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Chapter 1

Contents in Chapter 1
1.1 The general characteristics of enzymes
1.2 The relationship between enzyme and activation energy
1.3 Enzyme specificity relating to Key and Lock Model
1.4 Enzyme specificity relating to Induced-Fit Model
1.5 Factors affecting enzyme activities
-Enzyme concentration, substrate concentration, temperature, pH
1.6 Inhibition
-Basic principle of enzyme inhibition (competitive versus non-
competitive; reversible versus irreversible)
- One example of competitive and non-competitive inhibition
- One example of reversible and irreversible enzyme inhibition
1.7 Allosteric regulation
- Definition of allosteric activator and inhibitor
- Allosteric inhibition
1.8 Enzyme Classification (6 classes)
- Oxidoreductase, Transferase, Isomerase, Hydrolase, Lyase, and


Chapter 1: Enzymes

1.1 The general characteristics of enzymes

1.2 The relationship between enzyme and activation


1.3 Enzyme specificity relating to Key and Lock Model

1.4 Enzyme specificity relating to Induced Fit Model

Lesson learning outcome

Explain the properties of an enzyme.

Describe the enzymatic reaction.

Describe and differentiate between Key

and Lock Model and Induced Fit Model.


• The total of all the chemical reactions occur in
cells is known as metabolism.
• These chemical reactions may be classified
into two types:
- anabolism
- catabolism

– sum of all the chemical reactions that occur within an organism

- Simpler substances combined to form - Complex substances are broken
more complex substances. down to form simpler substance.

- Eg; - Eg;
synthesis of glycogen hydrolysis of glycogen
(glucose + glucose)n glycogen Breakdown of glycogen to glucose

- Require a constant input of energy to - Involve the breakdown of high energy

convert low energy substance into substances into lower energy products
higher energy products

- Endergonic reaction (energy needed - Exergonic reaction (energy is

to form chemical bond) released) 6


• Majority of these biochemical reaction do not

take place spontaneously.
 Catalysis make possible biochemical reactions.
• Catalysts – speed up chemical reaction but
stay unchanged at the end of the reactions.
• The catalysts of biochemical reaction are
- bringing about almost all of the chemical
reaction in living organisms.

Characteristics of enzyme
1. Enzymes globular protein with are catalytic properties.
 made a long and linear chains of amino acids that fold to
produce 3-D shape.
 mostly tertiary and quaternary structure.

2. Have active site for substrate binding.

 (active site - location the reaction occurs).
 Active site contains amino acid side chain that are
complementary to the substrate.


Characteristics of enzyme
3. Reaction reversible
 catalyzing reaction of enzyme is reversible and does not
consumed by the reaction.

4. Enzyme specificity
 For any chemical reaction, the reactant that an enzyme acts on
is called the substrate.
 Highly specific in their action, only certain substrate will fit into
enzyme’s active site.
 The enzyme binds to its substrate, forming an enzyme-substrate

Characteristics of enzyme
• Enzymes bind only certain substrate.

• Absolute specificity
- catalyze one reaction
• Group specificity
- act only on specific
functional group such as H20
amino, methyl and
• Linkage specificity
- act on particular type of
chemical bond


Characteristics of enzyme
5. Very efficient
 Only small amount of enzyme can change a large amount of
substrate into products.

6. Affected by many factors

 such as by pH, temperature, substrate concentration, enzyme
concentration, inhibitors and activators.

7. Catalysts
 because they can speed up chemical reactions by Lowering the
Activation Energy.

Enzymes speed up chemical reactions by lowering

activation energy
 Chemical reaction is a process of forming and breaking of
chemical bonds, leading to the changes of starting
materials (substrates) to the new substances (products).

 Chemical reactions need an initial input of energy so the

bonds in the substrate can break = THE ACTIVATION

 With the presence of an enzyme, the reaction runs in the

same direction as it would without the enzyme, just more

 Enzyme works by lowering the activation energy.


Enzymes speed up chemical reactions by lowering

activation energy

An enzyme catalyzes a reaction by lowering the EA :

 enabling the substrate molecules to absorb enough
energy to reach the transition state even at moderate
temperature (e.g. room temp).

• Unstable condition of substrate.

• Substrate activated; breaking and
making bonds can occur.
• increases the chances of a
successful collision.

delta G / ∆G
The different
between free


How enzyme lowering the activation energy

• In an enzymatic reaction, the substrate binds to the active
site of the enzyme
• The active site can lower an EA barrier by
– Orienting substrates correctly
 for substrate to come together in proper orientation for a
reaction to occur between them.
– Straining substrate bonds
 stretch substrate toward their transition state
conformation, stressing and bending critical chemical
bonds that must be broken
– Providing a favorable microenvironment
 If the active site has amino acid with acidic R group active
site maybe a pocket of low pH compare to the neutral cell.




(a) Exergonic reaction: energy released

2 type of enzymatic reaction :- △G = [E of product ] – [E of reactant]

a) Exergonic reaction
Amount of
- chemical reaction which energy
Free energy

(G  0)
energy is released. Energy
- breakdown of high energy
substances low energy
product Progress of the reaction

b) Endergonic reaction (b) Endergonic reaction: energy required

- chemical reaction which Products

energy is required.
Amount of
- simpler substances energy
Free energy

(G  0)
complex substances Energy
Energy coupling – Energy
generated by catabolic process
used by cells to perform anabolic Progress of the reaction



Mode of action/Mechanism of
enzyme action

Lock and Key Model

Induced-Fit Model

Lock and Key Model (Emil Fisher)

 In this theory, the lock is
the enzyme and the key is
the substrate.

 Only the correctly sized

key (substrate) fits into
the key hole (active site)
of the lock (enzyme).

 The active site has a fixed,

rigid gemometrical
structure (the lock), which
exactly matched the
structure of a specific
substrate (the key).


Induced-Fit Theory (Daniel Koshland)

 Some enzymes can change their shape (conformation).
 When a substrate combines with an enzyme, substrate
induces a change in the enzyme’s conformation.
 The active site is then moulded into a precise conformation.
 The active site has a flexibility of shape.
 When the product is release from the active site, the enzyme
returns to its original shape.

A change in the shape of an enzyme’s active site induced

by the substrate.