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When a non-competitive inhibitor is added the Vmax is changed, while the Km remains unchanged. According to the Lineweaver-Burk plot the Vmax is reduced during the addition of a non-competitive inhibitor, which is shown in the plot by a change in both the slope and y-intercept when a non-competitive inhibitor is added. [8]
Non-competitive inhibition does not change K m (i.e., it does not affect substrate binding) but decreases V max (i.e., inhibitor binding hampers catalysis). [24]: 97 Mixed-type inhibitors bind to both E and ES, but their affinities for these two forms of the enzyme are different (K i ≠ K i ').
Uncompetitive inhibition (which Laidler and Bunting preferred to call anti-competitive inhibition, [1] but this term has not been widely adopted) is a type of inhibition in which the apparent values of the Michaelis–Menten parameters and are decreased in the same proportion.
On the other hand, the V max will decrease relative to an uninhibited enzyme. On a Lineweaver-Burk plot, the presence of a noncompetitive inhibitor is illustrated by a change in the y-intercept, defined as 1/V max. The x-intercept, defined as −1/K M, will remain the same. In competitive inhibition, the inhibitor will bind to an enzyme at the ...
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With pure noncompetitive inhibition the apparent value of is decreased. This can be seen on the Lineweaver–Burk plot as an increased ordinate intercept with no effect on the abscissa intercept − 1 / K m {\displaystyle -1/K_{\mathrm {m} }} , as pure noncompetitive inhibition does not effect substrate affinity.
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