What are enzyme inhibitors (competitive and non-competitive)?
Inhibit the enzymes function thus becomes inactive or reduces its efficiency.
Competitive inhibitors are molecules which are very similar to the enzymes natural substrate, and thus compete for the active site. As a result, the the inhibitor binds to the active site and remains their, preventing further reactions.
The enzyme may react with the inhibitor and release the products as it would usually do to its substrate, thus the inhibitor and substrate compete for the active site.
Non-Competitive inhibitors bind to an allosteric site of the enzyme (A site on the enzyme which is not the active one). This results in a conformational change of the protein, distorting the active site and thus is unable to bind the substrate. So long as the non-competitive inhibitor is bound, the enzyme remains inactive.
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Enzyme inhibitors are molecules that hinder enzyme activity. Competitive inhibitors compete for the active site, while non-competitive inhibitors bind elsewhere, altering the enzyme's shape.
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When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.
When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.
When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.
When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.

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