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Cu2+
30% of activity obtained with Mg2+
MgCl2
-
highest activity: 10 mM MgCl2
NH4Cl
-
enzymatic activity increased in the presence of monovalent cations, maximal activity at 10 mM NaCl
Ca2+
supports formation of DNA-adenylate intermediate
Ca2+
40% of activity obtained with Mg2+
Ca2+
-
10fold lower activation than Mn2+, maximal activity at 2 mM
Ca2+
-
60% as active as Mg2+ in activation as reported in one study, no activity in another
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
Ca2+
-
the enzyme requires a divalent cation like Ca2+, optimal activity at about 20 mM Ca2+
Ca2+
-
activates wild-type enzyme and mutant enzyme DELTA582-667
Co2+
-
can partially substitute for Mg2+
Co2+
-
25% of the activity with Mg2+
Co2+
-
no activity observed in the presence of
K+
-
stimulates
K+
-
stimulates at low concentrations
K+
25 mM, stimulates activity
K+
-
highest activity below 10 mM
K+
-
activates at 1-150 mM
KCl
-
stimulation by 300 mM KCl, in 10% w/v polyethylene glycol 6000 solution or 150-300 mM KCl in 15% polyethylene glycol 6000 solution. Stimulation of intermolecular blunt end ligation by 150-250 mM KCl in 15% polyethylene glycol 600 solution
KCl
-
no activity is detected in the absence of KCl. Maximum activity at 3.2 M KCl, close to the intracellular KCl concentration of Haloferax volcanii cells
KCl
-
enzymatic activity increased in the presence of monovalent cations, maximal activity at 25 mM NaCl
Mg2+
-
highest activity at 5 mM
Mg2+
-
10fold lower activation than Mn2+, maximal activity at 1 mM
Mg2+
-
optimum concentration at 5 mM
Mg2+
-
requires divalent cations, Mn2+ or Mg2+
Mg2+
-
optimal concentration: 1-3 mM
Mg2+
-
Mg2+ activates at 4.0 mM
Mg2+
-
required for activity, maximal activity occurs with 10-20 mM MgCl2 in the presence of 30 mM each of KCl and (NH4)2SO4
Mg2+
-
or Mn2+ required, maximal activity at 10-15 mM
Mg2+
divalent cation required, optimal concentration: 10 mM
Mg2+
-
the enzyme requires a divalent cation like Mg2+, optimal activity at about 20 mM Mg2+
Mg2+
-
best metal-activator of wild-type enzyme and mutant enzyme DELTA582-667
Mg2+
-
requires divalent cations, Mn2+ or Mg2+
Mg2+
-
optimal concentration: 5-9 mM
Mn2+
-
can partially substitute for Mg2+
Mn2+
5 mM, most effective metal cofactor
Mn2+
50% of activity obtained with Mg2+
Mn2+
-
preference for Mn2+ as cofactor, maximal activity at 1 mM
Mn2+
-
requires divalent cations, Mn2+ or Mg2+
Mn2+
-
activation at 0.2-1.0 mM, inhibition at higher concentration
Mn2+
-
or Mg2+ required, maximal activity at 1 mM
Mn2+
-
the enzyme requires a divalent cation like Mn2+, maximal activity at 3 mM Mn2+
Mn2+
-
activates wild-type enzyme and mutant enzyme DELTA582-667
Mn2+
-
requires divalent cations, Mn2+ or Mg2+
Mn2+
-
optimal concentration: 3-6 mM
NaCl
-
stimulation of intermolecular cohesive-end ligation by 200 mM NaCl, in 10% w/v polyethylene glycol 6000 solution, or 100-200 mM NaCl in 15% polyethylene glycol 6000 solution. Stimulation of intermolecular blunt end ligation by 100-150 mM NaCl in 15% polyethylene glycol 600 solution
NaCl
-
enzymatic activity increased in the presence of monovalent cations, maximal activity at 5 mM NaCl
NH4+
-
stimulates
NH4+
-
stimulates at low concentrations
NH4+
-
stimulates enzyme activity at 10 mM
NH4+
10 mM, stimulates activity
NH4+
-
highest activity below 10 mM
NH4+
-
activates at 1-150 mM
Ni2+
supports formation of DNA-adenylate intermediate
Ni2+
10% of activity obtained with Mg2+
Ni2+
-
no activity observed in the presence of
Zn2+
5% of activity obtained with Mg2+
Zn2+
-
zinc binding motif, Cys437, Cys440, Cys455, Cys460
Zn2+
-
zinc binding motiv, C408, C411, C432 and C426
Zn2+
-
bound to the C-terminal fragment
Zn2+
0.24 mol per mol protein
Zn2+
1 mol per mol of enzyme, Cys406, Cys409, Cys422 and Cys427 form a zinc binding motif
additional information
-
Ca2+, Zn2+ and Cu2+ have no effect on activity
additional information
-
no zinc binding motif as known from most bacterial DNA-ligases
additional information
-
no zinc-binding motif as known for bacterial DNA-ligase
additional information
-
no zinc-binding motif as known for bacterial DNA-ligase