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|Vmax]] and K<sub | Uncompetitive inhibitors decrease both [[Vmax|Vmax]] and K<sub>m</sub><ref>T.Palmer,P.L.Bonner,(2007) Enzymes:Biochemistry,biotechnology,clinical chemistry, 2nd edition. Elsevier science and technology</ref>. The [[Vmax|V<sub>max</sub>]] decreases as the inhibitor prevents the enzyme-substrate complex from completing the reaction and releasing products. [[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. | ||
==== References ==== | ==== References ==== | ||
<references /> | <references /> | ||
Latest revision as of 16:37, 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.