| Origin | recombinant E. coli |
|---|---|
| Lineage name | Sucrose : orthophosphate α-D-glucosyltransferase |
| EC Number | 2.4.1.7 |
| Reaction formula | Sucrose + Orthophosphate →→→ D-Fructose + α-D-Glucose 1-phosphate |
SPECIFICATION
| Appearance | white lyophilizate | |
|---|---|---|
| Activity | ≧50 U/mg lyophilizate | |
| Contaminants | NADH oxidase ≦5.0×10-4% | |
| 6-phosphogluconate dehydrogenase ≦5.0×10-4% | ||
| Stabilizer | sucrose | |
| Storage | at-20℃ |
PROPERTIES
| Molecular weight | ca. 56 kDa (gel filtration) |
|---|---|
| Structure | monomer of 56 kDa (SDS-PAGE) |
| Isoelectric point | 4.6 |
| Michaelis constant | 3.9×10-2M (sucrose) |
| 6.2×10-3M (phosphate) | |
| pH Optimum | 7.5 |
| pH Stability | 5.0–8.0 |
| Optimum temperature | 40℃ |
| Thermal stability | below 45℃ |
| Stability (liquid form) | stable at 37℃ for at least two weeks |
| Stability (powder form) | stable at 30℃ for at least two weeks |
| Inhibitors | glucose, glucono-1,5-lactone |
| Specificity | sucrose (100), maltose (0), starch (0) |
APPLICATIONS
The enzyme is useful for the determination of inorganic phosphate in clinical analysis.
REFERENCES
- Koga, T. et al., Agric. Biol. Chem., 55, 1805–1810 (1991).
- Kitao, S. and Nakano, E., J. Ferment. Bioeng., 73, 179–184 (1992).
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