EC Number   |
Metals/Ions |
Reference |
|---|
   3.1.4.12 | Zn2+ |
required by the secreted enzyme form |
716445 |
| 3.1.4.12 | Zn2+ |
required for activity, best at 0.5-1 mM, inhibitory above 10 mM |
730731 |
| 3.1.4.12 | Zn2+ |
slight activation at 4 mM, Km at 2 mM |
649984 |
| 3.1.4.12 | Zn2+ |
the enzyme possesses at least two different binding sites for Zn2+. Zn2+ binding to the high affinity site can activate the enzyme, whereas the Zn2+ binding to the low-affinity site can activate the enzyme. Binding of the substrate to the enzyme is independent of the Zn2+ binding to the high-affinity site, but is competitively inhibited by the Zn2+ binding to the low-affinity site. 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 | Zn2+ |
Zn2+ binding to the high-affinity site activates the enzyme and, conversely, binding to the low-affinity site inhibits the enzyme |
678142 |
| 3.1.4.12 | Zn2+ |
Zn2+-dependent sphingomyelinase acid activity is much higher than Zn2+ independent isoform activity in both fetal and mother's blood |
665122 |
