Difference between competitive inhibitors and non-competitive inhibitors?
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A competitive inhibitor will block the enzyme's active site (ie: it will occupy the same space as the natural substrate, blocking it from being catalyzed). A non-competitive inhibitor will bind to the enzyme somewhere other than the active site of the enzyme; an allosteric site.
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A competitive inhibitor will block the enzyme's active site (ie: it will occupy the same space as the natural substrate, blocking it from being catalyzed). A non-competitive inhibitor will bind to the enzyme somewhere other than the active site of the enzyme; an allosteric site.
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Explanation:
competitive inhibitor.
- *Competitive inhibitors Increase km value without increasing vmax
- These resemble the normal substrate, these are attached with the active site of enzyme, so take part to reduce the function.
- if the reaction is reversible it can be controlled by increasing the conc of substrate
Non competitive inhibitor.
- When certain substances are attached to a part of enzyme, away from active site (attach to the allosteric position ).
- Due to the non active attack, it will decrease vmax without affecting the k value (Substrate binding capacity )
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