Practice question

Question

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 _________