TABLE 3.
Kinetic parameters of purified EstA on p-NP esters of fatty acidsa
| p-NP ester substrate | Km (mM) | Vmax (μmol min−1 mg of protein−1) |
|---|---|---|
| p-NP-ethanoate | 0.87 | 170 |
| p-NP-butanoate | 3.39 | 531 |
| p-NP-hexanoate | 0.09 | 332 |
| p-NP-octanoate | 0.06 | 297 |
| p-NP-decanoate | 0.01 | 75 |
| p-NP-dodecanoate | 0.01 | 26 |
| p-NP-tetradecanoate | — | — |
| p-NP-hexadecanoate | — | — |
a
Km and Vmax were calculated from Lineweaver-Burk plots of enzyme activity on p-NP ester substrates by using a least-squares best fit of the Michaelis-Menten equation. —, no enzyme activity.