ENZYMES

Dr. Md. Rageeb Md. Usman

(M. Pharm., Ph.D., FAPP, FICPHS, FSRHCP, FRSH, FSPER)
Associate Professor
Department of Pharmacognosy

Smt. Sharadchandrika Suresh Patil

College of Pharmacy, 1
 WHAT ARE ENZYMES?
Most enzymes are
Proteins (tertiary
and quaternary
structures)
Act as Biological
Catalyst to
accelerates a reaction
Soluble in water and
dil. alcohol

2
 ENZYMES

End in –ase
-Sucrase
-Lactase
-Maltase

3
HOW DO ENZYMES WORK?
Enzymes work by
weakening bonds
which lowers
activation energy

4
 ENZYMES
Without Enzyme
With Enzyme

Free Free energy of activation

Energy
Reactants

Products

Progress of the reaction

5
6
 ENZYME-SUBSTRATE
COMPLEX
The substance
(reactant) an
enzyme acts on
is the substrate

Joins
Substrate Enzyme

7
 ACTIVE SITE
A restricted region of an
enzyme molecule which binds
to the substrate.
Active
Site

Substrate
Enzyme

8
 INDUCED FIT
A change in the
shape of an
enzyme’s active
site
Induced by the
substrate

9
 INDUCED FIT

A change in the configuration of an

enzyme’s active site (H+ and ionic
bonds are involved).
Induced by the substrate.

Active Site
substrate
Enzyme

induced fit
10
 WHAT AFFECTS ENZYME ACTIVITY?

Three factors:
1. Environmental Conditions

2. Cofactors and Coenzymes

3. Enzyme Inhibitors

11
 1. ENVIRONMENTAL CONDITIONS

1. Extreme Temperature are the most

dangerous
- high temps may denature (unfold)
the enzyme.

2. pH (most like 6 - 8 pH near

neutral)
3. Ionic concentration (salt ions)

12
 2. COFACTORS AND COENZYMES

Inorganic substances (zinc, iron) and

vitamins (respectively) are sometimes need
for proper enzymatic activity.

Example:
Iron must be present in the quaternary structure - hemoglobin in order
for it to pick up oxygen.

13
TWO EXAMPLES OF ENZYME
INHIBITORS
a. Competitive inhibitors: are
chemicals that resemble an
enzyme’s normal substrate and
compete with it for the active
site.
Substrate
Enzyme
Competitive inhibitor

14
 INHIBITORS
b. Noncompetitive inhibitors:
Inhibitors that do not enter the
active site, but bind to another
part of the enzyme causing the
enzyme to change its shape, which
in turn alters the active
site. Noncompetitive
Substrate
Enzyme Inhibitor
active site
altered
15
 Fundamental Properties

1) Enzymes are excellent catalysts, speeding up reactions 108 to

1020 fold.

2) Specificity

a) for substrate - ranges from absolute (e.g., aspartase) to relative

b) for reaction catalyzed, i.e.,few side-reactions and by-products, etc.)

3) Regulated-- some enzymes can sense metabolic signals.

16
Classification of Enzymes
Class Reactions catalyzed
• Oxidoreductoases oxidation-reduction
• Transferases transfer group of
atoms
• Hydrolases hydrolysis
• Lyases bond add/remove atoms
to/from a double
• Isomerases rearrange atoms/
Intermolecular
Rearrangement

17

17
Class Reactions catalyzed

Ligases/ Syntheases Condensation of

two molecules coupled
with cleavage of
phosphate bond of
ATP

18
Classification of Enzymes on the Basis of Action

A) Endoenzymes:

Act only inside the cell

B) Exoenzymes:

Secreted outside the cell

19
Examples of Classification of Enzymes

• Oxidoreductoases
oxidases - oxidize ,reductases – reduce
• Transferases
transaminases – transfer amino groups
kinases – transfer phosphate groups
• Hydrolases
proteases - hydrolyze peptide bonds
lipases – hydrolyze lipid ester bonds
• Lyases
carboxylases – add CO2
hydrolases – add H2O

20 20