Kinetic constants (derived from the curves in Figs. 5–8)
| Substrate | Enzyme Source | Vmax | Km, Ks, or S50 | Ksi | H | β | R2 |
|---|---|---|---|---|---|---|---|
| nmol · mg−1 · min−1 | μM | ||||||
| 4-MU | 1A9-XHCa | 7.5 ± 0.2 | 3.5 ± 0.3 | 220 ± 20 | 0.99 | ||
| 1A9-TLa | 3.7 ± 0.1 | 2.9 ± 0.2 | 261 ± 20 | 0.99 | |||
| 2B7-XHAb | 2.6 ± 0.1c | 381 ± 34 | 1.3 ± 0.1 | 0.99 | |||
| 2B7-TLb | 3.2 ± 0.1c | 293 ± 25 | 1.3 ± 0.1 | 0.99 | |||
| Entacapone | 1A9-XHCd | 84 ± 3 | 13.0 ± 1.0 | 0.30 ± 0.02 | 0.99 | ||
| 1A9-TLd | 40 ± 2 | 8.0 ± 0.9 | 0.30 ± 0.02 | 0.97 | |||
| HLMd | 51 ± 2 | 6.6 ± 0.5 | 0.27 ± 0.02 | 0.98 | |||
| AZT | 2B7-Hise | 0.07 ± 0.001c | 216 ± 10 | 0.99 | |||
| 2B7-XHAa | 0.33 ± 0.01c | 186 ± 3 | 0.99 | ||||
| 2B7-TLe | 0.37 ± 0.01c | 135 ± 4 | 0.99 | ||||
| HLMe | 0.64 ± 0.01 | 117 ± 4 | 0.99 | ||||
↵a Data were fitted to the Substrate inhibition model (eq. 2).
↵b Data were fitted to sigmoid kinetics (Hill equation) (eq. 3).
↵c Normalization of the Vmax values for relative expression level was only possible in part of the samples.
↵d Data were fitted to the two-sites inhibition model (eq. 4).
↵e Data were fitted to the Michaelis-Menten model (eq. 1).