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Summary of Enzyme Inhibition
1) Understand the definition of enzyme inhibition
 Enzyme inhibition is a decrease in velocity of the enzyme reaction in the presence of a second agent
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o WHERE they bind
 Competitive inhibitors bind the enzyme in the active site
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2) Know the difference between the three types of inhibition:
competitive, noncompetitive, mixed noncompetitive
 Competitive Inhibition kinetics
o Km = changed
Vmax = unchanged
o Explanation: As substrate concentration increases, it
outcompetes the inhibitor for the active site and allows
the reaction to reach maximum velocity
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[Illustration: A beaker of enzyme that is
surrounded by much more substrate than inhibitor will
continue to react at the same rate]
o Additional notes: inhibitor often has similar characteristics to the substrate
 Non-competitive Inhibition kinetics
o Km = unchanged
Vmax = changed
o Explanation: As the inhibitor binds the enzyme, it
prevents the catalysis of the reaction without interfering
with the substrate
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(Illustration: Putting factory
workers on a break will slow down overall production,
Km
but the individuals will still work at the same pace]
 Mixed Non-competitive Inhibition kinetics (Figures below)
o K m = changed
Vmax = changed
o Explanation: Binding of the inhibitor at a secondary site prevents catalysis of the reaction AND interferes
with substrate binding at the active site
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e
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o Additional notes: more common type of inhibition



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