Use of inhibitors in elucidating the mechanism of an enzyme
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An irreversible inhibitor covalently binds to the enzyme’s active site, producing a permanent loss in catalytic efficiency even if we decrease the inhibitor’s concentration.
For example, an increase in slope, a decrease in the Linweaver–Burk plots for competitive inhibition, noncompetitive inhibition, and uncompetitive inhibition.The data in this exercise are adapted from jkimball.Your access to the NCBI website at gov has been temporarily blocked due to a possible misuse/abuse situation involving your site.On the other hand, in noncompetitive inhibition, an inhibitor molecule binds to the enzyme in a location other than an allosteric site and still manages to block substrate binding to the active site.When an inhibitor interacts with an enzyme it decreases the enzyme’s catalytic efficiency.
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