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Derived from Greek World ( En = in, Zyme = Yeast )

Enzymes are commonly proteinaceous substances of high molecular weight which accelerate, or
catalyze, chemical reaction of biological origin without them self undergoing any change.
Enzymes have a high degree of specificity for types of reaction catalyzed and for their substrate
The term enzymes was coined by Kuhne in 1878
First enzyme extract from yeast cell by Buchner (1897)
Enzyme nomenclature and classification
Previously enzymes use to be named by adding in e.g. Pepsin, trypsin etc.
In 1883 Duclaux proposed the naming of enzymes by adding the suffix "-ase" to the substrate on
which the enzyme acts or the chemical reaction it catalyzes. Example enzymes acting on sucrose as
sucrose, enzymes catalyzing oxidation oxidase.
The International Union of Biochemistry and Molecular Biology have developed the EC ( Enzyme
commission) numbers of four digits Preceded by EC.
First digit denotes: Class
Second digit denotes: Sub class
Third digit denotes: Sub-sub class
Fourth digit denotes: Sub-sub-sub class
For examples example, hexokinase (EC is a transferase (EC 2) that adds a phosphate group
(EC 2.7), a molecule containing an alcohol group (EC 2.7.1) to a hexose sugar (EC
First two digits represents type of reaction it catalyzed, last two digits represents substrate which enzyme
The International Enzyme commission (IEC) system has divided the enzymes into six major groups based
on type of reaction catalyzed
EC 1: Oxidoreductases
Enzymes of this group add or remove hydrogen and oxygen atoms or electrons from one substance to
another during the catalysis

Example: Oxidases, Dehydrogenases, Reductases

EC 2: Transferase
These enzymes catalyze the transfer of a functional group (methyl-,acyl-,amino- or phosphate) of atoms
from one molecule to another.


Transaminase (transfer amino groups), Kinases ( transfer phosphate group )

EC 3 Hydrolases:
Catalyze the hydrolysis ( cleavage of chemical bonds by the addition of water ) of various bonds

EC 4, Lyases:
Cleave various bonds by means other than hydrolysis and oxidation

EC 5, Isomerases: catalyze isomerization changes within a single molecule

EC 6, Ligases: join two molecules with covalent bonds with breakdown of the energy containing

Properties of enzymes
1. Enzyme is specialized protein
It exhibit all properties of proteins
2. Colloidal nature : Due to large size of molecules
3. Catalytic property
Enzymes are very efficient catalyst. Only small amount of enzymes is enough to convert large
quantity of substrate in product. It Speed up reaction by 106 - 1012 times greater than those of
the corresponding un catalyzed reactions
4. Specific
Enzymes are more specific toward their substrates and for the type of reactions that catalyze.
Enzymes shows 3 types of specificity
a. Specific specificity

Some enzymes act on only one substrate

e.g. Urease acts only on urea.
b. Group specificity
Catalyze the reaction of structurally related groups only
Amylase hydrolyses the group of substances like starch, dextrin and glycogen, which have the same
type of glycosidic linkages (1,4).
c. Optical Specificity
The enzymes acts on only one of the two optical isomers of a compound
For example L-amino acid oxidase acts only on L-amino acid but not on its D-form of amino acid.
5. Heat sensitivity ( note )
Enzyme is very sensitive to heat. Optimum temperature for enzyme action is 35-37 degree
centigrades. The enzymes activity decreases below or above this temperature due to denaturation.
6. pH sensitivity
Enzyme is dependent upon the pH of where the reaction is taking place, e.g. pepsin in the stomach
has an optimum pH of about pH2, Whereas salivary amylase has an optimum pH of about 7. 4.
7. Reversibility of reaction
Enzymes are capable of bringing reversion in a chemical reaction
Function of enzymes
1) To accelerate or retard or bring about reaction
2) Regulate reaction
3) To make possible the metabolic reactions
4) To facilitate reaction
5) To break down larger molecule to small molecule
6) To carry out flow of reaction smoothly

Mechanism of enzyme action

Enzymes helps in the progress of the reaction in 2 ways
1. Lowering activation energy
2. Formation of enzyme substrate complex
There are three theories to explain formation of enzymes substrate complex.
a. Michaelis-Menton Hypothesis
The theory postulates that the enzymes has number of active sites where the substrate is bounded to form
weak enzyme substrate complex (S). This enyzme-substrate complex, on hydrolysis, decomposes to yield
the reaction product (P) and the free enzyme (E). These reactions may be symbolically represented as
[S] + [E] ----------> [ES] ---------> P+[E]

b. Fishers lock and key model

This model was proposed by Emil Fischer in 1898. According to this model, the union between the
substrate and the enzyme takes place at the active site more or less in a manner in which a key fits a lock
and results in the formation of an enzyme substrate complex. The enzyme-substrate complex is highly
unstable and almost immediately this complex decomposes to produce the end products of the reaction
and to regenerate the free enzyme.


Koshlands Induced fit model

Enzyme structure flexible, not rigid
Enzyme and active site adjust shape to bind substrate
Increases range of substrate specificity
Shape changes also improve catalysis during reaction

Compounds which convert the enzymes into inactive substances and thus adversely affect the rate of
enzymatically-catalyzed reaction are called as enzyme inhibitors. Such a process is known as enzyme
1. Reversible inhibitors
A reversible inhibitor dissociates very rapidly from its target enzyme
A. Competitive inhibitors
Has a structure similar to substrate
Occupies active site
Competes with substrate for active site
Has effect reversed by increasing substrate concentration

For example:- An enzyme, succinic acid dehydrogenase (= succinodehydrogenase) catalyzes the

conversionof succinic acid to fumaric acid.but presence of malonic acid inhibit the reaction.
B. Non-competitive inhibitors
The inhibitor has little or no structural resemblance with the substrate and it binds with the enzyme at a
place other than the active site.

For example presence of heavy metal like Ag+, Hg +2 etc inhibit the activity of a variety of enzymes.
3. Irreversible inhibitors
Irreversible inhibitors are those that combine with or destroy a functional group on the enzyme that is
essential for its activity. For example iodoacetamide irreversibly inhibit the catalytic activity of some
enzymes by modifying cysteine.