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Consider a simple uni-substrate enzyme that follows Michaelis-Menten kinetics. When theenzyme catalyzed reaction was carried out in the presence of 10 nM concentration of aninhibitor. there was no change in the maximal velocity. However. the slope of theLineweaver-Blu'k plot increased 3-fold. The dissociation constant for the enzyme-inhibitorcomplex (in nM) is

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