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Biomolecule (Da) approximately. Micromolecules have

molecular weight less than 1000 Da.
Introduction b) Acid insoluble pool
The acid insoluble fraction,
 The living organisms are made of different
has only four types of organic compounds i.e.,
types of compound  Proteins,
 The chemical analysis reveals that it is  Nucleic acids,
composed of elements like C,H,O,  Polysaccharides and
 A piece of non living matter also contains  Lipids.
same type of elements  But the molecular weights of lipids do not
 In fact the living things and non living things exceed 800 Da, come under acid insoluble
fraction. Because Cell membrane and other
are made up of same elements
membranes are broken into pieces during
 However the relative abundance of Carbon, the experiment , and form vesicles which are
hydrogen is higher in the living organism not water soluble. Therefore, these
than in non living matter membrane fragments in the form of vesicles
get separated along with the acid insoluble
pool and hence in the macromolecular
fraction.Therefore lipids are not strictly
macromolecule.
 The acid insoluble fraction has molecular
weight greater than 10000 Da.

Analysis of inorganic elements and compounds

in the living tissue
All the carbon compounds that we
How to analyze chemicalcomposition?
get from living tissues can be called
Analysis of Organic elements and compounds in ‘biomolecules’. However,living organisms have
the living tissue also got inorganic elements and compounds in
them. A slightly different but destructive
 Take any living tissue (a vegetable or a piece experiment has to be done. One weighs a small
of liver, etc.) and grind it in Trichloroacetic amount of a living tissue (say a leaf or liver and
acid (Cl3CCOOH) using a mortar and a pestle. this is called wet weight) and dry it. All the
 We obtain a thick slurry. water,evaporates. The remaining material gives
 If we were to strain this through a cheese dry weight. Now if the tissue is fully burnt, all the
cloth or cotton we would obtain two carbon compounds are oxidised to gaseous form
fractions. (CO2, water vapour) and are removed. What is
a)The filtrate or, the acid-soluble pool remaining is called ‘ash’. This ash contains in
(micromolecule/biomolecule ), organic elements (like calcium, magnesium
b) The retentate or the acid-insoluble fraction etc). Inorganic compounds like sulphate,
(Biomacromolecule ). phosphate, etc., are also seen in the acid-
soluble fraction.
a)Acid soluble pool
Scientistshave found thousands of organic
compounds in the acid-soluble pool. There is one
feature common to all those compounds found in
the acidsoluble pool. They have molecular
weights ranging from 18 to around 800 daltons
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 Another feature of these metabolic reactions
is that every chemical reaction is a catalysed
reactions and it is catalysed by enzymes.
Eg: 1. In Glycolysis, glucose becomes Pyruvic
acid through ten different enzymes catalysed
metabolic reactions. But under normal
aerobic condtions pyruvic acid is formed.
Eg :2 .In yeast, during fermentation, the same
pathway leads to the production of ethanol
(Alcohol)
The acid soluble pool represents roughly
Eg: 3.In our skeletal muscle, under anaerobic
the cytoplasmic composition. The
condtions, lactic acid is formed
macromolecules from cytoplasm and organelles
become the acid insoluble fraction. Together
they represent the entire chemical composition
of living tissues or organism. Primary and secondary metabolites
 Metabolites are organic compounds
constantly utilzed in various metabolic
Biomolecules, i.e., chemical compounds found in activities in the cells.
living organisms are of two types. One, those  There are two types of metabolites
which have molecular weights less than one a)Primary metabolites:
thousand dalton and are usually referred to as  It is essential to the growth of the cell.
micromolecules or simply biomolecules while  Primary metabolites have identifiable
those which are found in the acid insoluble functions and play known roles in normal
fraction are called macromolecules or physiologial processes
biomacromolecules.  They are produced continuously during the
growth phase and are involved in primary
metabolic processes
Eg: proteins, nucleic acids, and
polysaccharides
b)Secondary metabolites:
 They are the compounds which are derived
by pathways from primary metabolic routs,
and are not essential to sustain the life of
cells.
 These compounds do not have a continuous
production
 Secondary metabolites are the end products
of primary metabolites such as alkaloids,
toxins, steroids, essential oils, lectins, drugs
Metabolism etc
 The sum total of all chemical reactions taking  Many of secondary metabolites are useful
place in aliving organism is called metabolism to ‘human welfare’ (e.g., rubber, drugs,
spices, scents and pigments).
 Majority of these metabolic reactions are
 Some secondary metabolites have
always linked to some other reactions. This
ecological importance
series of linked reactions is called metabolic
pathways (So a multistep chemical reactions,
when each of the step is catalysed by the
same enzyme complex or different enzyme is
called a metabolic pathway.)
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Difference between primary metabolites

and secondary metabolites
Primary metabolites Secondary metabolites
They are involved in They are not directly
normal growth involved in growth
,development and development and
reproduction reproduction
Examples include Amino Examples included
acids,sugars.. pigments,alkaloids…
Essential to sustain life of not essential to
organism sustain the life of cells.
They are produced These compounds do
continuously during not have a continuous
the growth phase production
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
1. AMINO ACIDS
Amino acids are building blocks of
Classification of amino acids
a) Based on number of amino and carboxyl
proteins.
groups, amino acids are classified into
 Amino acids are organic compounds i)Acidic amino acids
containing an amino group an acidic group Eg:Glutamic acid, Aspartic acid
as substituents on the same carbon i.e., the
αcarbon. Hence, they are called α-amino
acids. They are substituted methanes.
 There are four substituent groups
occupying the four valency positions.
Theseare hydrogen, carboxyl group,
amino group and a variable group
designated as R group. ii)Basic amino acids Eg: Lysine
iii)Neutral aminoacids:Eg: Valine
 There are aromatic amino acids
Eg: Tyrosine, Phenylalanine, Tryptophan

 Based on the nature of R group there are  Sulphur containing amino acid
many amino acids. However, those which Eg:Cysteine
occur in proteins are only of twenty types.

b)Based on the need to the human body ,

Amino acids are also classified into
a)Essential amino acids
b)Non essentialamino acids
a)Essential amino acids
The amino acids that cannot be
synthesized in our body and it should be
provided through food is called essential amino
acids
b)Non essentialamino acids
The amino acids that can be synthesized
in our body and no need to be supplied
through food is called non essential amino
acids
ZWITTER ION
A particular property of amino acids
is the ionizable nature of –NH2 and –COOH
groups. Hence in solutions of different pHs,
the structure of amino acids changes.At a
particular pH (Isoelctric point) of solution,
amino acids occur as a dipolar ions with +ve

SOHSS-AREEKODE/2023 [email protected]
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and –ve charge in the same molecule. They are  The first amino acid is also called as N-
called Zwitter ions terminal amino acid. The last amino acid is
called the C-terminal
terminal amino acid.
 The primary structure of protein gives the
positional information of amino acids in a
protein.
2. PROTEINS
 Proteins are polypeptides formed of
number of amino acidss linked together by
means of Peptide bond.
b)Secondary structure of protein
 Each protein is a polymer of amino acids
 If the polypeptide is coiled to form of a helix
 Peptide bond is formedmed is formed when
(similar to a revolving staircase) the
the carboxyl (-COOH)COOH) group of one
structure is called secondary structure of
amino acid reacts with the amino (-NH2)
(
protein.
group of the next amino acid with the
 In proteins, only right handed helices are
elimination of a water (the process is
observed.
called dehydration)
c)Tertiary structure of protein
 Proteins are formed of number of different
 If protein chain is also folded upon itself
kinds amino acids and hence proteins are
like a hollowwoolen ball, giving rise to the
called heteropolymers.
tertiary structure. 3-dimensional
dimensional view of a
protein.
 Tertiary structure is absolutely
necessary for the many biological
activities of proteins.
d)Quaternary structure
If proteins are formed of more than one
polypeptide chain or subunits
ubunits The manner in
which these individual folded polypeptides or
subunits are arranged with respect to each
other (e.g. linear string ofspheres, spheres
arranged one upon each other in the form of a
cube or plate etc.) is the architecture of a
protein otherwise
therwise called the quaternary
structure of a protein.
Eg: adult Haemoglobin consist of 4 subunits.
 Collagen is the most abundant protein in
It consist of 2α and 2β chain.
animal world
 Ribulosebisphosphate Carboxylase-
Carboxylase
Oxygenase (RuBisCO) is the most
abundant protein in the whole of the
biosphere

 Biologists describe the protein structure at four

levels
a)Primary structure of proteins
 Here the amino acidss are arranged in a line .
 If a protein is imagined as a line, the left end
represented by the first amino acid and the
right end represented by the last amino acid.
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b)Glycerol
 Another simple lipid is glycerol which is
trihydroxy propane

c)Triglycerides (Fats and Oils)

Manylipids have both glycerol and fatty
acids. Here the fatty acids are found esterified
with glycerol. They can be

i)Monoglycerides=
onoglycerides= 1 Fatty acids+ 1 Glycerol
ii)Diglycerides=
iglycerides= 2 fatty acids+ 1glycerol
cerides=3 fatty acids+1 gl
iii)Triglecerides=3 glycyerol

3. LIPIDS
 Lipids are water Insoluble
 They could be simple fatty acids, Glycerol,and
may have both glycerol and fatty acids
a)Fatty acids.
A fatty acid has a carboxyl group attached
to an R group.

 These are also called fats and oils based on

The R group could be a methyl ((–CH3), or melting point.
ethyl (–C2H5) or higher number of –CH2
CH2 groups  Oils have lower melting point (e.g., gingely
(1 carbon to 19 carbons). oil) and hence remain asoil in winters.
winters
For example  Fats have high melting point and occur in
(a)Palmiticacid : solid form in room temperature.
It has 16 carbons including carboxyl
carbon.  Some lipids have phosphorous and a
phosphorylated organic compound in them.
Theseare phospholipids.. They are found in
(b)Arachidonicacid:
cell membrane.
atoms including the carboxyl
It has 20 carbonatoms
Eg: Lecithin
carbon.
 Fatty acids could be
i) Saturated-it is without double bond
ii) Unsaturated-It is with one or more
C=C double bonds).
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4. Polysaccharide 5. Nucleic acids
 Acid insoluble macromolecule  Nucleic acids are macro molecule and found
 Polysaccharides are long chains of sugars. in the acid insoluble part .
 They are threads containing different  Nucleic acids act as the genetic material in all
monosaccharides as building blocks. organisms.
 Nucleic acids are polynucleotides (Formed of
number of nucleotides)
 A nucleotide has three chemically distinct
components.
 A heterocyclic compound,
For example,  A monosaccharide
1)cellulose is a polymeric polysaccharide  A phosphoric acid or phosphate.
consisting of only one type of monosaccharide  The heterocyclic compounds in nucleic acids are
i.e., glucose. Cellulose is a homopolymer. Plant the nitrogenous bases named adenine, guanine,
cell walls are made of cellulose uracil, cytosine, and thymine. Adenine and
Guanine are substituted purines while the rest are
2)Starch is a variant of this butpresent as a store
substituted pyrimidines. The skeletal heterocyclic
house of energy in plant tissues. It is also a
ring is called as purine and pyrimidine
homopolymer of glucose. respectively.
3.Glycogen : Animals have another variant called  The sugar found in polynucleotides is either ribose
glycogen. It is also a homopolymer of glucose. (a monosaccharide pentose) or 2’ deoxyribose. A
4.Inulin is a polymer of fructose. nucleic acid containing deoxyribose is called
 In apolysaccharide chain (say glycogen), deoxyribonucleic acid (DNA) while that which
the right end is called the reducing end contains ribose is called ribonucleic acid (RNA)
and the left end is called the non-reducing  Nucleic acids are of two types DNA and RNA
end. DNA (Deoxy ribonucleic acid )
Starch forms helical secondary structures. starch  DNA is formed of two polynucleotides. Each
can hold I2 molecules in the helical portion. The poly nucleotides are formed of number of
starch-I2 is blue in colour. Cellulose does not nucleotides.
contain complex helices and hence cannot hold  A Single nucleotide is formed of nucleoside
I2. and phosphate.
Eg: Adenylic acid, thymidylic acid, guanylic
 There are more complex polysaccharides in acid, uridylic acid and cytidylic acid are
nature. They have as building blocks, amino- nucleotides
sugars and chemically modified sugars (e.g.,  A nucleoside formed of sugar and nitrogen
glucosamine, N-acetyl galactosamine, etc.). base
 Eg:Adenosine, guanosine, thymidine, uridine
6)Exoskeletons of arthropods have a complex and cytidine are nucleosides.
polysaccharide called chitin.It is a homopolymer  Sugar in DNA is deoxyribose and sugar in RNA
is ribose
 Nitrogen bases are heterocyclic compounds.It
is of two types, purines (Double rings ) and
Pyramidine (Single ring).
 Purines include Adenine, Guanine,
 Pyramidine include Uracil, Cytosine and
Thymine
 Nitrogen bases in DNA are Adenine,
guanine,thymine,Cytosine
 Nitrogen bases in RNA is Adenine, guanine,
uracil ,Cytosine
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 There are two hydrogen bonds between A  Each step of ascent is represented by a pair of
and T and three hydrogen bonds between G bases. At each step of ascent, the strand turns
and C. 36°.
 At each step of ascent, the strand turns  One full turn of the helical strand would
36°.One
One full turn of the helical strand would involve ten steps or ten base pairs. Attempt
involve ten steps or ten base pairs.. The pitch drawing a line diagram.
would be 34Å. The rise per base pair would be  The pitch would be 34Å. The rise per base pair
3.4Å.Å. This form of DNA with the above would be 3.4Å. This form of DNA with the
mentioned salient features is called B-DNA. above mentioned salient features is called
 In a nucleic acid a phosphate moiety links the BDNA.
3’-carbon
carbon of one sugar of one nucleotide to
the 5’-carbon
carbon of the sugar of the succeeding
nucleotide. The bond between the phosphat
phosphate
and hydroxyl group of sugar is an ester bond
bond.
As there is one such ester bond on either side,
it is called phosphodiester bond

Diagram indicating secondary structure of DNA

Watson crick Model of DNA

 This model says that DNA exists as a
double helix. The two strands of
polynucleotides are antiparallel i.e., run in
the opposite direction.
 The backbone is formed by the sugar
phosphate-sugar chain.
 The nitrogen bases are projected more or
less perpendicular to this backbone but
face inside.
 A and G of one strand compulsorily base
pairs with T and C, respectively, on the
other strand.
 There are two hydrogen bonds between A
and T and three hydrogen bonds between
G and C.
 Each strand appears like a helical staircase.
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Physical Process and Chemical Process 6. Enzymes
 Enzymes are biological catalyst capable of
Physical Reaction Chemical Reaction promoting biochemical reactions within a
A physical change when bonds are broken
living system.
simply refers to a and new bonds are
change in shape formed during
 Almost all enzymes are proteins.
without breaking of transformation, this will  But some nucleic acids behave like enzymes
bonds. be called a chemical are called Ribozymes (Non Protein enzyme)
reaction` Substrate : Substance upon which the enzyme
Example: ice melts into Example: act.
water, or when water Ba(OH)2 + H2SO4 → Active site : it is the substrate binding site of an
becomes a vapour BaSO4 + 2H2O enzyme
End product : the substance obtained at the end
Rate of a physical or chemical process of enzymatic reactions
 Rate of a physical or chemical process refers  Enzymes are damaged at high temperature
to the amount of product formed per unit (Above 40 c)
time. It can be expressed as  Some enzymes isolated from organism who
normally live under extreme high
temperature (like hot vents ) are stable and
retain their catalytic power even at high
 A general rule of thumb is that rate doubles temperature (80-90 c).
or decreases by half for every 10°C change in  Thermal stability is thus an important quality
either direction. of such enzymes isolated from thermophilic
 Catalysed reactions proceed at rates vastly organisms .
higher than that of uncatalysed ones.
 When enzyme catalysed reactions are Nature of Enzyme action
observed, the rate would be vastly higher Each enzyme (E) has a substrate (S)
than the same but uncatalysed reaction. binding site in its molecule so that ahighly
For example reactive enzyme-substrate complex (ES) is
produced. Thiscomplex is short-lived and
dissociates into its product(s) P.
The catalytic cycle of an enzyme
 In the absence of any enzyme this reaction is action can be described in the followingsteps:
very slow, with about 200 molecules of H2CO3 1. First, the substrate binds to the active site of
being formed in an hour. However, by using the enzyme, fitting into the active site.
the enzyme present within the cytoplasm 2. The binding of the substrate induces the
called carbonic anhydrase, the reaction enzyme to alter its shape,fitting more tightly
speeds dramatically with about 600,000 around the substrate.
molecules being formed every second. The 3. The active site of the enzyme, now in close
enzyme has accelerated the reaction rate by proximity of the substrate breaks the
about 10 million times. The power of enzymes chemical bonds of the substrate and thenew
is incredible indeed! enzyme- product complex is formed.
4. The enzyme releases the products of the
reaction and the free enzyme is ready to bind
to another molecule of the substrate andrun
through the catalytic cycle once again

 When substrate is bound to the enzyme active

site, a new structure of the substrate called
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transition state structure is formed. Very soon,  Enzymes eventually bring down this energy
after the expected bond breaking/making is barrier making the transition of ‘S’ to ‘P’ more
completed, the product is released from the easy.
active site

Factors affecting enzyme activity

Concept of activation energy The activity of an enzyme can be affected
by a change in the conditionswhich can alter
the tertiary structure of the protein.
 These include temperature, pH, change in
substrate concentration or binding of specific
chemicals that regulate its activity
a)Temperature and pH

 In the above graph the y-axis represents the

potential energy content.  Enzymes generally function in a narrow
 The x-axis represents the progression of the range of temperature and pH.
structural transformation or states through  Each enzyme shows its highest activity at a
the ‘transition state’. particulartemperature and pH called the
 Here we can see two things. The energy level optimum temperature and optimum pH.
difference between S and P.  Activity declines both below and above the
 If ‘P’ is at a lower level than ‘S’, the reaction optimum value.
is an exothermic reaction. One need not  Low temperature preserves the enzyme in a
supply energy (by heating) in order to form temporarily inactive state where as high
the product. However, whether it is an temperature destroys enzymatic activity
exothermic or spontaneous reaction or an because proteins are denatured by heat.
endothermic or energy requiring reaction, the b) Concentration of Substrate
‘S’ has to go through a much higher energy
state or transition state.
 The difference in average energy content of
‘S’ from that of this transition state is called
‘activation energy’
 Activation energy is defined as the minimum
amount of extra energy required by a
reacting molecule to get converted into
product.
 Enzymes perform a very important task by
lowering the activation energy of the reaction
(the energy put in for the reaction to begin).  With the increase in substrate concentration,
This lowering of energy allows the biological the velocity of the enzymatic reaction rises at
reaction to proceed very quickly at a very low first. The reaction ultimately reaches a
temperature which is bearable by living maximum velocity (Vmax) which is not
organisms.
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exceeded by any further rise in concentration 4.Lyases: Enzymes that catalyse removal of
of thesubstrate. groups from substrates by mechanisms other
 This is because the enzyme molecules are than hydrolysis leaving double bonds.
fewer than the substrate molecules and after
saturation of these molecules, there are no
free enzyme molecules to bind with the
additional substrate molecules
5.Isomerases: Includes all enzymes catalysing
inter-conversion of optical,geometric or
c) Enzyme Inhibition positional isomers.
The substance that shutoff the enzyme 6.Ligases: Enzymes catalysing the linking together
activities are called inhibitors and the process is of 2 compounds, e.g.,enzymes which catalyse
called enzyme inhibition. When the inhibitor joining of C-O, C-S, C-N, P-O etc. bonds.
closely resembles the substrate in its molecular
structure and inhibits the activity of the enzyme,
it is known as competitive inhibitor. Due to its Co-factors
close structural similarity with the substrate, the The protein Part of an enzyme is called
inhibitor competes with the substrate for the apoenzyme. The non protein part of enzyme is
substrate binding site of the enzyme (Active site). called cofactor.Three kinds of cofactors may be
Consequently, the substrate cannot bind andas a identified: prosthetic groups,co-enzymes and
result, the enzyme action declines, metal ions.
e.g., Inhibition of succinic dehydrogenase by a)Prosthetic groups:
malonate which closely resembles the They are organic compounds and are
substratesuccinate in structure. distinguished from other cofactors in that they
 Such competitive inhibitors are often used in are tightly bound to the apoenzyme.
the control of bacterial pathogens. Example: in peroxidase and catalase, which
catalyze the breakdown of hydrogen peroxide to
water and oxygen, haem is the prosthetic group
Classification and Nomenclature of
and it is a part of the active site of the enzyme.
Enzymes b)Co-enzymes :
Thousands of enzymes have been They are also organic compounds but their
discovered, isolated and studied. Mostof these association with the apoenzyme is only transient,
enzymes have been classified into different usually occurring during the course ofcatalysis.
groups based on the type of reactions they The essential chemical components of many
catalyse. Enzymes are divided into 6 classes each coenzymes are vitamins, e.g., coenzyme
with 4-13 subclasses and named accordingly by a nicotinamide adeninedinucleotide (NAD) and
four-digit number. NADP contain the vitamin niacin.
1.Oxidoreductases/dehydrogenases: Enzymes c)Metal ions :
which catalyse oxidoreduction between two A number of enzymes require metal ions for their
substrates S and S’ e.g., activity which formcoordination bonds with side
S reduced + S’ oxidised → S oxidised + S’ reduced. chains at the active site and at the sametime
2.Transferases: Enzymes catalysing a transfer of a form one or more cordination bonds with the
group, G (other thanhydrogen) between a pair of substrate,
substrate S and S’ e.g., e.g., zinc isa cofactor for the proteolytic enzyme
S - G + S’ → S + S’ - G carboxypeptidase.
3.Hydrolases: Enzymes catalysing hydrolysis of  Catalytic activity is lost when the co-factor
ester, ether, peptide, glycosidic, C-C, C-halide or is removed from the enzyme
P-N bonds.
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Scan QR code For Video lesson

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Previous year questions
1. General structure of amino acid is given :

Draw the structure of the amino acids,

(a) glycine and (b) Serine. (HSE-,MARCH-2023)(2)
2. Observe the illustration : (HSE-,MARCH-2023)(2)

(HSE-SAY/IMP-JAN -2022)(2)

8. Catalytic activity is lost when the co-factors are

removed from the enzyme.
(a) What are co-factors ?
(b) Name two kinds of co-factors
(HSE-SAY/IMP-JAN -2022)(3)
9. Observe the graph and comment
(a) Identify A & B and fill the blanks.
(b) What happens when the co-factor is removed
from the enzyme ?
3. Distinguish between : (HSE-,MARCH-2023)(3)
(a) Nucleosides and Nucleotides
(b)Primary metabolites and Secondary
metabolites
(c) Ligases and Lyases
4. Name the most abundant protein in animal world. (HSE-Sept-2021)(1)
(HSE-JUNE-2022)(1)
5. (a) Identify the level of protein structure in the 10. Write the structure of (HSE-Sept-2021)(2)
given diagram (HSE-JUNE-2022)(3) (a) Alanine (b) Glycine
(b) Name two levels of protein structure which 11. Non-protein constituents called co-factors are
are not three dimensional. bound to the enzyme, to make it catalytically
(c) Give an example for protein having quaternary active. (HSE-Sept-2021)(3)
structure and justify your answer. (a) Name the protein part of the enzyme.
(b) Mention any two kinds of co-factors with
examples.
(c) What happens to the catalytic activity of
enzyme, when the co-factor is removed ?
12. Observe the following equation

a)Explain the catalytic cycle of the enzyme on

the basis of above equation
b)Write any 2 factors affecting enzyme
activity ? (HSE-Dec-2020)(3)
13. Which among the following is a primary
6. Name a protein enables glucose transport into metabolite ? (HSE-March-2020)(1)
cells. (HSE-SAY/IMP-JAN .-2022)(1)
7. (a) Identify the following nitrogen bases A and B.
(b) Write the nucleosides of these.
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NAVAS CHEEMADAN SOHSS-Areekode

14. When substrate concentration increases, the 19. Observe the graph given below
velocity of enzymatic reaction increases (HSE-Aug-2018)(3)
atfirst. After attaining a maximum velocity, it
cannot be exceeded by further addition of
substrates. Why ? (HSE-March-2020)(2)
15. Match the following (HSE-July-2019)(3)

a) Identify the graph.

b) Mention the role of Enzyme in this
process.
20. The molecular structure of 2 amino acids are
given below Name them.(HSE-March-2018)(2)
16. ........... is the most abundant protein in the animal
world.(HSE March 2019)(1)
17. Observe the diagram A and B given below

21. a)Complete the diagrammatic representation

showing the nature of enzyme action :
(HSE-March-2018)(3)

a)What is A and B’
b)Mention the other two levels of protein
structure ?(HSE March 2019)(2) b) List out any two factors affecting enzyme
activity.
c)Based on the reaction formulae given
18. General formula of amino acid is given below
below, identify the classes of the enzymes.

(HSE-Model-2019)(3)
(a) Prepare the amino acide serine using this
formula
(b) Proteins carry out manyfunctionsin living 22. a) Effect of change in concentration of
organisms, Iist any four. substrate on enzyme activity is graphically
(c) Give one word represented' After reaching a maximum
(i) The nucleic acid that behave like velocity (Vmax)" the reaction is not exceeded
enzymes by any further rise in concentration of
(ii) The organic compound tightly substrate' Explain"
bound to the apoenzyme. b) Mention any 2 other factors that affect
(iii) The non-protein organic enzyme activity ?(HSE-Model-2018)(3)
compound that are not tightly
bound to the apoenzyme
(iv) The protein part of the enzyme
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NAVAS CHEEMADAN SOHSS-Areekode

28. a)Name the biomacromolecule (Polymer) in

which peptide bond is present ?
b)Name the bond present between
phosphate and hydroxy group of sugar in
23. Fill in the blanks suitably (HSE-Model-2018)(2)
nucleic acid ? (HSE-sept-2016)(2)
In a proteins aminoacids are linked by
….(a)…In a polysacharides individual
monosacharides are linked by…….(b)….. 29. Metabolites are organic compunds constantly
24. Identify the wrong statement from the utilzed in various metaolic activities in the
following and correct it (HSE-July-2017)(1) cells (HSE-March-2016)(2)
a)Lipds are not strictly macromolecule a)What are the two types of metabolites in
b)Cellulose is not a polysaccharide the cells?
25. Examples of 2 enzymatic reactions A and B b)Give an example for each type of
are given. Identify the class of enzyme in A metabolites?
and B (HSE-July-2017)(2) 30. Enzymes are biocatalyst which regulate
A) S reduced + S’ oxidised → S oxidised + S’ reduced.
various biochemical reaction
(S,S’- Substrate )
Illustrate the following reaction
B) S - G + S’ → S + S’ – G
(S,S’- substrate,G-Group) (HSE-March-2016)(2)

OR 31. Compelete the following sequence

26. “ Proteins is a heteropolymer not a
with approprite words
homopolymer “ . Substantiate the statement
? (HSE-July-2017)(2) (HSE September-2015)(1)
Amino acids:………(a)…….bond:protein
27. Identify the given biomolecule that comes ………(b)………: glycosidic bond :
under fat (HSE-sept-2016)(1) polysacharide
32. Based on the graph given below,
explain the effect of concentration of
substrate on enzyme activity.
(HSE September-2015)(2)
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NAVAS CHEEMADAN SOHSS-Areekode

c.Identify the type of protein structure
of a and b (HSE August-2014)(3)

33. Identify the protein structures, (a) and

(B) from the following figure
6. Symbolic presntation of a functional
(HSE March-2015)(1)
enzyme is given below
(HSE August-2014)(3)

34. Analyze the graph showing the activity a.Write one difference between
of an enzyme, influenced by cofactor and apoenzyme?
temperature (HSE march-2015)(2) b.name the different types of cofactor
c.what is the cofactor for the enzyme ,
carboxypeptidase
7. Name the chemical bond formed
between the following
(HSE March-2014)(1)
a. Amino acids in a protein moleucle
b. Sugar and phosphate in a nucleic
a)What is meant by optimum acid
temperature? 8. Distinguish between cofactor and
b)why does enzyme activity declines at coenzyme with an example for each?
too low and at too high temperature? (HSE March-2014)(2)
5. a. Why are proteins heteropolymers? 9. Oserve the graph and answer the
b.Identify the proteins from the given following (HSE-SEPTEMBER-2013)(3)
list of iomacromolecule and write its
functions
(Cellulose,starch,antibody, inulin)
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NAVAS CHEEMADAN SOHSS-Areekode

a. Name the possible enzyme involved
in this reaction?
b. Where is its site of action
c. Mention any other factor which
affects this enzyme
d. Name another similar enzyme
acting on the same sustrate
12.Fill in the blanks
(HSE September-2012)(1)
a.Find out the role of enzyme?
Carbohydrate : sugar
b.Mention any two factors that
Proteins:…………..
influence the activity of an enzyme and
13.Analyse the graph showing the activity
state their influences?
of salivary amylase
(HSE September-2012)(1)
10.

(HSE MARCH-2013)(1.5)
a. Identify this compound?
b. Name the bond produced when
another compound of the same
category combine with this? a.Which is the optimum
c. If a number of such molecule temperature for salivary amylase
bonded together , what will e the from the graph?
resultant molecule ? b.Why the activity declines below
11.Oserve the graph shoing the activity of the optimum value ?
an enzyme influenced y pH 14.Non protein constituent called cofactor
(HSE march-2013)(2) are bound to the enzyme to make the
enzyme catalytically activity
(HSE March-2011)(3)
a.Name the protein portion of the
enzyme
b.What happens to the catalytic
activity when the cofactor is removed
from the enzyme?
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NAVAS CHEEMADAN SOHSS-Areekode

c.Mention any two kinds of cofactor
with examples?
15.Observe the graph

(HSE-March 2010)
a.What is meant by ‘Vmax’ value?
b.Why is ‘Vmax’ not exceeded by any
further rise in the substrate
concentration
c.If a chemical substance closely
resembling to that of a substrate is
introduced into a reaction system,
what will be the consequences?
Sustantiate
16.Fill in the blanks coloumns with the
correct terms/sentence
(HSE march-2009) (2)
A B
…………(1)………. Catalyse oxiod
reduction
between 2
sustrate
Transferase …………(2)………..
Lyases Catalyse hydrolysis
of ester, glycosidic
bond
………(3)………. Catalyse inter
conversion of
opical isomers
Ligase ………(4)……….