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ENZYMES
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Enzymes are proteinaceous, biocatalysts.
First enzyme discovered by Buchner R E L AT E D C O N T E N T
Term enzyme was given by Kuhne. Cell Biology, Chapter

Notes, Class 11, Biology
Zymase (from yeast) was the first discovered enzyme. (Buchner)
(https://edurev.in/studytube/Cell-
The first purified and crystalized enzyme was urease (by J.B. Biology-Chapter-Notes-
Class-11-
Sumner) from Canavalia/Jack Bean (Lobia plant) Biology/f5c47383-035c-
Proteinaceous nature of enzyme was established by Northrop and 4132-918f-
13fcd6844639_t)
Sumner. Doc | 75 Pages
DEFINITION Enzymes:
Characteristics,
Enzymes are biocatalysts made up of proteins (except ribozyme), Mechanism -
Biomolecules, Biology,
which increases the rate of biochemical reactions by lowering Class 11
down the activation energy. (https://edurev.in/studytube/Enzymes-
Characteristics-
First discovered ribozyme was L19 RNAase by T.Cech from rRNA Mechanism-
Biomolecules-
of a protozoan Tetrahymena thermophila and RNAase P or
B/26301b1b-3a7b-4324-
Ribionuclease P by Altman in prokaryotic cell (Nobel prize). aed1-9e2e99ee6c30_v)
Video | 11:47 min
GENERAL PROPERTIES OF ENZYMES
Nervous System,
Large sized biomolecules, colloid nature with high Chapter Notes, Class 11,
Biology
molecular weight - (https://edurev.in/studytube/Nervous-
System-Chapter-Notes-
Large size (equal to colloid particles)
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Class-11-
so passes large no. of active site. Large number of substrate Biology/6b957223-0ffb-
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converted into product by one molecule of enzyme at a time.
86a7fdb011ec_t)
Highest molecular weight is of enzyme pyruvate dehydrogenase Doc | 69 Pages
complex (46 lakh) participate in link reaction of respiration. Circulatory System,

Chapter Notes, Class 11,
Biology
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Proteinous nature
Excellent Average Poor System-Chapter-Notes-
Monomer unit of a enzyme is FAmino
R E L AT E D O R U M : acid x Class-11-
Biolo/cea7858c-2f67-
in liver how many mitochondria are present in 41c5-8e3e-
Amino acids linked togather to form polypeptide chain
human body Related: Cell Bio... more a7e3a0f9fa15_t)
Enzymes are polypeptide chains
(/question/816873/in- Doc | 55 Pages
Most of enzymes arrange in tertiary structure of protein or
how-
R E L AT E D T E S T S
globular proteins except
many-isoenzyme (Quaternary st.)
mitochondria- ECOSYSTEM
Tertiary structure of protein provides stability and water soluble CHAPTER 14 BIOLOGY
are-
nature to enzymes. present- (/course/quiz/attempt/-1_ECOSYSTEM-
CHAPTER-14-
in-
synthesis of enzymes occurs on ribosomes under the control of BIOLOGY/85cd3695-
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869b-4f5e-b63a-
genes.
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According to one gene one polypeptide hypothesis, if a enzyme is Test | 10 questions | 5 min
made up of same kind of polypeptide chains then synthesize ENVIRONMENTAL

ISSUES CHAPTER 16
under control of same gene and if made up of different kinds of
BIOLOGY
polypeptide chains then synthesized under the control fo (/course/quiz/attempt/-1_ENVIRONMENTAL
ISSUES-CHAPTER-16-
different genes. Ex. Rubisco, cytochrome oxidase, Nitrogenase. BIOLOGY/6ef37354-
da16-475d-80a6-
dde6c0efd53e)
Specificity Test | 10 questions | 5 min
BIODIVERSITY AND
Enzymes are specific for pH, temperature and substrate
CONSERVATION
pH - The common pH range of enzymes activity is 6 - 8. CHAPTER 15 BIOLOGY
(/course/quiz/attempt/-1_BIODIVERSITY-
Every enzyme works on specific pH, Pepsin-2.5 pH, Hydrolase-4- AND-CONSERVATION-
5, CHAPTER-15-
BIOLOGY-/af1fa482-
Rubisco, Pepcase-8.5 pH, Trypsin - 8.5 pH 7759-4b17-af42-
bf258944cf60)
Test | 10 questions | 5 min
ORGANISMS AND
POPULATION
CHAPTER 13 BIOLOGY
(/course/quiz/attempt/-1_ORGANISMS-
AND-POPULATION-
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Temperature Please rate the document to help us maintain content quality
Test | 10 questions | 5 min
Common range of temperature for enzyme activity is 20 – 40°C Test: Enzymes

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Enzymes works on body temperature of organism not on
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Enzymes of plants are affected by evironmental temperature Test | 15 questions | 15 min
change as plants does not show homeostasis.
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At low temperature enzymes
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Substrate
how-
Biology 28 Years
many-
Every enzyme works on specific substrate NEET/AIPMT Question
mitochondria- Papers of Class 11
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Ex. succinic dehydrogenase acts on succinic acid while pyruvate
dehydrogenase acts on pyruvic acid. Chemistry Class 11
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Enzymes increase the rate of reaction by decreasing
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activation energy -
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The number of reactent moleules converted into product by one

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molecule of enzyme in unitrate
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Enymes follows the Michaelis-Menten
R E L AT E D F O R U M : reaction kinetics x JOIN THE
DISCUSSION
It represents the substrate inconcentration
liver how many mitochondria
at which rateareof
present in
enzymetic reaction becomes the half of maximum Class 11 Group (/group/28/Class-11)
velocity or rate. liver- mitochondria-are-present-in-huma)
how-
If a enzyme passes high km constant then it’s affinity towards
many-
substrate is low and rate reaction is
mitochondria- Refer & Earn
are-
also low.
present-
in-
huma)
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STRUCTURE OF ENZYME
Simple enzymes
They are made up of only protein. eg. pepsin, trypsin.
Conjugated enzymes
They are made up of protein & non protein part.
TChoe-eyn azryem geesn -e rCaoll-ye nmzaydmee su pa rteo
nvoitna-mpriontse.in, orgainc groups, which are loosely attached
to apoenzymes. Please rate the document to help us maintain content quality
Prosthetic group - When non-protein part is tightly or firmly

attached to apoenzymes.
CMae,t aMl ag,c tCivuators/co-factros/metallic factor :- Lossely
attached inorganic co-factor eg. Mn, Fe, Co, Zn,
Excellent Average Poor

Active site :- The part
R E Lof polypeptide
AT E D FORUM: chain made up of specific x
sequence of amino acids atinwhich

liver how many mitochondria are present in
specific
saut bascttriavtee sisit eto i(/question/816873/in-liver-how-many-
sb ed ebtienrdmedin eadn db yc
agtaelnyeseticd , ckondoewsn. as active site. Very specific
how-
sequence of amino acids,
many-
mitochondria-
are-
Allosteric site : - Besides
present-the active site's some enzymes posess
in-
additional sites, at which chemical
huma)
eonthzeymr eth wanith s aulblossttreartice s(aitellso satreer icca
mlleodd ausl aatlolorss)t earriec beinnzdy. mTehse.s ee .gs.it
ehse xaorek inknaoswe,n p ahso sapllohsotferruicc tsoitkeisn
aasned.
TERMINOLOGY
Endoenzymes - Enzymes which are functional only inside the

cells. Ex. Enzymes of metabolism.
Enxzoyemnzeysm oefs i n- sEencztiyvmoeros ucsa tpallaynstesd,

Zthyem raesaec ticoonms poleuxts iodfe f ethrme ecnetlal
tEiogn:.- enzymes of digestion, some
Please
TPrryopesninzoygmeen/ rate the document
Zeytcm. to help are
ogen- These us maintain content
precursor of quality
enzymes or inactive forms of enzymes.eg. Pepsinogen,
Icsaolleend ziysmoeensz-y Emnezsy.m 1e6s fhoarmvisn go fs
imilar action, but little difference in their molecular
configuration are 3

Forms of Pepcase areRknown.
E L AT E D FT-haemsyel
ORUM: aaslle i soofe x
in liver how
wnzhyemate &fo 5rm fso ramres soyfmany mitochondria
nLthDeHs are present
is(eLda cbtya in
tdei fdfeerhenytd rgoegneens aasned) tissue and organ specific.
INnidtruogceibnlaes ee,n zymes - When formation of enzyme is
how-
induced by substrate many-
availability. eg. Lactase, -galactosidase.
mitochondria-
tEexmtrpeemraotuzyrem)
are- ees.g .- TEanqz pyomlyems,e
present-
rwahseic.h may also function at extremely adverse conditions
in-
(very high huma)
Abzymes - When the monoclonal antibodies (Mab) are used as

enzymes.
pBriootdeeotlyetricg eenntzsy -m Eensz.ymes used in washing

powders are known as bio-detergents eg.-amylase, lipase,
eHsosuesneti akl eteop cinegll./ cEoxn.s Etintuztyimvee se nozf

ycmeell sr e-s Wpirhaitciohn a. re always present in constant
amount & are also
NOMENCLATURE AND CLASSIFICATION
Enzyme commision of IUB-1961 divides all enzyes into 6 major

classes on basis of types of reactions catalysed by them. It also
proposed an international code of 4 digits for each enzyme. Suffix
‘-ase’ is used
for a enzyme.
Class-1 : Oxido-reductases - These enzymes involve in oxidation-

reduction reactions.
it involves 3 sub classes (i) Oxides (ii) dehydrogenase (iii)
reductase
e.g. Cytochrome oxides.
Please rate the document to help us maintain content quality
Class-2 : Trasferases - These Enzymes transfer specific group

from one substrate to another.
e.g. Transaminase, Hexokinase.
Class-3 : Hydrolases - These Enzymes involve in hydrolysis

reactions with help of H2O
e.g. Protease, Lipase, Carbohydrase. AB +Average
Excellent HOH AH + BOH Poor
Class-4 : Lyases - Spilt
R Ethe
L AT Esustrate
D F O R U M :molecule without water. x

These Enzymes splits the specfifc
covalent bonds without hydrolysis or H2O addition. AB
A+B
e.g. Aldolase liver- mitochondria-are-present-in-huma)
how-
Class-5 : Isomerases -many-
Rearrangement of molecular structure to
mitochondria-
form isomers.
are-
e.g. Isomerase, Epimerase
present-
in-
Class-6 : Ligases (Synthases)
huma) - Covalent bonding of two
substrates to from a large molecule. A + B AB
e.g. Citrate synthetase, Ligase, ATPsynthase
MODE OF ACTION OF ENZYME
Lock and Key theory or template theory :-
Given by Emil Fischer

According to this theory active sites of enzymes serve as a lock, at
which the reactant/substrate
fits like a key. Supported by competitive inhibition.
Enzyme-substrate complex theory :-
Given by Michaelis & Menten

E+S ESC ESC E+P
Induced fit theory : -
Given by D.E. Koshland (1973-74)

G According to this theory active site is not static, but it
undergoes a conformational change which is induced by specific
substrate. The active site has two groups, (1) Buttressing
(supporting) group & (2) Catalytic group.
Butterssing group is meant for supporting the substrate, while

the catalytic group break the substrate into product.
ALLOSTERIC MODULATION
Jacob & Monad. - First discovered L-threonine dehydratase,

inhibited by its product isoelucine.
In the allosteric modulation, chemical or products fits in allostric
sites & bring change in shape of active site of enzyme.
Chemicals which bindR Eat allostric
L AT E D F O R U site
M: of allostric enzymes are x

known as allostric modulators.
These modulators may be activators (positive modulators) or
inhibitors (nagetive modulators) of allosteric enzymes.
how-
If allostric modulator positively change the configuration of
many-
active site, then calledmitochondria-
positive allosteric modulation and if
are-
negatively change then called negative allosteric modulation
present-
respctively by+ve modulator
in- (activators) and-ve modulator
huma)
(inhibitors).
Ex. Phosphofructokinase inhibited by ATP, activated by ADP.

some times product also binds at allostetric site and inhibits the
enzyme.
Ex. Hexokinase inhibited by glucose-6P and exhibits feed back

inhibition.
This is a type of reversible and non-competitive inhibition found
in allosteric enzymes.
All allosteric modulation are not feed-back inhibition.
FACTORS
pH - Enzymes very sensitive to pH.

Temperature - High temp inactivates enzyme causing their
denaturation. They also get inactive at lower temp. Generally all
enzymes better perform at body temp. of organism.
Enzyme concentration - Increase in conc. of enzymes will
increases the rate of enzymetic reaction till enough the substrate.
Substrate conn- Increase in substrate conn increases the activity
of enzymes until all the active sites of enzyme ae saturated.
Inhibitors/Enzyme inhibition :-
Competitive inhibitors or competitive inhibition and reversible

type -
These are substrateExcellent
analogues, which bindAverage
to the active site and Poor
enzymes get inhibited,
R Esuch
L AT E Dinhibition
FORUM: is called as competitve x
inhibition. in liver how many mitochondria are present in

Eg. Succinic dehydrogenase is inhibited by its competitor
malonate. liver- mitochondria-are-present-in-huma)
how-
This is reversible inhibition. Malonate is known as substrate
many-
analogue of succinate.mitochondria-
are-
Similarly sulpha drugs are substrate analogue of para-amino
present-
benzoic acid (PABA) used
in- in folic acid synthesis in bacterical
huma)
cells. Hence these drugs are used to kill bacterial cells.
Non-competitve inhibitors or non competitive inhibition

and irreversible type :-
In this type of inhibition, inhibitor substance can bind

simultaneously to an enzyme, at any site
and destroy the sulfhydryl (S-H) group of enzyme.
Example :- Toxic metals, CO, CN poisoning of cytochrome
oxidase.
Such inhibition are irreversible inhibition.
Non competitive & reversible type :-

When inhibitor binds at allosteric site reversibly.
So, product inhibition is always reversible inhibition.
If competitive inhibitor (Reversible) is present, then, km -
and Vmax - No change.
If Non competitive (reversible) inhibitor is present, then, Km-No
change, Vmax -Decrease
Competitive inhibition is overcome by increase in concentration
of substrate.


how-
many-
mitochondria-
are-
present-
in-
huma)
SPECIAL POINTS OF ENZYMES

NAD = Nicotinamide Adenine Dinucleotide
DPN = Diphospho Pyridine Nucleotide
NADP = Nicotinamide Adenine Dinuclotide Phosphate
TPN = Triphospho Pyridine Nucleotide
FAD = Flavin Adenine Dinucleotide
FMN = Flavin Mono Nucleotide
Co A = Adenosine Triphospho Panta thenyl thio Ethanol Acetyl
Amine
I ATP = 7.6 K cal
Important Coenzymes are
Co-1 (NAD)/DPN Niacin
Co-II (NADP)/TPN Niacin

FAD Riboflavin
FMN Riboflavin
TPP Thiamine
CO-Q Ubiquinone
CO-R Biotine
Co-A Pantothenic Acid
R E L AT E D FORUM: x
Important Co-factor :- in liver how many mitochondria are present in

Fe++ = Cytochrome Oxidase, Catalase, Peroxides, Aconitase
Cu++ = Cytochrome oxidase, Tyrosinase
how-
Zn++ = Carbonic anhydrase, Alcohol dehydrogenase, Caboxy
many-
peptidase mitochondria-
are-
Mg++ = Hexokinase, Glucokinase, Pyruvate kinase, Pepcase,
present-
Rubisco in-
huma)
K+ = Pyruvate kinase
Mn++ = Arginase, Ribonucleotide reductase, Decarboxylase.
Mo = Nitrogenase complex, Nitrate reductase
Se = Glutathione peroxidase
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Enzymes, Chapter Notes, Class 11, Biology: Edurev

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Term enzyme was given by Kuhne. Cell Biology, Chapter

complex (46 lakh) participate in link reaction of respiration. Circulatory System,

made up of same kind of polypeptide chains then synthesize ENVIRONMENTAL

Common range of temperature for enzyme activity is 20 – 40°C Test: Enzymes

change as plants does not show homeostasis.

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the transiation state of chemical reaction or to undergo the 151 tests

chemical reaction. English Class 11

For Your Perfect

The number of reactent moleules converted into product by one

Highest T.O.N is of carbonic anhydrase (360 lakh / minute)

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The substrate concentration at which enzyme inhibitor complex

Prosthetic group - When non-protein part is tightly or firmly

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sequence of amino acids atinwhich

Endoenzymes - Enzymes which are functional only inside the

Enxzoyemnzeysm oefs i n- sEencztiyvmoeros ucsa tpallaynstesd,

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Abzymes - When the monoclonal antibodies (Mab) are used as

pBriootdeeotlyetricg eenntzsy -m Eensz.ymes used in washing

eHsosuesneti akl eteop cinegll./ cEoxn.s Etintuztyimvee se nozf

NOMENCLATURE AND CLASSIFICATION

Enzyme commision of IUB-1961 divides all enzyes into 6 major

Class-1 : Oxido-reductases - These enzymes involve in oxidation-

Class-2 : Trasferases - These Enzymes transfer specific group

Class-3 : Hydrolases - These Enzymes involve in hydrolysis

in liver how many mitochondria are present in

MODE OF ACTION OF ENZYME

Lock and Key theory or template theory :-

Given by Emil Fischer

Enzyme-substrate complex theory :-

Given by Michaelis & Menten

Induced fit theory : -

Given by D.E. Koshland (1973-74)

Butterssing group is meant for supporting the substrate, while

Jacob & Monad. - First discovered L-threonine dehydratase,

in liver how many mitochondria are present in

Ex. Phosphofructokinase inhibited by ATP, activated by ADP.

Ex. Hexokinase inhibited by glucose-6P and exhibits feed back

pH - Enzymes very sensitive to pH.

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Competitive inhibitors or competitive inhibition and reversible

inhibition. in liver how many mitochondria are present in

Non-competitve inhibitors or non competitive inhibition

In this type of inhibition, inhibitor substance can bind

Non competitive & reversible type :-

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in liver how many mitochondria are present in

SPECIAL POINTS OF ENZYMES

Co-II (NADP)/TPN Niacin

Important Co-factor :- in liver how many mitochondria are present in

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