Table 1.
Steady-state kinetic parameters for selected proteins
| UniProt | Protein name | Substrate | kcat, s−1 | Km, μM | kcat/Km, s−1⋅M−1 |
| H0QCK5 | Putative β-PGM | β-Glucose 1,6-BP | 1.3 ± 0.1 | 11 ± 1 | 1.2 × 106 |
| Q7M7U5 | Putative serB | Phosphoserine | 40 ± 3 | 250 ± 30 | 1.6 × 105 |
| R4UY31 | Putative serB | Phosphoserine | 40 ± 1 | 250 ± 9 | 1.6 × 105 |
| Q9K8N3 | BH2972 protein | Phosphoserine | 50 ± 1 | 1,800 ± 80 | 2.8 × 104 |
| Phosphothreonine | 40 ± 3 | 3,500 ± 80 | 1.1 × 104 | ||
| X3MFA4 | Hydrolase | Phosphoserine | 160 ± 10 | 30 ± 1 | 5.1 × 106 |
| Phosphothreonine | 40 ± 5 | 520 ± 10 | 7.3 × 104 | ||
| C3NVP9 | Phosphoserine phosphatase | Phosphoserine | 160 ± 2 | 440 ± 20 | 3.6 × 105 |
| Phosphothreonine | 640 ± 120 | 21,700 ± 6,600 | 3.0 × 104 | ||
| Q81IN0 | Putative phosphoglycolate phosphatase* | Phosphocholine | 3.1 ± 0.3 | 390 ± 100 | 7.9 × 103 |
| Q8A9J5 | Hypothetical protein | O-phosphotyrosine | 74 ± 5 | 230 ± 20 | 3.2 × 105 |
| Q926W0 | Hypothetical protein | l-xylitol 5-P | 0.130 ± 0.004 | 120 ± 20 | 1.1 × 105 |
| d-mannitol 6-P | 4.0 ± 0.5 | 1,500 ± 600 | 2.7 × 103 | ||
| d-mannitol 1-P | 0.56 ± 0.05 | 290 ± 70 | 1.9 × 103 | ||
| d-allitol 6-P | 0.300 ± 0.001 | 170 ± 30 | 1.7 × 103 | ||
| 2′-deoxy 6-phosphoglucitol | 0.9 ± 0.1 | 800 ± 200 | 1.1 × 103 |
*
This enzyme did not catalyze hydrolysis of phosphoglycolate; data shown are the result of three measurements, error is the SD.