EC Number   |
Metals/Ions |
Reference |
|---|
    2.2.1.1 | Ca2+ |
- |
486023 |
| 2.2.1.1 | Ca2+ |
2.5 mM used in assay conditions |
756232 |
| 2.2.1.1 | Ca2+ |
activates |
735856 |
| 2.2.1.1 | Ca2+ |
bound at the subunit interface |
690883 |
| 2.2.1.1 | Ca2+ |
can replace Mg2+ |
735708 |
| 2.2.1.1 | Ca2+ |
can replace Mg2+ to some extent |
485999 |
| 2.2.1.1 | Ca2+ |
holoenzyme reconstituted in the presence of Ca2+ is more stable than its Mg2+ counterpart |
675747 |
| 2.2.1.1 | Ca2+ |
in the presence of Ca2+, the enzyme exhibits strong negative active site cooperativity in both xylulose 5-phosphate binding and ribose 5-phosphate binding and positive cooperativity in the catalytic activity |
696175 |
| 2.2.1.1 | Ca2+ |
in the presence of free Ca2+, the equivalence of the two active centers of the enzyme is lost. Negative cooperativity is induced on binding of either xylulose 5-phosphate or ribose 5-phosphate, whereupon the catalytic conversion of the bound substrates causes the interaction between the centers to become positively cooperative. Enzyme total activity increases in presence of Ca2+ |
720982 |
| 2.2.1.1 | Ca2+ |
kinetics in presence of Ca2+ |
658741 |
