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e) a noncompetitive inhibitor
Wed, 27 Aug 2008 04:00:41 GMT
e) a noncompetitive inhibitor Non-competitive inhibition differs from competitive inhibition in that the inhibitor always binds to the enzyme at a site other than the enzyme's active site (this other site is called an allosteric site). This affects the rate of the reaction catalysed by the enzyme because the presence of the inhibitor causes a change in the structure and shape of the enzyme.
change in shape means the enzyme is no longer able to bind with a substrate correctly (Lock and Key Hypothesis). This reduces the concentration of 'active' enzyme resulting in a decrease in the Vmax. In this mode of inhibition, there is no competition between the inhibitor and the substrate, so increasing the concentration of the substrate still does not allow the maximum enzyme activity rate to be reached.
change in shape means the enzyme is no longer able to bind with a substrate correctly (Lock and Key Hypothesis). This reduces the concentration of 'active' enzyme resulting in a decrease in the Vmax. In this mode of inhibition, there is no competition between the inhibitor and the substrate, so increasing the concentration of the substrate still does not allow the maximum enzyme activity rate to be reached.
Wed, 27 Aug 2008 04:04:24 GMT
product molecules
Wed, 27 Aug 2008 04:04:49 GMT
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