Uncompetitive inhibitors: Difference between revisions
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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,(2007) Enzymes:Biochemistry,biotechnology,clinical chemistry, 2nd edition. Elsevier science | 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 and 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.