TABLE 1.
VKOR in vitro reaction enzymatic parameters for human enzymes overexpressed in HEK 293T cells
| Enzyme | Substratea | Inhibitor | Kmb | Vmaxb | % Inhibitionc |
|---|---|---|---|---|---|
| μm | nmol·mg−1·h−1 | ||||
| VKORC1L1 | K1>O | 4.15 ± 0.10 | 2.57 ± 0.05 | 0 | |
| VKORC1L1 | K1>O, 50 μm | Warfarin, 5 μm | 29.2 ± 7.9 | ||
| VKORC1L1 | K2>O | 11.24 ± 0.23 | 13.46 ± 0.22 | 0 | |
| VKORC1 | K1>O | 1.88 ± 0.13 | 1.13 ± 0.03 | 0 | |
| VKORC1 | K1>O, 50 μm | Warfarin, 5 μm | 52.9 ± 6.6 | ||
| VKORC1 | K2>O | 1.55 ± 0.55 | 1.72 ± 0.10 | 0 |
a Range of K > O substrate concentrations: 1–16 μm; DTT-driven (5 μm) VKOR enzymatic reaction run under pseudo first-order conditions at maximum velocity for each substrate concentration.
b Apparent Km and Vmax mean values ± graphically determined error range of data scatter from Eisenthal & Cornish-Bowden direct linear plots.
c Values for % Inhibition are means ± S.E.