EC Number   |
Metals/Ions |
Reference |
|---|
    2.7.7.23 | Mg2+ |
strictly required. Two magnesium ions catalyze the sugar-nucleotidyl transfer reaction. 5 mM used in assay conditions |
760506 |
| 2.7.7.23 | Mn2+ |
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation |
725308 |
| 2.7.7.23 | Mn2+ |
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+ |
748158 |
| 2.7.7.23 | Mn2+ |
activates |
756049 |
| 2.7.7.23 | Mn2+ |
can partially replace Mg2+ |
643057, 643058, 643059, 643061, 643067 |
| 2.7.7.23 | Mn2+ |
no activity is detectable when a divalent cation is removed from the reaction buffer. The order of effectiveness of metal ions on GlcNAc-1-P UTase activity is Mg2+ > Zn2+ > Ca2+ > Co2+ > Mn2+, which is different from that of its Glc-1-P TTase activity, Co2+ > Mn2+ > Mg2+ > Zn2+ > Ca2+ |
748123 |
| 2.7.7.23 | Mn2+ |
or Mg2+, required |
721526 |
| 2.7.7.23 | Mn2+ |
or Mg2+, required. At 5 mM, 126% of the activity with Mg2+ |
721526 |
| 2.7.7.23 | Mn2+ |
required for maximum activity, 0.5-1 mM |
643065 |
| 2.7.7.23 | more |
the three-dimensional structure of the ST0452 mutant Y97N is not changed by due to lack of metals but the interactions with the substrate is slightly modified, which might cause the activity to increase |
760395 |
