EC Number   |
Metals/Ions |
Reference |
|---|
   3.1.4.12 | Co2+ |
- |
135148 |
| 3.1.4.12 | Co2+ |
activates |
729131 |
| 3.1.4.12 | Co2+ |
activates, Km is 1.46 mM |
730073 |
| 3.1.4.12 | Co2+ |
can replace Mg2+ |
650502 |
| 3.1.4.12 | Co2+ |
can replace Mg2+, 50% activation at 0.0015 mM |
651801 |
| 3.1.4.12 | Co2+ |
Km: 0.142 mM, activation of sphingomyelinase activity in the order of decreasing efficiency Co2+, Mn2+, Mg2+, Ca2+, Sr2+. There are three distinct metal ion-binding sites in a long horizontal cleft across the bc-SMase molecule |
665716 |
| 3.1.4.12 | Co2+ |
lysosomal enzyme, stimulation at pH 5-7.5 |
135163 |
| 3.1.4.12 | Co2+ |
rank-order of increasing activation: Mg2+, Co2+, Mn2+, Zn2+. The four metal ions compete with each other for the same binding site on the enzyme molecule |
663762 |
| 3.1.4.12 | Co2+ |
required |
714926 |
| 3.1.4.12 | Cu2+ |
107% activity at 1 mM Mg2+ |
704743 |
