Steady-state kinetics data for the determination of K_i for 15-LOX-2 with MLS000536924.

(A) Initial enzymatic rate (µmol/min/mg) versus substrate concentration (µM) at inhibitor concentrations of 0 µM (open circles) 1 µM (open squares) 2 µM (open diamonds) and 5 µM (closed circles) fitted to the Henri–Michaelis– Menten equation to yield V_max (µmol/min/mg) and V_max/K_M (µmol/min/mg/µM). All measurements were done in triplicate. (B) K_M/V_max replot (closed circles) (units are µM/µmol/min/mg) versus [Inhibitor] (µM), which yielded a K_i of 2.5+/−0.5 µM. 1/V_max replot (open circles) (units are 1/µmol/min/mg) versus [Inhibitor] (µM), value did not change with increasing inhibitor concentration, indicating competitive inhibition.