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 _________

Answer 1

First figure out moles of enzyme: 1 mg = 0.001g / 120 kiloDa per mole = 8.3 X 10-6 moles per mg enzyme Then figure out moles of active site, since there are 6 per enzyme.

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