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Consider a simple uni-substrate enzyme that follows Michaelis-Menten kinetics. When the enzyme catalyzed reaction was carried out in the presence of $10$ nM concentration of an inhibitor, there was no change in the maximal velocity. However. the slope of the Lineweaver-Burk plot increased $3$-fold. The dissociation constant for the enzyme-inhibitor complex (in nM) is ____________
in Biochemistry 1.4k points
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