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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]
Thus, in the presence of the inhibitor, the enzyme's effective K m and V max become (α/α')K m and (1/α')V max, respectively. However, the modified Michaelis-Menten equation assumes that binding of the inhibitor to the enzyme has reached equilibrium, which may be a very slow process for inhibitors with sub-nanomolar dissociation constants.
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 /, as pure noncompetitive inhibition does not effect substrate affinity.
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 ...
The reaction rate will either decrease to zero under complete inhibition, or it will decrease to a non-zero asymptote during partial inhibition. [3] This can be described by the Haldane (or Andrew) equation, [4] which is a common deviation of the Michaelis-Menten equation, and takes the following form:
a possible mechanism of non-competitive inhibition, a kind of mixed inhibition.. Mixed inhibition is a type of enzyme inhibition in which the inhibitor may bind to the enzyme whether or not the enzyme has already bound the substrate but has a greater affinity for one state or the other. [1]
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.
Intrinsic kinetic isotope values stem from the difference in the bond vibrational environment of an atom in the reactants at ground state to the environment of the atom's transition state. [3] Through the kinetic isotope effect much insight can be gained as to what the transition state looks like of an enzyme-catalyzed reaction and guide the ...