ABC - Enzymes

SPECIFICITY OF ENZYMES
- Prepared by
Mrunali Bhosale
213242179
INDEX
• Introduction
• Specificity of enzymes
• Alteration specificity of enzymes
• References
INTRODUCTION
• Enzyme:- Proteins that acts as catalyst to speed up the rate of a chemical reaction in a living
organism.
• Active site of enzyme:-
i. Active site- The sites on enzymes where substrate binds. It is a three dimensional entity.
ii. Made up of groups that come from different parts of the amino acid sequence.
iii. Active sites contains amino acids such as aspartic acid, glutamic acid, lysine, serine,
Histidine, etc.
iv. Conjugate proteins function only in the presence of non-protein molecules or metal ions
called as prosthetic groups. Fig1:- Active site on enzyme
v. True prosthetic group- If non- protein molecule is tightly bound to the protein.
vi. Cofactor- If non- protein molecule is weakly bound to the protein.
vii. Cofactors can be organic as well as inorganic substance9usually meta cation, such as
magnesium, zinc, ferrous).
viii. Coenzyme- when cofactor is organic substance.
Apoenzyme(inactive)+cofactor = holoenzyme(active)
SPECIFICITY OF ENZYMES
• The ability of an enzyme to discriminate between the two competing

substrates is called as the Specificity of enzymes.
• Enzymes are highly specific in the reaction they catalyse and the
substrate they act upon.
TYPES AND CLASSIFICATION OF ENZYMES SPECIFICITY
1. Substrate Specificity
a. Absolute substrate specificity

• Enzymes are specific to only one substrate and one reaction.
• Example:-
1. Lactase acts only on lactose
2. Sucrase acts only on sucrose
3. Maltase acts only on maltose
b. Relative substrate specificity
• Enzymes acts on more than one substrate.
• Types of relative substrate specificity:-
i. Bond specificity
• Enzymes acts on substrate that are similar in structure and have same type of bond.
• Example:- Peptidase enzyme are specific to peptide bond formed between any amino acids.
Fig2:- Specificity of Peptidase enzyme

ii. Group specificity
• Enzyme specific to type of bond and group surrounding it.
• Example:-
1. Pepsin hydrolyze a peptide bond in which the amino group is
contributed by an aromatic amino acid (phenylalanine, tyrosine and
tryptophan).
Fig3:- Specificity of Pepsin enzyme

2. Trypsin hydrolyze a peptide bond in which amino group is
contributed by a basic amino acid (lysine, arginine and histidine).
Fig4:- Specificity of Trypsin enzyme
3. Chymotrypsin hydrolyze a peptide bond in which the carboxyl

group is contributed by an aromatic amino acid (phenylalanine,
tyrosine and tryptophan).
Fig5:- Specificity of Chymotrypsin enzyme

c. Broad Substrate specificity.
• In this case, an enzyme acts on more than one structurally related
substrates.
• Example, Hexokinase catalyses the phosphorylation of more than one
kind of hexoses such as glucose, fructose and mannose.
2. Reaction Specificity
• In this case, an enzyme is specific to a particular reaction but not to substrate(s)
and catalyzes only one type of reaction.
• Example:- pyruvate can undergo several reactions. Each reaction is catalysed by a
separate enzyme which catalyzes only that reaction and none other.
Fig6:- Reaction specificity

3. Stereo-Specificity
• Stereo-specificity of enzymes is also known as optical specificity of enzymes.
• Enzyme are specific not only to substrate but also to its optical configuration.
• Example:- L-amino acid oxidase acts only on L-amino acids
Fig7:-Stereo-specificity of L-alanine oxidase enzyme

• D-amino acid oxidase acts only on D-amino acids.
• α -glycosidic bonds of starch and glycogen are hydrolyzed only by α-
glycosidase (α -amylase).
• ß-glycosidic bonds of cellulose are hydrolyzed only by ß-glycosidase
(ß-amylase).
Fig8:-Stereo-specificity of α-amylase
enzyme
Alteration of Enzyme Specificity
• The specificity of some enzymes is altered by physiological behavior.
• Lactose Synthetase catalyzes the synthesis of lactose(glucose + galactose).
• Consists of catalytic subunit and modifier subunit.
• Catalytic subunit alone cannot synthesize lactose.
• Instead, it catalyzes the attachment of galactose to the proteins that contain
covalently linked carbohydrate chain.
• Modifier subunit alters the specificity of catalytic subunit so that it links Fig2:- Alteration enzyme specificity
galactose to glucose in order to form lactose.
• The level of modifier subunit is under hormonal control.
• During the pregnancy, the catalytic subunit is formed in the mammary glands
and very little modifier subunit is formed.
• Whereas, during parturition, the hormonal level changes significantly and the
modifier subunit is synthesized in greater quantities, thus resulting in the
production of large amounts of lactose.
References
https://www.easybiologyclass.com/enzyme-substrate-specificity-types-classification
/
https://www.worthington-biochem.com/introBiochem/specificity.html
https://blogs.ntu.edu.sg/cy1101-1819s1-g09/2018/10/enzymes-receptors/
https://bio.libretexts.org/Bookshelves/Microbiology/Book%3A_Microbiology_(Bou
ndless)/2%3A_Chemistry/2.7%3A_Enzymes/2.7.2%3A__Enzyme_Active_Site_and
_Substrate_Specificity
THANK YOU!

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SPECIFICITY OF ENZYMES

• The ability of an enzyme to discriminate between the two competing

a. Absolute substrate specificity

Fig2:- Specificity of Peptidase enzyme

Fig3:- Specificity of Pepsin enzyme

Fig4:- Specificity of Trypsin enzyme

3. Chymotrypsin hydrolyze a peptide bond in which the carboxyl

Fig5:- Specificity of Chymotrypsin enzyme

Fig6:- Reaction specificity

Fig7:-Stereo-specificity of L-alanine oxidase enzyme

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