Non-competitive inhibitor: Difference between revisions
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A non-competitive inhibitor binds to an [[ | A non-competitive inhibitor binds to an [[Enzyme|enzyme]] in another place other than its [[Active site|active site]]. This results in a change in the enzymes structure so that it is no longer complimentry to its [[Substrate|substrate]] and therefore reduces its [[Catalytic activity|catalytic activity]]. | ||
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The effects of a non-competitive inhibitor can be depicted by changes in its Michaelis-Menten graph: | |||
*'''K<sub>m</sub> is unaltered''' as the affinity with which substrates bind to the enzyme stays the same. | |||
*'''V<sub>max</sub> decreases''' because rate of reaction decreases due to the fact that as the reaction progresses, the concentration/amount of effective enzymes decreases. | |||
Revision as of 18:57, 3 December 2016
A non-competitive inhibitor binds to an enzyme in another place other than its active site. This results in a change in the enzymes structure so that it is no longer complimentry to its substrate and therefore reduces its catalytic activity.
The effects of a non-competitive inhibitor can be depicted by changes in its Michaelis-Menten graph:
- Km is unaltered as the affinity with which substrates bind to the enzyme stays the same.
- Vmax decreases because rate of reaction decreases due to the fact that as the reaction progresses, the concentration/amount of effective enzymes decreases.