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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 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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Effects of different types of inhibition on the double-reciprocal plot. When used for determining the type of enzyme inhibition, the Lineweaver–Burk plot can distinguish between competitive, pure non-competitive and uncompetitive inhibitors. The various modes of inhibition can be compared to the uninhibited reaction.
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This can be competitive inhibition, uncompetitive inhibition, non-competitive inhibition or partially competitive inhibition. If the molecule induces enzymes that are responsible for its own metabolism, this is called auto-induction (or auto-inhibition if there is inhibition).