Uncompetitive inhibitors

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(Created page with "Uncompetitive inhibitors are one of three reversible enzyme inhibitors. They are similar to a [[Non-competitive inhibitor|non-com...")
 
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Uncompetitive [[Enzyme Inhibitors|inhibitors]] are one of three [[Reversible inhibitor|reversible]] enzyme inhibitors.  
 
Uncompetitive [[Enzyme Inhibitors|inhibitors]] are one of three [[Reversible inhibitor|reversible]] enzyme inhibitors.  
  
They are similar to a [[Non-competitive inhibitor|non-competitive inhibitor]], as they utilise a binding site away from the enzyme active site, but uncompetitive inhibitors only bind to an [[Enzyme-substrate complex|enzyme-substrate complex]]<ref>V.Leskovac. Comprehensive enzyme kinetics. New York:Kluwer academic/Plenum Publishers,2003</ref>, rather than free enzymes.  
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They are similar to a [[Non-competitive inhibitor|non-competitive inhibitor]], as they utilise a binding site away from the enzyme active site, but uncompetitive inhibitors only bind to an [[Enzyme-substrate complex|enzyme-substrate complex]]<ref>V.Leskovac,(2003) Comprehensive enzyme kinetics. New York:Kluwer academic/Plenum Publishers</ref>, rather than free enzymes.  
  
 
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==== '''Effect on V<sub>max</sub> and K<sub>m</sub>'''  ====
 
==== '''Effect on V<sub>max</sub> and K<sub>m</sub>'''  ====
  
Uncompetitive inhibitors decrease both Vmax and K<sub><span style="font-size: 11.0667px;">m<ref>T.Palmer,P.L.Bonner.Enzymes:Biochemistry,biotechnology,clinical chemistry.2nd.Elsevier science &amp;amp;amp;amp; technology,2007</ref></span></sub><span style="font-size: 11.0667px;">.</span><br>The [[Vmax|V<sub>max</sub>]] decreases as the inhibitor prevents the enzyme-substrate complex from completing the reaction and releasing products.<br>[[Michaelis constant|K<sub>m</sub>]] decreases due to the enzyme-substrate complex being unable to dissociate, which increases the enzyme's affinity for the substrate.  
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Uncompetitive inhibitors decrease both Vmax and K<sub><span style="font-size: 11.0667px;">m<ref>T.Palmer,P.L.Bonner,(2007) Enzymes:Biochemistry,biotechnology,clinical chemistry, 2nd edition. Elsevier science &amp;amp;amp; technology</ref></span></sub><span style="font-size: 11.0667px;">.</span><br>The [[Vmax|V<sub>max</sub>]] decreases as the inhibitor prevents the enzyme-substrate complex from completing the reaction and releasing products.<br>[[Michaelis constant|K<sub>m</sub>]] decreases due to the enzyme-substrate complex being unable to dissociate, which increases the enzyme's affinity for the substrate.  
  
 
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Revision as of 10:44, 4 December 2017

Uncompetitive inhibitors are one of three reversible enzyme inhibitors.

They are similar to a non-competitive inhibitor, as they utilise a binding site away from the enzyme active site, but uncompetitive inhibitors only bind to an enzyme-substrate complex[1], rather than free enzymes.


Effect on Vmax and Km

Uncompetitive inhibitors decrease both Vmax and Km[2].
The Vmax decreases as the inhibitor prevents the enzyme-substrate complex from completing the reaction and releasing products.
Km decreases due to the enzyme-substrate complex being unable to dissociate, which increases the enzyme's affinity for the substrate.


References

  1. V.Leskovac,(2003) Comprehensive enzyme kinetics. New York:Kluwer academic/Plenum Publishers
  2. T.Palmer,P.L.Bonner,(2007) Enzymes:Biochemistry,biotechnology,clinical chemistry, 2nd edition. Elsevier science &amp;amp; technology

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