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Answer Posted / swetha
In noncompetitive inhibition, the inhibitor works by
occupying some other site on the enzyme, as in non-
classical competitive inhibition. In this case, the enzyme
will bind with the inhibitor creating an E-I complex. The
substrate will still be allowed to bind to the enzyme, thus
creating an E-I-S complexe thereafter. The reaction will
still take place when the inhibitor leaves the enzyme, but
the speed will be decreased. The Michaelis-Menten constant,
Km, which is a measure of the substrate's affinity for the
site will remain the same, even though the maximum speed of
the reaction decreases. 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.
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