TABLE 2.
Kinetic constants of yeast esterase on different compounds functioning as substrates for the enzymea
| Substrate | Km (mM) | Vmax/mg of protein (U/mg) | kcat/Km (mol−1 s−1) |
|---|---|---|---|
| α-Naphthyl acetate | 0.86 | 19 | 1.5 × 104 |
| 4-Methylumbelliferyl acetate | 0.076 | 15 | 1.3 × 105 |
| p-Nitrophenyl acetate | 0.35 | 12 | 2.3 × 104 |
| Carboxyfluorescein diacetate | 0.056 | 15 | 1.8 × 105 |
| S-Formylglutathione | 0.88 | 220 | 1.7 × 105 |
Km and Vmax values for the substrates were determined with the most purified enzyme preparation. The kcat is Vmax/[E]T, where [E]T is the (total) concentration of the enzyme. Activities for S-formylglutathione were measured in 50 mM potassium phosphate (pH 7.0) at 30°C.