EC Number   |
Metals/Ions |
Reference |
|---|
   3.1.4.54 | Ba2+ |
10 mM, stimulates |
710098 |
| 3.1.4.54 | Co2+ |
10 mM, stimulates |
710098 |
| 3.1.4.54 | Mg2+ |
10 mM, stimulates |
710098 |
| 3.1.4.54 | Ni2+ |
10 mM, stimulates |
710098 |
| 3.1.4.54 | Sr2+ |
10 mM, stimulates |
710098 |
| 3.1.4.54 | Zn2+ |
a binuclear Zn2+ center is involved in hydrolysis |
752275 |
| 3.1.4.54 | Mg2+ |
activates, methyl arachidonyl fluorophosphonate inhibits activation by Mg2+ slightly |
714339 |
| 3.1.4.54 | Ca2+ |
activation is observed only in the enzyme preparations after solubilization, EC50: 3 mM. Synergistic activation of the enzyme by spermine and CaCl2 or by spermine and Triton X-100 is not observed |
708109 |
| 3.1.4.54 | Zn2+ |
dependent on, NAPE-PLD belongs to the zinc metallohydrolase family of the beta-lactamase fold |
710115 |
| 3.1.4.54 | Ca2+ |
in the presence of 100 mM phospholipid (phosphatidylethanolamine, phosphatidylcholine, or phosphatidylserine), Ca2+ dose-dependently activates NAPE-PLD in varied degrees. Ca2+ at 10 mM stimulates the activity 2.1 fold in the presence of phosphatidylethanolamine. In the presence of phosphatidylcholine or phosphatidylserine, the stimulatory effects of 10 mM Ca2+ (5.2 and 10 fold, respectively) are similar to the effect by 10 mM Ca2+ in the absence of phospholipids (7fold) |
710098 |
