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I believe non competitive antagonists bind to an allosteric site that prevents the enzyme from binding substrate whereas uncompetitive binds and stabilizes the ES complex which slows down the reaction.

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Q: What is Difference between uncompetitive and non competitive enzyme inhibition?
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How do allosteric regulation and competitive inhibition compare?

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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In a mixed inhibition scenario, as the concentration of the inhibitor increases, the Lineweaver-Burk (LB) plot takes on a distinctive pattern. Unlike uncompetitive or competitive inhibition, mixed inhibition involves the inhibitor binding to both the enzyme-substrate complex and the free enzyme, affecting the reaction kinetics. As the inhibitor concentration rises, the LB plot displays converging lines, indicating that the apparent affinity of the enzyme for the substrate diminishes. This convergence suggests that the inhibitor alters both the enzyme's active form and its substrate-bound configuration. The LB plot, in this context, serves as a visual representation of how the inhibitor impacts the enzyme's catalytic activity, offering insights into the complex interplay between substrates, enzymes, and inhibitors at varying concentrations.


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