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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]
If the inhibitor is different from the substrate, then competitive inhibition will increase Km while Vmax remains the same, and non-competitive will decrease Vmax while Km remains the same. However, under substrate inhibiting effects where two of the same substrate molecules bind to the active sites and inhibitory sites, the reaction rate will ...
For example, an inhibitor might compete with substrate A for the first binding site, but be a non-competitive inhibitor with respect to substrate B in the second binding site. [26] Traditionally reversible enzyme inhibitors have been classified as competitive, uncompetitive, or non-competitive, according to their effects on K m and V max. [14]
The apparent unimolecular rate constant k cat is also called turnover number, and denotes the maximum number of enzymatic reactions catalysed per second. The Michaelis–Menten equation [10] describes how the (initial) reaction rate v 0 depends on the position of the substrate-binding equilibrium and the rate constant k 2.
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.
The Michaelis constant is defined as the concentration of substrate at which the reaction rate is half of . [6] Biochemical reactions involving a single substrate are often assumed to follow Michaelis–Menten kinetics, without regard to the model's underlying assumptions.
Analyzing through kinetics, fukugetin decreased the Vmax while it increased the Km for these KLKs. [5] Typically, in competitive inhibition, Vmax remains the same while Km increases, and in non-competitive inhibition, Vmax decreases while Km remains the same. The change in both of these variables is another finding consistent with the effects ...
In the field of biochemistry, the specificity constant (also called kinetic efficiency or /), is a measure of how efficiently an enzyme converts substrates into products. A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.e., substrate specificity).