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Types of Enzyme Inhibition Explained

This document discusses different types of enzyme inhibition. There are two broad classes: irreversible inhibition, which permanently inactivates the enzyme, and reversible inhibition. Reversible inhibition includes competitive inhibition, where the inhibitor binds the enzyme's active site and prevents substrate binding; uncompetitive inhibition, where the inhibitor binds the enzyme-substrate complex; and noncompetitive inhibition, where the inhibitor can bind either the enzyme or the enzyme-substrate complex. The key effects are that competitive inhibition increases the Km value but not the Vmax, uncompetitive inhibition decreases both Km and Vmax, and noncompetitive inhibition decreases Vmax but not Km.

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159 views10 pages

Types of Enzyme Inhibition Explained

This document discusses different types of enzyme inhibition. There are two broad classes: irreversible inhibition, which permanently inactivates the enzyme, and reversible inhibition. Reversible inhibition includes competitive inhibition, where the inhibitor binds the enzyme's active site and prevents substrate binding; uncompetitive inhibition, where the inhibitor binds the enzyme-substrate complex; and noncompetitive inhibition, where the inhibitor can bind either the enzyme or the enzyme-substrate complex. The key effects are that competitive inhibition increases the Km value but not the Vmax, uncompetitive inhibition decreases both Km and Vmax, and noncompetitive inhibition decreases Vmax but not Km.

Uploaded by

Bright Chimezie
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PPTX, PDF, TXT or read online on Scribd

CHE 511 ENZYME INHIBITION

 Inhibitors are molecules that resemble the substrate(s) or product(s) and


bind to active site thus they interfere with catalysis slowing or halting
enzymatic reactions. They have their physiological effect by decreasing
the activity of a specific enzyme. Concentration of inhibitor needed to
inhibit enzyme depends on how tightly inhibitor binds to the enzyme.

 Inhibition constant (Ki) is used to describe how tightly an inhibitor binds


to an enzyme.
Types of Inhibitors
There are two broad classes of enzyme inhibitors:
• Irreversible
• Reversible
Irreversible
irreversible inhibitors are those that bind covalently with enzyme or destroy a
functional group on an enzyme that is essential for enzyme’s activity.
Reversible
 This type of inhibition involves equilibrium between enzyme and inhibitor
equilibrium constant (ki) being the measure of affinity of the inhibitor for the
enzyme.
 This inhibition is further classified into three categories:
 Competitive
 Uncompetitive
 Noncompetitive.
Competitive Inhibition
 Competitive inhibitors bind only to free enzyme and to the same site as the
substrate.
 Competitive inhibitors are molecules that usually look like the substrate but
can’t undergo the reaction.
 At an infinite concentration of the substrate, competitive inhibitor cannot
bind to the enzyme since substrate concentration is high enough that there is
virtually no free enzyme present.
 Since competitive inhibitors have no effect on the velocity at
saturating (Vmax) concentrations of the substrate intercepts of the
double reciprocal plots (1/Vmax) at all the different inhibitor
concentrations are the same.
 The lines at different inhibitor concentrations must all intersect on
the y axis at the same 1/Vmax.
 At low concentrations of substrate ([S] << Km) enzyme is
predominantly in the E form.

 competitive inhibitor can combine with E so the presence of the


inhibitor decreases the velocity when substrate concentration is low.
Competitive Inhibition

Under competitive inhibition


Vmax remains unchanged ; Km increases
Uncompetitive Inhibition

 If inhibitor combines only with ES (and not E), inhibitor exerts its effect
only at high concentrations of substrate at which there is lots of ES around.

 This means that the increasing substrate concentration (S) doesn’t prevent
binding of the inhibitor.
 Km value is consistently smaller than Km value of the uninhibited reaction
which implies that S is more effectively bound to the enzyme in the
presence of the inhibitor.
 The sequence of this type of reaction is
 This type of inhibition is often observed for enzymes that catalyze the
reaction between two substrates.

 Often an inhibitor that is competitive against one of the substrates is found to


give uncompetitive inhibition when the other substrate is varied.

 The inhibitor does combine at active site but does not prevent binding of one
of the substrates (and vice versa).
 In this type of inhibition Vmax as well as Km both are decreased .

Uncompetitive Inhibition
Non-competitive Inhibition
Compounds that reversibly bind with either the enzyme or the
enzyme substrate complex are designed as noncompetitive
inhibitors and the following reaction describe these events.

Non competitive Inhibition


 Noncompetitive inhibition therefore differs from competitive
inhibition in that inhibitor can combine with ES, and S can
combine with EI to form in both instances EIS.

 This type of inhibition is not completely reversed by high


substrate concentration.

 Km is not altered but Vmax is decreased.

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