Non-competitive inhibitors don't bind to the active sites of enzymes. However, in the presence of non-competitive inhibitors, the Michaelis-Menten constant is found to decrease. Why is this so?

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    $\begingroup$ The premise of the question is wrong. In MM kinetics, non-competitive inhibition does not change $K_M$. $\endgroup$
    – Curt F.
    Jun 23 '17 at 19:57

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