Uncompetitive inhibitor
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Uncompetitive inhibition takes place when an enzyme inhibitor binds only to the complex formed between the enzyme and the substrate (the E-S complex).
This reduction in the effective concentration of the E-S complex increases the enzyme's apparent affinity for the substrate through Le Chatelier's principle (Km is lowered) and decreases the maximum enzyme activity (Vmax), as it takes longer for the substrate or product to leave the active site. Uncompetitive inhibition works best when substrate concentration is high. In addition to what is said, uncompetitive inhibitors binds themeselves to the allosteric site of the the enzyme, this will change the shape of the active site of the enzyme and stops the substrate from fitting into the active site properly. This inhibitor doesn't need the active site of the enzyme to function. The effect of this inhibitor is that is slows the rate of reactions down or totally stops the reaction.
Competitive inhibition - Uncompetitive inhibition - Non-competitive inhibition - Suicide inhibition - Mixed inhibition
Acetylcholinesterase inhibitors - Aromatase inhibitors - Carbonic anhydrase inhibitors - Kinase inhibitors - Monoamine oxidase inhibitors - Reverse transcriptase inhibitors - Phosphodiesterase inhibitors - Protease inhibitors
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