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, rather than free enzymes.
Effect on Vmax and Km
Uncompetitive inhibitors decrease both Vmax and Km.
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.
- ↑ V.Leskovac. Comprehensive enzyme kinetics. New York:Kluwer academic/Plenum Publishers,2003
- ↑ T.Palmer,P.L.Bonner.Enzymes:Biochemistry,biotechnology,clinical chemistry.2nd.Elsevier science &amp;amp; technology,2007