Enzyme Inhibition Kinetics

The rate of substrate disappearance depends on the substrate and inhibitor concentrations as well as the parameters , , and . The Lineweaver–Burk plot of versus () is a straight line (except for the self-inhibited case). Increasing the inhibitor concentration increases the intercept for competitive inhibition (with slope not changing), but increases the slope for uncompetitive inhibition leaves the intercept unchanged. Increasing the inhibitor concentration increases both the slope and intercept for noncompetitive or mixed inhibition. The effect of changing inhibitor concentration can also be seen on the Michaelis–Menten plot, which plots versus (). When a reaction is self inhibiting, the substrate concentration (-axis) is the inhibitor concentration, so the slider is disabled.


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Reaction Pathways
values come from respective reaction coefficients
represents the concentration of an enzyme-substrate complex
represents the concentration of an enzyme-inhibitor complex
represents the concentration of an enzyme-inhibitor-substrate complex
is the total enzyme concentration
Competitive: Inhibitor competes with substrate for enzyme to form an inactive complex
(4) (inactive)
Uncompetitive (Anti-Competitive) Inhibition: The inhibitor binds to the enzyme-substrate complex forming an inhibitor-enzyme-substrate complex
(4) (inactive)
Noncompetitive Inhibition (Mixed Inhibition): Mixed inhibition is most commonly seen for enzymes with two or more substrates. The inhibitor can bind to the enzyme or enzyme-substrate complex. The substrate can also bind to the inhibitor-enzyme complex.
(2) (inactive)
(4) (inactive)
(5) (inactive)
Substrate Inhibition: In the case of uncompetitive inhibition, the inhibitor ties up the enzyme-substrate complex to form an inactive substrate-enzyme-substrate complex.
(4) (inactive)
[1] H. S. Fogler, Essentials of Chemical Reaction Engineering, 1st ed., Upper Saddle River, NJ: Pearson Higher Education, 2010 pp. 364–370.
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