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A competitive inhibition and allosteric regulation both involves an inhibitor molecule binding to the enzyme at a different area. The difference between the two is that allosteric inhibitors are modulator molecules which bind somewhere besides the catalytic activity.

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Compare competitive and noncompetitive inhibition and how it affects enzyme function?

Competitive inhibition occurs when an inhibitor molecule competes with the substrate for binding to the active site of an enzyme, effectively reducing the enzyme's activity. In this case, increasing substrate concentration can overcome the inhibition. Noncompetitive inhibition, on the other hand, involves an inhibitor binding to a site other than the active site, altering the enzyme's shape and function regardless of substrate concentration. As a result, noncompetitive inhibition cannot be reversed by increasing substrate levels, leading to a decrease in the maximum reaction rate of the enzyme.


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