EC Number |
Metals/Ions |
Reference |
---|
6.5.1.2 | Ca2+ |
10fold lower activation than Mn2+, maximal activity at 2 mM |
672811 |
6.5.1.2 | Ca2+ |
40% of activity obtained with Mg2+ |
651212 |
6.5.1.2 | Ca2+ |
60% as active as Mg2+ in activation as reported in one study, no activity in another |
1909, 1910 |
6.5.1.2 | Ca2+ |
activates wild-type enzyme and mutant enzyme DELTA582-667 |
661789 |
6.5.1.2 | Ca2+ |
in presence of Ca2+ MtuLigA is able to carry out the first two steps of ligation reaction that is the transfer of AMP to enzyme from NAD+ and further transfer of it to substrate to form DNA-adenylate intermediate. Ca2+ can not support nick closure activity |
677062 |
6.5.1.2 | Ca2+ |
supports formation of DNA-adenylate intermediate |
653379 |
6.5.1.2 | Ca2+ |
the enzyme requires a divalent cation like Ca2+, optimal activity at about 20 mM Ca2+ |
714854 |
6.5.1.2 | Co2+ |
25% of the activity with Mg2+ |
653388 |
6.5.1.2 | Co2+ |
can partially substitute for Mg2+ |
652175 |
6.5.1.2 | Co2+ |
no activity observed in the presence of |
728580 |