10/29/2014

Energy, Enzymes, and Catalysis Problem Set

Energy, Enzymes, and Catalysis Problem Set

Problem 3 Tutorial: Kinetics of an allosteric enzyme.
Which of the following graphs shows the results of reaction rate vs substrate concentration
for an allosteric enzyme in the absence and presence of an allosteric inhibitor?

Allosteric enzymes
Enzymes with multiple subunits have quaternary structure. One consequence of multiple
subunits is that individual catalytic subunits each have their own active site. This means that
an enzyme with quaternary structure can bind more than one substrate molecule. Allostery
means "different shape." Allosteric enzymes change shape between active and inactive
shapes as a result of the binding of substrates at the active site, and of regulatory molecules
at other sites. In the simple case of an allosteric enzyme with an active and inactive form,
the change in reaction rate with increasing substrate concentration is typically an "S-shaped"
curve. For more information on allosteric enzyme, see the tutorial for question 14.
Binding of effectors to regulatory subunits
Allosteric enzymes may also have regulatory subunits that bind either activators or
inhibitors. Activators and inhibitors are termed "effectors." Inhibitors cause the allosteric
enzyme to adopt the inactive shape. Activators promote the active shape.
An equilibrium exists between the active and inactive shapes. The amount of active and
inactive enzyme is dependent on the relative concentrations of substrate and inhibitor, as
suggested by the diagram:

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Energy, Enzymes, and Catalysis Problem Set

The binding of an allosteric inhibitor causes the enzyme to adopt the inactive conformation,
and promotes the cooperative binding of a second inhibitor.
An excess of substrate can overcome the inhibitor effect. Substrate binding causes the
enzyme to assume the active conformation, and promotes the cooperative binding of
additional substrate, leading to product formation.
The meaning of the S-shaped Curves with and without inhibitor
The shape of the curve minus inhibitor is described in more
detail in the tutorial to question 14. As the substrate
concentration is increased, substrate binds to enzyme and
triggers a conformation change to the active shape of the
enzyme.
In the presence of inhibitor (plus inhibitor), higher
concentration of substrate is required to shift the enzyme to
the active conformation. However once a high enough
concentration of substrate is reached to promote active shape,
the substrate binds cooperatively (S-shaped curve), and the
same maximum rate is achieved as without inhibitor.

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Energy, Enzymes, and Catalysis Problem Set

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