Table II. Kinetics parameters of r-PAPhy enzymes.
The specific activities were determined at 36°C, pH 5.0. r-TaPAPhy_b1 and phytate were used for reference. All data were determined in triplicate.
| Substrate and Protein | Km | Vmax | kcat | kcat/Km |
| μm | μmol min−1 mg−1 | s−1 | ×104 s−1m−1 | |
| Phytate | ||||
| r-TaPAPhy_a1 | 35 ± 6.8 | 223 ± 9.4 | 279 | 796 |
| r-TaPAPhy_b1 | 45 ± 3.4 | 216 ± 12.4 | 270 | 600 |
| r-HvPAPhy_a | 36 ± 4.2 | 208 ± 6.8 | 260 | 722 |
| r-HvPAPhy_b2 | 46 ± 7.3 | 202 ± 9.9 | 253 | 550 |
| r-ZmPAPhy_b | 48 ± 6.9 | 198 ± 13.5 | 248 | 517 |
| r-OsPAPhy_b | 54 ± 8.2 | 185 ± 11.7 | 231 | 428 |
| r-TaPAPhy_b1 | ||||
| p-NPP | 1,917 ± 32.5 | 496 ± 11.0 | 620 | 32.34 |
| Fru-1,6-bisP | 921 ± 21.8 | 36 ± 3.5 | 45 | 4.89 |
| Phosphoenolpyruvate | 1,793 ± 33.4 | 256 ± 8.4 | 320 | 17.85 |
| Glycerol-1-phosphate | 1,650 ± 42.1 | 653 ± 14.3 | 816 | 49.47 |
| Pyrophosphate | 343 ± 12.8 | 22 ± 3.1 | 28 | 8.13 |
| Glc-6-P | 2,675 ± 64.3 | 22 ± 7.2 | 28 | 1.04 |
| Fru-1-P | 2,314 ± 54.7 | 24 ± 4.4 | 31 | 1.33 |
| Phospho-Ser | 2,560 ± 48.2 | 15 ± 2.2 | 19 | 0.75 |
| Adenosine triphosphate | 1,046 ± 132.3 | 111 ± 4.2 | 139 | 13.26 |
| Adenosine diphosphate | 1,377 ± 142 | 66 ± 3.2 | 83 | 6.03 |
| r-TaPAPhy_b1, phytate control | 100% | |||
| Pyridoxal-5-phosphate | 6% ± 1.2% | |||
| ortho-Carboxyphenyl phosphate | 45% ± 4.6% | |||
| Naphthyl phosphate | 68% ± 7.4% | |||
| Adenosine monophosphate | 11% ± 2.6% | |||
| Guanosine triphosphate | 210% ± 7% | |||
| Fru-6-P | Not detectable |