Table 1.
Kinetic and stability constants for GlTIM WT and double (Dmut) and triple (Tmut) mutants compared with GlTIM derivatized with methyl methanethiosulfonate (MMTS) and GlTIM tetramer. ND, not determined.
| Enzyme | Km (mM) | kcat (105 min−1) | kcat/Km (mM−1min−1) | Tmapp (°C) | Reference |
|---|---|---|---|---|---|
| GlTIM WT | 0.78 ± 0.06 | 4.6 ± 0.16 | 5.9 × 105 | 58 | This work |
| DMut C222A-C228A | 0.38 ± 0.03 | 3.78 ± 0.12 | 9.9 × 105 | 54.5 | This work |
| Tmut C202A-C222A-C228A | 1.2 ± 0.09 | 2.35 ± 0.14 | 1.15 × 105 | 55.9 | This work |
| GlTIM WT + MMTS | 0.97 ± 0.1 | 1.9 ± 0.08 | 1.96 × 105 | 54 | Enríquez-Flores, et al.19 |
| GlTIM tetramer | 0.87 ± 0.07 | 1.47 ± 0.04 | 1.69 × 105 | ND | López-Velázquez, et al.22 |
The data represent the mean of four independent experiments.