CHAPTER 1

BIO150
 CONTENTS:
N ZY
08 Allosteric Regulation
 WHAT ARE
ALLOSTERIC
REGULATION?
Definition: The activities of enzyme is affected by the binding of regulatory molecule at
1 the allosteric site.
Regulatory molecule can be either inhibitor or
2 activator.

Regulatory molecule change shape of enzyme

3 between active and inactive shape.
Inhibitor cause the allosteric enzyme to adopt
4 the inactive shape, and reduce the enzyme
activity.

5 Activator promotes the active shape, and increasing enzyme activity.

 WHAT ARE
ALLOSTERIC
REGULATION?
The binding of an activator stabilizes the shape
6 that has functional active sites.

7 The binding of an inhibitor stabilizes

the inactive form of the enzyme.

In many cases both inhibitor and activator are similar enough in shape that they compete
8 for the same allosteric site.

These regulatory molecules maybe products and substrates of that particular metabolic
9 pathway.
Allosteric Inhibition
Most non competitive inhibitors bind to the allosteric site (Greek
1 word: allos, “other” + steros, “form”).
Allosteric
Active site site
enzyme

2 The binding of inhibitor to the allosteric site can switch the enzyme to
an active or inactive configurations. Substrate
cannot fit
Inhibitor
Substrate into the
molecule
fits into the active site
Allosteric enzyme is present
active site enzyme site empty

inhibitor
3 The active site change in shape and preventing the binding of the
substrate.
 Initial

Active
substrate
(threonin
e)
Feedback
site
available
Threonine
in active
Inhibition
site The end product of metabolic pathway act as
Enzyme 1
(threonin
inhibitor at early reaction in the pathway. End
Isoleucin
e
e product inhibit the 1st enzyme.
deaminas
used up
e) End product act as non competitive reversible
by Intermediate
Active site of
cell Feedbac A inhibitor, it binds at the allosteric site and
enzyme 1 is
no longer able k Enzyme
to catalyze the inhibitio 2
regulates the metabolic pathway.
conversion n Intermediate
of threonine to
intermediate
B The pathway is switched off by the inhibitory
A; Enzyme binding of its end products.
pathway is 3
switched off. Intermediate
Isoleucin C It happens because of the accumulation of end
e Enzyme
binds to 4 product. The end products are controlling their
allosteri Intermediate own rate of production.
c D
site. Enzyme
5 When the inhibitor concentration diminishes, the
enzyme’s conformation changes back to its
End
product active form, causes the inhibitor to leave the
(isoleucine) allosteric site.
 To be continued…

ENZYME

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