Table 1.
Parameters for ht-ADH mutants at 30 °C.
| Mutant |
kcat, s−1a |
Km(NAD+)a | Km(Alcohol)a | Dkcata | pKa |
kcat optimum s−1b |
|---|---|---|---|---|---|---|
| WT | 25 (±3) | 1.1 (±0.1) | 6.8 (±0.5) | 3.1 (±0.2) | 7.0 (±0.1) | 50 (±1) |
| L176V | 1.7 (±0.1) | 1.2 (±0.2) | 5.3 (±0.9) | 4.1 (±0.4) | 8.2 (±0.2) | 16 (±1) |
| L176A | 2.8 (±0.3) | 2.6 (±0.6) | 5.8 (±1.5) | 4.1 (±0.6) | 7.9 (±0.4) | 13 (±1) |
| L176G | 7.7 (±1.4) | 25 (±8) | 9.8 (±3.4) | 4.0 (±1.1) | 7.3(±0.2) | 22 (±1) |
| L176Δ | 0.43 (±0.1) | 37 (±14) | 7.4 (±3.5) | 4.4 (±1.4) | 7.6 (±0.8) | 1.8 (±0.2) |
| V260A | 2.4 (±0.2) | 10 (±1.6) | 4.2 (±0.8) | 4.1 (±0.4) | 7.8 (±0.1) | 20 (±1) |
a
At pH 7.0.
b
This is the value of kcat estimated in the limit of fully ionized enzyme.