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ENZYME

INHIBITION
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ENZYME INHIBITION
A

variety of small molecules exists that can reduce the


rate of an enzyme- catalysed reaction.

They

are called enzyme inhibitors.

Inhibition

is a normal part of the regulation of enzyme


activity within cells.

Many drugs and poisons also act as enzyme inhibitors.

Inhibition

may be competitive or non- competitive,


reversible or irreversible.
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Competitive Inhibition
Competitive

inhibitionis a form of
enzyme inhibitionwhere binding of the
inhibitor to the active site on theenzyme
prevents binding of thesubstrate
andvice versa.

Most

competitive inhibitors function by


binding reversibly to the active site of the
enzyme.
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Competitive Inhibition

Competitive inhibitors have a shape that is


somewhat similar to the normal substrate and
while it binds to the active site of the enzymes
it prevents the normal substrate from binding
hence prevents a reaction from occurring.

characteristic feature of competitive


inhibition is that an increase in substrate
concentration will increase the rate of the
reaction.
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Competitive Inhibition

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Example of competitive inhibition

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Non-competitive Reversible
Inhibition
This

type of inhibitor has no structural


similarity to the substrate.

The inhibitor combines at a point rather than


the active site.

It does not affect the ability of the substrate to


bind with the enzyme but it makes it
impossible for a reaction to take place.

The

rate of the reaction decreases with


increasing rate
of the inhibitor concentration.
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Non-competitive Reversible
Inhibition
When

inhibitor saturation is reached


the rate of reaction will be almost nil.

Increasing

the substrate
concentration will not increase the
rate of the reaction unlike
competitive inhibition.

The

inhibitor does not permanently


bind to the enzyme hence, inhibition
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Non- competitive Irreversible


Reaction
In

this type of inhibition, inhibitor leaves


the enzyme permanently damaged and
so it is unable to carry out catalytic
functions.

Heavy

metals for example mercury and


silver break the disulphide bonds.

Once

broken the enzyme structure


becomes irreversibly altered with
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Negative Feedback
Inhibition
Inhibition

feedback occurs in metabolic


pathways, i.e. a series of reactions that
transforms one substance into another.

In

negative feedback, a product near the


end of the pathway works to inhibit the
reactions at the start of the pathway, so
the reaction rate decreases.
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Negative Feedback
Inhibition

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Negative Feedback
Inhibition

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Allosteric Enzyme
Allo-

different, steric- shape

Allosteric

(noncompetitive) inhibition results from a


change in the shape of the active site when an
inhibitor binds to an allosteric site.

When

this occurs the substrate cannot bind to its


active site due to the fact that the active site has
changed shape and the substrate no longer fits.

Allosteric activation results when the binding of an


activator molecule to an allosteric site causes a
change in the active site that makes it capable of
binding substrate.
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Allosteric Enzyme

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Enzyme Cofactors
Anon-protein
If

component of enzymes is called the cofactor.

the cofactor is organic, then it is called a coenzyme.

Coenzymes

are relatively small molecules compared to the protein


part of the enzyme.

Many

of the coenzymes are derived from vitamins.

The

coenzymes make up a part of the active site, since without the


coenzyme, the enzyme will not function.

There

are three recognized types


of cofactors:
MAKE
NOTES ON
Inorganic ions
THESE!

Prosthetic groups
Coenzymes

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