EC Number   |
Metals/Ions |
Reference |
|---|
   2.7.7.79 | Co2+ |
the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Activity in presence of 10 mM Co2+ is 13% compared to the activity in presence of 10 mM Mg2+ |
712335 |
| 2.7.7.79 | Mg2+ |
required |
760482, 761088, 761202, 761296, 761511, 761936, 762372, 762377 |
| 2.7.7.79 | Mg2+ |
required for ATPase activity, the 5'-triphosphophate of the incoming GTP is coordinated with a Mg2+ ion |
760493 |
| 2.7.7.79 | Mg2+ |
the dGTP-bound crystal structure reveales two bound Mg2+ ions associated with the nucleoside triphosphate. The distance between the two metal ions is 4.3 A. The two hTHG1 aspartates (D29 and D76) coordinate the two divalent metal ions, whereas E77 points away from the metals |
713422 |
| 2.7.7.79 | Mg2+ |
the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Maximal activity by 10 mM Mg2+ |
712335 |
| 2.7.7.79 | Mn2+ |
the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Activity in presence of 10 mM Mn2+ is 70% compared to the activity in presence of 10 mM Mg2+ |
712335 |
| 2.7.7.79 | Zn2+ |
the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Activity in presence of 10 mM Zn2+ is 15% compared to the activity in presence of 10 mM Mg2+ |
712335 |
