Prepared By:

Catherine M.
Precioso

Matching Game!

What Are Enzymes?

Most enzymes
are Proteins
Act as
Catalyst to
accelerate a
reaction

Not
permanently
changed in
the process

Enzymes
4

Are specific for what they

will catalyze
Are Reusable
End in ase
-Sucrase
-Lactase
-Maltase

Gelatin and pineapple

tidbits

Bromelain and Papain

10

How enzyme works?

11

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How do enzymes Work?

Enzymes work
by weakening
bonds which
lowers
activation
energy

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Activation Energy

Refers to the energy level that the

reactant molecules must overcome
before a reaction can occur

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How enzymes work

The activation energy barrier is like a

wall between two parts of a pond. If an
enzyme lowers the wall, more frogs have
enough energy to reach the other side.

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Enzymes
Without Enzyme
With Enzyme

Free
Energy

Free energy of activation

Reactants

Products

Progress of the reaction

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How enzymes work?

Enzyme-Substrate Complex
18

The substance (reactant) an

enzyme acts on is the

substrate
Substrate

Joins

Enzyme

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Active Site
Refers to the restricted
region of an enzyme
molecule
which binds to
Active
the substrate.
substrate
Site
Substrate

Enzyme

The Lock and Key

Hypothesis
S

E
E
E

Enzymesubstrate
complex

Enzyme may
be used again
P
P

Reaction coordinate
2007 Paul Billiet ODWS

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Induced Fit

A change in the shape of

an enzymes active site
Induced by the substrate

What Affects Enzyme

Activity?
Three factors:
1. Environmental Conditions
22

2. Cofactors and Coenzymes

3. Enzyme Inhibitors

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1. Environmental
Conditions

1. Extreme Temperature
are the most dangerous
- high temps may denature
(unfold) the enzyme.

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Why is having a fever a

problem?
Enzymes work best in small temperature
range around the organisms body
temperature (98.60 C)

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2. pH (most like 6 - 8 pH near

neutral)
3. Substrate concentration

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2. Cofactors and
Coenzymes
Inorganic substances

(zinc, iron) and vitamins

are sometimes needed
for proper enzymatic
activity.
activity

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

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Coenzyme

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3. Two examples of Enzyme

Inhibitors
30

a.

Competitive inhibitors:

are chemicals that resemble an

enzymes normal substrate and
compete with it for the active site.
site
Substrate

Competitive inhibitor

Enzyme

Inhibitors

31

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

Enzyme

Noncompetitive
Inhibitor

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Components of an
Enzyme

Holoenzyme (whole enzyme)

Apoenzyme (Protein portion)
Cofactor (non protein factor)

Types of Enzymes
34
Class

Function

Catalyze oxidationOxidoreductas reduction reactions

e

Transferases

Hydrolase

Catalyze the transfer

of a functional group
between two
substrates

Catalyze hydrolysis
reactions (addition of
water molecule to a
bond)

Class
35
Lyases

Isomerase

Ligase

Function
Catalyze the addition
of a group to a double
bond or removal of a
group to create a
double bond
Catalyze the
conversion of
substrate into another
compound

Catalyze the bonding

of two substrates with
the participation of
ATP

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For Laboratory Activity

Salivary amylase is an enzyme that
breaks down starch into maltose.
Its optimum temperature for activity
is around 37C.
Design an experiment to find out how
enzyme activity is affected by
different factors. The experimental
design should consists of: Introduction
(brief introduction about enzymes),
objective and methods and materials.