ENZYMES

Deepak Rajan DS
Department of Biochemistry
 DEFINITION

Enzymes are biocatalysts.

Enzymes may be defined as biocatalysts synthesized by living cells.

They are protein in nature (exception – RNA acting as ribozyme), colloidal and
thermolabile in character, and specific in their action.
CLASSIFICATION
 1. Oxidoreductases

 Oxidation to Reduction

 E.g.: Alcohol dehydrogenase

 Alcohol + NAD+ Aldehyde + NADH + H+

CLASSIFICATION
 2. Transferases

 Group Transfer

 E.g.: Hexokinase

 Hexose + ATP Hexose-6-phosphate+ ADP

CLASSIFICATION
 3. Hydrolases

 Hydrolysis

 E.g.: Acetylcholine esterase

 Acetylcholine + H2O choline + acetate

CLASSIFICATION
 4. Lyases

 Addition to Elimination

 E.g.: Aldolase

 Fructose -1,6-bisphophate Glyceraldehyde-3-phosphate

 + dihydroxy acetone phosphate
CLASSIFICATION
 5. Isomerases

 Interconversion of isomers

 E.g.: Triose phosphate isomerase

 Glyceraldehyde-3-phosphate dihydroxy acetone

 phosphate
CLASSIFICATION
 6. Ligases

 Condensation (dependent on ATP

 E.g.: Acetyl CoA carboxylase

 Acetyl CoA + CO2 + ATP Malonyl CoA+ ADP + Pi

CLASSIFICATION
 ACTIVE SITE

 The active site (or active centre) of

an enzyme represents as the small

region at which the substrate(s)

binds and participates in the

catalysis.
 SALIENT FEATURES
 Tertiary structure - Three dimensional.

 Catalytic residues

 Amino acids - Serine, Aspartate, Histidine, Cysteine, Lysine, Arginine,

Glutamate, Tyrosine.

 Not rigid

 Flexible in nature

 Possess - Substrate binding site & Catalytic site

 COENZYME
 Many enzymes require certain non-protein small additional factors, collectively

referred to as cofactors for catalysis.

 The cofactors may be organic or inorganic in nature.

 The non-protein, organic, low molecular weight and dialysable substance

associated with enzyme function is known as coenzyme.

 TYPES

 B - complex vitamins - TPP, FMN, FAD, PLP.

 Non-vitamin coenzymes - ATP, CDP & UDP.

 Nucleotide coenzymes - NAD, NADP.

 Protein coenzymes - Thioredoxin

FACTORS AFFECTING ENZYME ACTIVITY

1) Enzyme concentration

2) Effect of Substrate concentration

3) Effect of Temperature

4) Effect of pH

5) Effect of product concentration

6) Effect of activators

7) Effect of light and radiation

8) Effect of time
 ENZYME CONCENTRATION

 Rate of a reaction or
velocity (V) is directly
proportional to the enzyme
concentration.

 Velocity of reaction
increases proportionately
with the concentration of
enzyme
 EFFECT OF SUBSTRATE
CONCENTRATION

 Substrate concentration is

increased, the velocity is also

correspondingly increased in the

initial phases; but the curve

flattens afterwards.
 EFFECT OF TEMPERATURE

 The velocity of enzyme

reaction increases when

temperature of the medium is
increased; reaches a maximum
and then falls (Bell shaped
curve).
 EFFECT OF PH

 Each enzyme has an optimum pH.

 Optimum pH may vary depending

on the temperature, concentration of

substrate, presence of ions, etc.
Effect of product concentration

 The accumulation of reaction products generally decreases the

enzyme velocity.

Effect of activators

 Some of the enzymes require certain inorganic metallic cations like

Mg2+, Mn2+, Zn2+, Ca2+, Co2+, Cu2+, Na+, K+ etc. for their
optimum activity.
Effect of time

 Under ideal and optimal conditions (like pH, temperature etc.), the time required
for an enzyme reaction is less.

Effect of light and radiation

 Exposure of enzymes to ultraviolet, beta, gamma and X-rays inactivates certain

enzymes