EC Number   |
Metals/Ions |
Reference |
|---|
    2.5.1.21 | Mg2+ |
required, the catalytic site is composed of the large central cavity formed by antiparallel alpha helices with two aspartate rich regions (DXXXD) on opposite walls, these residues are considered to play roles in binding of prenyl phosphates by binding Mg2+ ions |
723148 |
| 2.5.1.21 | Mg2+ |
the aspartate side chains are involved in binding multiple Mg2? ions that stabilize binding of diphosphate groups in the substrate |
723165 |
| 2.5.1.21 | Mg2+ |
the enzyme requires either Mg2+ or Mn2+ as metal cofactor |
737345, 739406 |
| 2.5.1.21 | Mn2+ |
activates 40% compared to Mg2+ at 1,25 mM |
738214 |
| 2.5.1.21 | Mn2+ |
in presence of Mn2+ and Mg2+ the activity is reduced to one-third of that in presence of Mn2+ alone |
489837 |
| 2.5.1.21 | Mn2+ |
more effective than Mg2+ in activation of dehydrosqualene formation |
489828, 489838 |
| 2.5.1.21 | Mn2+ |
six times more effective in activation than Mg2+ |
489837 |
| 2.5.1.21 | Mn2+ |
stimulates, maximum stimulation at 0.1 mM |
489838 |
| 2.5.1.21 | Mn2+ |
stimulation |
489837 |
| 2.5.1.21 | Mn2+ |
the enzyme requires either Mg2+ or Mn2+ as metal cofactor |
737345, 739406 |
