Table 2.
Michaelis-Menten Kinetic Constants for Sudoxicam and Meloxicam Metabolites from Human Liver Microsome Reactions.
| Steady-state kinetic constants for individual metabolitesa | |||||||
|---|---|---|---|---|---|---|---|
| Substrate | Metabolite | Vmax1b | Km1 (μM) | Vmax/Km1 | Vmax2b | Km2 (μM) | Vmax/Km2 |
| sudoxicam | glyoxal | 13 ± 0.75 | 5.9 ± 1.2 | 2.2 | NA | NA | 0.021 c |
| meloxicam | methylglyoxal | 8.4 ± 0.39 | 26 ± 4.9 | 0.32 | NA | NA | NA |
| 5-hydroxymethyl-meloxicam | 29 ± 2.0 | 15 ± 2.9 | 1.9 | NA | NA | 0.014 c | |
| 34 ± 24d | 14 ± 9.5d | 2.4 | 140 ± 84d | 380 ± 55d | 0.37 | ||
Best fit models shown in Fig. 4 were determined using corrected Akaike information criterion. Values shown with standard error from mean.
Units are pmol/min/mg protein.
Efficiency estimated based on slope of linear function.
Data reported by others (Chesne et al., 1998).