Kinetic constants for enzymatic hydrolysis of d- and l-methylphenidate (d-MP and l-MP)
The values of kinetic constants were reported as mean ± standard error. Two individual sets of data were reported for each enzymatic reaction. The standard error of each constant was less than 14% of the mean value.
Enzyme | kcat | Km | kcat/Km | |
|---|---|---|---|---|
| min-1 | μM | mM-1 min-1 | ||
| CES1A1 (native) | l-MP | 0.34 ± 0.02 | 43.8 ± 5.8 | 7.7 ± 0.7 |
| 0.28 ± 0.01 | 40.1 ± 5.4 | 7.0 ± 0.7 | ||
| d-MP | 0.19 ± 0.01 | 89.9 ± 6.6 | 2.1 ± 0.1 | |
| 0.18 ± 0.01 | 80.0 ± 5.8 | 2.3 ± 0.1 | ||
| CES1A1 (recombinant) | l-MP | 0.31 ± 0.01 | 40.1 ± 5.4 | 7.8 ± 0.8 |
| 0.36 ± 0.02 | 47.1 ± 5.6 | 7.6 ± 0.6 | ||
| d-MP | 0.16 ± 0.01 | 126.2 ± 12.0 | 1.3 ± 0.1 | |
| 0.17 ± 0.01 | 110.4 ± 11.3 | 1.6 ± 0.1 | ||
| CES2 (native and recombinant) | l-, d-MP | 0 | 0 | |
| CES3 (recombinant) | l-, d-MP | 0 |
| 0 |