Kinetic parameters for Ylehd under steady-state conditionsa.
| Compounds | Binding energy from docking studies (kJ mol−1) | k 303 K (μM−1 s−1) | K m (mM) | k cat b (s−1) | k cat/Km (mM−1 s−1) | E c |
|---|---|---|---|---|---|---|
| rac-PGE | −25.73 | 17.3 + 0.82 | 0.6 ± 0.009 | 7.34 ± 0.06 | 12.2 ± 0.78 | 1.5 |
| (R)-PGE | −26.27 | 28.11 + 0.73 | 1.32 ± 0.045 | 33.79 ± 0.87 | 25.5 ± 0.97 | |
| (S)-PGE | −25.77 | 21.9 + 1.05 | 0.93 ± 0.071 | 15.66 ± 0.49 | 16.6 ± 0.057 | |
| rac-BGE | −26.36 | 21.3 + 0.08 | 0.15 ± 0.002 | 5.73 ± 0.54 | 38.2 ± 1.08 | 10.37 |
| (R)-BGE | −27.15 | 18.2 + 0.47 | 0.8 ± 0.01 | 3.45 ± 0.089 | 4.31 ± 0.07 | |
| (S)-BGE | −28.41 | 31.1 + 0.97 | 0.27 ± 0.024 | 12 ± 0.97 | 44.7 ± 0.87 |
Kinetic constants calculated by non-linear regression analysis in Microcal Origin.
Kinetic studies for all compounds were carried out with 2 μg protein except for (R)-BGE wherein 10 μg protein was used.
Enantiomeric ratio (E) was calculated as ratio of kcat/Km of the fast-acting enantiomer over the slow acting one.