Figure 1.

Determination of the K_i of compound 3 with the MsEH (2 nM) by using [³H]-1,3-diphenyl-trans-propene oxide as substrate (21). For each substrate concentration (2.5–50.0 μM), the velocity is plotted as a function of the inhibitor concentration (0–100 nM), allowing the determination of an apparent inhibition constant (K_iapp) (20). K_iapp values are plotted as a function of the substrate concentration (Inset). For [S] = 0, a K_i value of 26 nM is found. Similar plots were obtained with the human enzyme and 3 (K_i = 30 nM) and the murine enzyme and 20 (K_i = 3 nM).