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Competitive inhibition can be overcome by adding more substrate to the reaction, which increases the chances of the enzyme and substrate binding. As a result, competitive inhibition alters only the K m, leaving the V max the same. [3] This can be demonstrated using enzyme kinetics plots such as the Michaelis–Menten or the Lineweaver-Burk plot.
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Allosteric competitive inhibition by an inhibitor that, when bound to the enzyme's allosteric site, physically blocks access to the active site. Date: 29 October 2010, 22:52 (UTC) Source: Comp inhib.svg: Author: Comp inhib.svg: *SVG version:Srhat (talk · contribs) PNG version:Jerry Crimson Mann at en.wikipedia
Allosteric competitive inhibition by reciprocal induction of conformational changes. Binding of subsrate at active site induces a conformational change in the allosteric site and vice versa. Date: 29 October 2010, 22:56 (UTC) Source: Comp_inhib.svg; Author: Comp_inhib.svg: *SVG version:Srhat (talk · contribs) PNG version:Jerry Crimson Mann at ...
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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 active site, competing with the substrate.
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Image:Competitive inhibition.svg, which is a vector version of Image:Competitive inhibition.png: Author: Authored by Jerry Crimson Mann, modified by TimVickers, vectorized by Fvasconcellos and made into international version by myself (User:PatríciaR: Permission (Reusing this file)