# GATE2018-53

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 ____________