TABLE 1. Comparison of kinetic constants for EAH and HPO hydroxylases.
Constants were calculated by nonlinear regression fits to the Michaelis-Menten equation.
| Enzyme | Substrate | Product | Km | kcat | kcat/Km |
|---|---|---|---|---|---|
| µm | S−1 | ||||
| EAHa | EA | Capsidiol | 19.2 ± 2.9 | 0.5 ± 0.04 | 0.03 |
| 1β-(OH)EA | Capsidiol | 1.7 ± 0.1 | 0.6 ± 0.01 | 0.35 | |
| HPO | PSD | Solavetivol | 14.0 ± 1.9 | 2.1 ± 0.10 | 0.15 |
| PSD | Solavetivone | 1.7 ± 0.2 | 0.1 ± 0.01 | 0.06 | |
| Solavetivol | Solavetivone | 1.2 ± 0.1 | 0.1 ± 0.01 | 0.08 | |
| Valencene | α-Nootkatol | 11.5 ± 1.9 | 0.1 ± 0.01 | 0.01 | |
| Valencene | β-Nootkatol | 7.4 ± 1.2 | 1.9 ± 0.07 | 0.26 | |
| EA | 2β-(OH)EA | 3.3 ± 0.3 | 0.2 ± 0.01 | 0.06 | |
| EE | 2β-(OH)EE | 7.8 ± 1.0 | 0.8 ± 0.03 | 0.10 | |
| Cedr-8-ene | Cedr-8-en-15-ol | 26.5 ± 1.1 | 0.1 ± 0.01 | 0.00 | |
a
EAH kinetic data are from Takahashi et al. (15); EA, 5-epi-aristolochene; PSD, premnaspirodiene; EE, epi-eremophilene.