EC Number   |
Metals/Ions |
Reference |
|---|
    2.5.1.17 | Ca2+ |
activates 2.5fold |
674277 |
| 2.5.1.17 | Co2+ |
- |
636871 |
| 2.5.1.17 | Co2+ |
1.75fold activation |
674277 |
| 2.5.1.17 | Co2+ |
activates, KD: 0.27 mM |
652541 |
| 2.5.1.17 | Co2+ |
activation, less effective than Mn2+ |
636864, 636865 |
| 2.5.1.17 | Co2+ |
activity with divalent cations in descending order: Mg2+, Mn2+, Co2+ |
659058 |
| 2.5.1.17 | Co2+ |
enzyme depends absolutely on divalent cations in the descending order Mg2+, Mn2+, Co2+, 39% of the activity with Mg2+ |
652541 |
| 2.5.1.17 | Co2+ |
tetradentate coordination for the cobalt ion, binding structure, overview. In the four-coordinate state, the lower ligand and entire nucleotide arm are displaced by Phe91 and Trp93 and the N-terminal helix from the opposing subunit. This yields a closed active site or conformation for the enzyme. Relative to the five-coordinate cob(II)alamin state, this displacement involves a conformational change in the loop that extends from Met87 to Cys105 and includes a change in the orientation of Phe91 and Trp93 |
721682 |
| 2.5.1.17 | Cs+ |
activation |
636866 |
| 2.5.1.17 | Fe2+ |
required |
738459 |
