Uncompetitive inhibitors: Difference between revisions
Jump to navigation
Jump to search
Added some links |
Reformatted the page. |
||
| Line 1: | Line 1: | ||
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 [[ | They are similar to a [[Non-competitive inhibitor|non-competitive inhibitor]], as they utilise a binding site away from the [[Enzyme active site|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. | ||
< | ==== Effect on V<sub>max</sub> and K<sub>m</sub> ==== | ||
== | Uncompetitive inhibitors decrease both [[Vmax|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>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 / | |||
Revision as of 16:36, 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.