. If the sequence of bases in one of the DNA strand .
is AG GAG AA, then the sequence of bases in (2) Thweonine and serine
the other complementary strand of DNA would be (3) Phenylalanine and tyrosine
(1) CCTTCTT () TCTCTCC (4) Tryptophan
and phenylalanine
@ TCCTCTT 4 CCTCTCT 46. Lysine is an essential amino acid because
39. RNA is a polymerof (1) Rtis very rare
(1) Ribonucleotides (2) It has a high nutritive value
(2) Deoxyribonucleotides (3) Itis an important constituent of all proteins
(3) Deoxyribonucleosides (4) It is not formed in the body and has to be
@) Ri provided through diet
40. +RNA constitutes about 47. In which of the following
energy is released?
(1) 70-80% of the total RNA (1) Conversion
of glucose into pyruvate
(2) 15% of the total RNA (2) Formation of proteins from amino acids
(3) 5% of the total RNA (3) Conversion
of glucose into lactic acid
(4) 1-3% of the total RNA (4) Both (1) & (3)
48. Adenosine Triphosphate (ATP) liberates high energy ~ 54. Match column A with column B
by the breakdown of Column A Column B
(1) Glycosidic bond a. Glucose () Ninhydrin test
12) Hydrogen bond b. Castorol (i) Red coloration on
(3) Phosphate bond adding Millon's
(4) Both
(1) & (3)
49. Which of the following stalements is correct? ¢ Amino acids Aabivi-Raiy it
(1) Biocatalysts accelerate the rate of a given solution
metabolic reaction d. Proteins (W) Brick red precipitate
(2) Biocatalysts are generally proteins on heating with
(3) Enzyme catalyst differs from inorganic catalyst Fehling's solution
@) All of these QmsethIW. ) )
50. Which of the following statements is incorrect (1) o), bW, o). 41} ) afl) bO). cli), o)
w.r.t. inorganic catalysts? (3) afi). biiv). cfii), d(i) (4) ali). b{i), cfiii), d(iv)
(1) They do not occur in living cells 55. bsu_;.e_ catalyses covalent bonding of two
sul s.
They are not specific for reaction
Ei The:getd fa magedmhig:r:m tur re o
per (2) Amylase
{4) They work efficiently at high pressure (3) Glutamate pyruvate transaminase
51. Enzymes catalyse biochemical reactions by @) PEP xylase
1) Lowering the activation energ
” i -n Y 56. The enzyme that catalyses the conversion of
(2) Increasing the activation energy glucose-6-phosphate into fructose-6-phosphate is
(3) Establishing stable bonds with substrate (1) Aligase
(4) Increasing temperature (2) An isomerase
52. Read the following : (3) Alyase
(a) Low temperature preserves the enzyme (4) Ahydrolase
(b) Enzyme activity increases above optimum 57. Study the following statements :
temperaiure (a) The substrate binds to the active site of the
(c) Enzyme gets denatured at high temperature enzyme.
(d) Competitive inhibitor competes with the product (b) Enzymes isolated from thermophilic organisms
formed get denatured at 50°C.
Which of the following statement are true? (c) The active site of enzyme breaks the chemical
bonds of the product
(1) @ &) @ ()& .
(d) Prosthetic groups are tightly bound to the
@) ()& (@) (4) (a) & (b) apoenzyme.
53. Enzymes catalysing the breakdown of larger Select the option which includes all correct
molecules into smaller molecules are statements :
(1) Hydrolases (1) (@)& (c)
(2) Isomerases 2) (c) & (d)
@) Ligase (3) (b)& (c)
(4) Both
(1) & (3) (4) (a)&(a)
58. All enzymes are proteins except (3) Inhibiting cytochrome oxidase, a mitochondrial
(1) Trypsin enzyme essential for cellular respiration by
@) Pepsi Non-competitive inhibition
'epsin
B (4) Killing the cells of cardiac muscles
@ " €0. Electron iandemn enzymes belong to
(4) Ribozyme and Ribonuclease-P ' 9
59. Cyanide kills an animal by m T@
(1) Kiling the brain cells @) Oridoreductases
(2) Competitive inhibitor of enzyme cytochrome ©) Lyases
oxidise (4) Isomerases
m .

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Chapter 2

The most abundant element in celllliving matter is oxygen.

Hydrogen (H) 014 05

Polysaccharides %im Nucleic acid

Table : Average composition of cells

Note: Water is the mast abundant chemical in living organisms.

PRIMARY AND SECONDARY METABOLITES

Table : Some secondary metabolites

Example - Ribose, glucose, fructose efc.

« Sugar alcohol : e.g. mannitol (present in brown algae)

M Gucoss Maltose " Glucoss H

‘ SfHOH .iu,on H,OH

Fig. : Structural formulae of common disaccharides

Fig. : Diagrammatic representation of a portion of glycogen

(e) Cellulose (Hexosan polysaccharide) : Cellulose is an unbranched homopolysaccharide of f-glucose

Fig. : Cartoon showing : Secondary structure (a-helix) of protein

(c) Tertiary structure

Collagen |Intercellular ground substance

Simple lipids Cqmpound or Dar_M;d

Neutral or Waxes Cutin

Phospholipids ~ Glycolipids Lipoproteins ~ Chromolipids

Fatty acids are of two types :

(i) A phosphate group :

Nitrogenous | Nucleoside | Nucleotide

Fig. : Diagram indicating secondary structure of DNA

Watson-Crick Model of DNA

11. Which of the following amino acid is basic in nature?

DYNAMIC STATE OF BODY CONSTITUENTS - CONCEPT OF METABOLISM

THE LIVING STATE

How do enzymes bring about such high rates of chemical conversions?

g Activation energy with enzyme

Nature of Enzyme Action

Factors Affecting Enzyme Activity

(i) Hydrogen ion concentration (pH)

(iii) Concentration of substrate

* K (Michaelis constant) is a mathematical derivation or constant which indicales the substrale

(a) Buttressing group is meant for supporting the substrate.

Inhibition of Enzyme Activity

1. EffectonV,,, : The effect of a competitive inhibitor is reversed by increasing [S].

) 1‘ Malonic acid (competitive inhibitor)

Succinic Succinic acid Active centre Substrate

Classification and Nomenclature of Enzymes

Three types of co-factors are identified :

Fe™, Fe™ Cytochrome oxidase, catalase, aconitase, peroxidase

Ca* Lipase, Succinic dehydrogenase

Mg™ Hexokinase, pyruvate kinase, DNA polymerase, enolase, phosphotransferase

Zn** Alcohol dehydrogenase, Carbonic anhydrase, LDH, carboxypeptidase

(4) Ribozyme was discovered by Altman et al.

22, Study the reaction given below

€O, +H,0—2™ 1,co,

(2) Sulpha drugs used to control bacterial pathogens

() Znc (2) Copper

(1) High temperature @

(4) First increases then decreases

B 6. Dehydration synthesis during peptide bond

c. Inuini ii Branched polymer

(4) Concanavalin A is a lectin which is

molecules [NCERT Pg. 144]