Non-competitive inhibitor: Difference between revisions

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[[Image:Enzyme inhibitors.gif|right|Michael-Menten Graph depicting effects of competitive and non-competitive enzyme inhibitors.]] 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]].   
[[Image:Enzyme inhibitors.gif|right|Michael-Menten Graph depicting effects of competitive and non-competitive enzyme inhibitors.]] 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 structure of the enzyme so that it is no longer complementary to its [[Substrate|substrate]] and therefore reduces its [[Catalytic activity|catalytic activity]].   


The effects of a non-competitive inhibitor can be depicted by changes in its [[Michaelis-Menten constant|Michaelis-Menten]] graph<ref>Berg JM, Tymoczko JL, Gatto GJJ, Stayer L. Biochemistry. Eight Edition. New York: W. H. Freeman and Company; 2015</ref>:  
The effects of a non-competitive inhibitor can be depicted by changes in its [[Michaelis-Menten constant|Michaelis-Menten]] graph<ref>Berg JM, Tymoczko JL, Gatto GJJ, Stayer L. Biochemistry. Eight Edition. New York: W. H. Freeman and Company; 2015</ref>:  
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=== References  ===
=== References  ===


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Latest revision as of 07:21, 20 October 2018

Michael-Menten Graph depicting effects of competitive and non-competitive enzyme inhibitors.
Michael-Menten Graph depicting effects of competitive and non-competitive enzyme inhibitors.

A non-competitive inhibitor binds to an enzyme in another place other than its active site. This results in a change in the structure of the enzyme so that it is no longer complementary 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[1]:

  • 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. 

References

  1. ↑ Berg JM, Tymoczko JL, Gatto GJJ, Stayer L. Biochemistry. Eight Edition. New York: W. H. Freeman and Company; 2015
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