A competitive inhibitor physically mimics the substrate for a specific enzyme and engages in binding competition with the substrate at the enzyme's active site.
A noncompetitive inhibitor can bind to either the free enzyme or the enzyme-substrate complex and binds at a location different from the active site.
<h3>What are inhibitors that are competitive and noncompetitive? How do they function?</h3>
The substrate cannot attach to the active site because the competitive inhibitor is bound there. The noncompetitive inhibitor attaches to a different spot on the enzyme.
The inhibitor binds at an allosteric location apart from the active site of substrate binding in noncompetitive inhibition. Therefore, in noncompetitive inhibition, the inhibitor can attach to its target enzyme even if a bound substrate is present.
Inhibitors that are non-competitive can bind to both the enzyme and the enzyme-substrate complex. Uncompetitive inhibitors only bind to the complex of the enzyme and substrate.
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