TABLE 6.
In vitro esterase activities
Esterase activity was measured from purified enzymes using pNPB and pNPA as test substrates. Km and Vmax values were calculated using Michaelis-Menten approximations. Data are mean values from three independent experiments with the respective S.D. values.
| Enzyme | Substrate | Vmax | Km |
|---|---|---|---|
| μmol/min/mg | mm | ||
| Lpx1p | pNPB | 3.76 ± 0.54 | 0.89 ± 0.13 |
| pNPA | 10.94 ± 0.98 | 2.50 ± 0.22 | |
| Ldh1p | pNPB | 0.90 ± 0.15 | 0.89 ± 0.15 |
| pNPA | 1.26 ± 0.18 | 1.78 ± 0.25 | |
| Ayr1p | pNPB | 14.06 ± 2.23 | 1.52 ± 0.24 |
| pNPA | 18.50 ± 2.76 | 3.50 ± 0.52 | |
| Eht1p | pNPB | 1.01 ± 0.14 | 0.88 ± 0.12 |
| pNPA | 3.44 ± 0.48 | 2.06 ± 0.29 | |
| Ybr056wp | pNPB | 1.439 ± 0.22 | 0.81 ± 0.12 |
| pNPA | 7.02 ± 1.26 | 3.51 ± 0.63 | |
| Control: GST tag | pNPB | 0.35 ± 0.05 | 0.37 ± 0.05 |