[in-i-bish-uhn, in-hi-]

In enzymology, a phenomenon in which a compound (an inhibitor), usually similar in structure to the substance on which an enzyme acts (substrate), interacts with the enzyme so that the resulting complex cannot undergo the usual reaction or cannot form the usual product. The inhibitor may function by combining with the enzyme at the site at which the reaction usually occurs (competitive inhibition) or at another site (noncompetitive inhibition). Seealso allosteric control, feedback inhibition, repression.

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Suppression of the activity of an enzyme by a product of the sequence of reactions in which the enzyme is participating. When the product accumulates in a cell beyond an optimal amount, it decreases its own production by inhibiting an enzyme involved in its synthesis. After the product has been used or broken down, inhibition is relaxed and formation of the product resumes. Enzymes whose ability to catalyze a reaction depends on molecules other than the substances on which they act directly are said to be under allosteric control.

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