TABLE 2.
Comparison of the kinetic parameters of various trehalases using trehalose as the substratea
| Organism | GH family | kcat (s−1) | Km (mM) | kcat/Km (s−1 mM−1) | Temp (°C), pH |
|---|---|---|---|---|---|
| T. volcanium | 15 | 63.0 | 48.7 | 1.29 | 50, 3.7 |
| T. acidophilum | 15 | 66.7 | 40.2 | 1.66 | 50, 3.7 |
| M. smegmatis | 15 | NDb | 20.0 | NDb | 37, 7.1 |
| E. coli (cytoplasmic) | 37 | 57.6c | 1.9 | 30.3 | 30, 5.5 |
| E. coli (periplasmic) | 37 | 84.1c | 0.8 | 105 | 30, 5.5 |
| S. cerevisiae (acidic) | 65 | 67.7c | 4.7 | 14.4 | 37, 4.5 |
| S. cerevisiae (neutral) | 37 | 148c | 34.5 | 4.29 | 37, 7.0 |
a
The kinetic parameters of various trehalases and the conditions for activity measurements were obtained for T. volcanium and T. acidophilum (this study), M. smegmatis (12), E. coli (cytoplasmic) (8), E. coli (periplasmic) (49), S. cerevisiae (acidic) (50), and S. cerevisiae (neutral) (51).
b
ND, not determined.
c
The values were estimated from the Vmax for each enzyme based on its monomeric molecular mass.