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The Michaelis-Menten equation describes the rate of enzymatic reactions by relating the reaction velocity to substrate concentration. For a non-competitive inhibitor, the inhibitor binds to an allosteric site on the enzyme, not the active site, which means it can bind both to the free enzyme (E) and the enzyme-substrate complex (ES) without affecting substrate binding, but it decreases the overall catalytic activity. The basic reaction scheme in the presence of a non-competitive inhibitor (I) can be represented as: E + S _________ ______ _____ ___ ________ ___ __________ _______ _______ _____ _______.
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