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Cd2+
-
1 mM, supports autoadenylation reaction. Does not support nick-joining activity at 2-5 mM
Cu2+
-
1 mM, supports autoadenylation reaction. Does not support nick-joining activity at 2-5 mM
Fe3+
contains two Fe3+-tyrosinate centers, reduction of the Fe3+ to Fe2+ results in an 80% decrease in DNA substrate binding and an increase in the pH activity optimum to 5.0
KCl
optimum concentration: 5 mM
Sr2+
-
40% of activity with Mg2+, maximal activity at 25 mM
Ca2+
the enzyme requires Mg2+ or Mn2+ for activity, Ca2+ or Co2+ are less effective
Ca2+
-
5 mM, increases activity 9fold
Ca2+
exhibits some activation on ligation
Ca2+
-
approx. 10% of activity with Mg2+
Ca2+
-
enzyme can utilize Ca2+ as cofactor
Ca2+
-
1 mM, supports autoadenylation reaction. Does not support nick-joining activity at 2-5 mM
Ca2+
divalent cation required for activity, most effectiv cation together with Mg2+ for native DNA ligase, maximal activity at 5 mM
Ca2+
-
9% of activity with Mg2+, maximal activity at 5 mM, inhibition above 40 mM
Co2+
the enzyme requires Mg2+ or Mn2+ for activity, Ca2+ or Co2+ are less effective
Co2+
10 mM, divalent cation required for activity
Co2+
-
approx. 12% of activity with Mg2+
Co2+
-
nick sealing by LigD in the presence of 0.1 mM ATP requires a divalent cation cofactor. Cobalt supports the conversion of the 12-mer pDNA strand to a 24-mer which es elongated to 25-mer and 26-mer products
Co2+
-
1 mM, supports autoadenylation reaction. Does not support nick-joining activity at 2-5 mM
K+
-
3fold stimulation at 70 mM KCl, 4fold stimulation at 150 mM KCl
K+
Tequatrovirus T4
-
polyethylene glycol 6000, 15%, stimulates, when NaCl and KCl are both absent. With 10% polyethylene glycol 6000, both cohesive and blunt end ligation are increased at high concentrations of salt, 150-200 mM NaCl, or 200-250 mM KCl. With 10% polyethylene glycol 6000, intermolecular and intramolecular ligation occurs at low salt concentrations, 0.1 mM NaCl or 0-150 mM KCl. Only linear oligomers are formed by intermolecular ligation at the high concentrations
K+
monovalent cations stimulate activity, maximal activation at 10-30 mM
Mg2+
optimal concentration: 15 mM, the enzyme requires Mg2+ or Mn2+ for activity, Ca2+ or Co2+ are less effective
Mg2+
-
optimal concentration: 10 mM
Mg2+
-
optimum concentration at 5 mM
Mg2+
DNAligI uses Mn2+ or Mg2+ as metal cofactors, optimal ligation activity at 4 mM of Mg2+
Mg2+
-
5 mM, increases activity 9fold
Mg2+
-
efficient nick-joining is observed in the presence of Mg2+ and Mn2+
Mg2+
-
optimal concentration 5 mM
Mg2+
-
Mn2+ or Mn2+ required
Mg2+
-
Mn2+ is more effective than Mg2+ at 0.5-1 mM
Mg2+
-
Mn2+ or Mn2+ required
Mg2+
-
Mn2+ or Mn2+ required
Mg2+
-
Mn2+ and Ca2+ cannot replace Mg2+ in activation
Mg2+
-
required for activity
Mg2+
-
LIG1 requires multiple Mg2+ ions for catalysis
Mg2+
dependent on metal ions of Mg2+ and Mn2+. Ligation activity with a 2 to 25 mM concentration, optimal Mg2+ concentration is 10 mM
Mg2+
10 mM, divalent cation required for activity
Mg2+
-
LigD has 3'-5' single-stranded DNA exonuclease activity that requires magnesium or manganese
Mg2+
-
absolutely required for activity, maximal activity at 2 mM
Mg2+
Paramecium bursaria chlorella virus
10 mM, standard reaction condition
Mg2+
-
maximal activation at 0.6 mM
Mg2+
-
nick sealing by LigD in the presence of 0.1 mM ATP requires a divalent cation cofactor. Magnesium supports the conversion of the 12-mer pDNA strand to a discrete 24-mer ligation product. An additional minor species corresponding to AppDNA is also produced
Mg2+
MgCl2 is required for enzyme activity, with an optimal concentration between 1 and 5 mM
Mg2+
optimal concentration: 4 mM
Mg2+
-
1 mM, supports autoadenylation reaction. Required for nick-joining activity at 2-5 mM
Mg2+
divalent cation required for activity, most effectiv cation together with Ca2+ for native DNA ligase, maximal activity at 5 mM
Mg2+
Tequatrovirus T4
-
required
Mg2+
Tequatrovirus T4
-
optimal concentration: 10 mM
Mg2+
Tequatrovirus T4
-
required for activity
Mg2+
Tequatrovirus T4
-
divalent cation required for activity, maximal activity at approx. 10 mM
Mg2+
Tequatrovirus T4
-
10 mM, required for activity
Mg2+
Tequatrovirus T4
-
the ligation does not take place unless Mg2+ is added to the ligation mixture
Mg2+
-
divalent cation required for activity, maximal activity at 15 mM
Mg2+
required for activity, maximal activity at 14-18 mM
Mg2+
optimum concentration at 50 mM
Mg2+
-
required for activity
Mn2+
optimal concentration: 7.5 mM, the enzyme requires Mg2+ or Mn2+ for activity, Ca2+ or Co2+ are less effective
Mn2+
-
increases activity
Mn2+
DNAligI uses Mn2+ or Mg2+ as metal cofactors, optimal ligation activity at 1 mM of Mn2+
Mn2+
-
5 mM, increases activity 7fold
Mn2+
-
efficient nick-joining is observed in the presence of Mg2+ and Mn2+
Mn2+
-
optimal concentration: 0.5 mM
Mn2+
-
Mg2+ or Mn2+ required
Mn2+
-
Mg2+ or Mn2+ required
Mn2+
-
Mn2+ is more effective than Mg2+ at 0.5-1 mM
Mn2+
-
Mg2+ or Mn2+ required
Mn2+
-
Mn2+ cannot replace Mg2+ in activation
Mn2+
dependent on metal ions of Mg2+ and Mn2+
Mn2+
10 mM, divalent cation required for activity
Mn2+
-
LigD has 3'-5' single-stranded DNA exonuclease activity that requires magnesium or manganese
Mn2+
-
approx. 20% of activity with Mg2+
Mn2+
-
maximal activation at 6 mM
Mn2+
-
nick sealing by LigD in the presence of 0.1 mM ATP requires a divalent cation cofactor. Conversion of the 12-mer pDNA strand results in ligated products consisting of a triplet of 24-, 25-, and 26-mer species. In addition, manganese prompted the appearance of discrete radiolabeled 13- and 14-mer species
Mn2+
-
1 mM, supports autoadenylation reaction. Supports nick-joining activity to a much lesser extent than Mg2+
Mn2+
divalent cation required for activity, most effectiv cation for recombinant DNA ligase, 10times higher efficiency than with Mg2+, maximal activity at 2-5 mM
Mn2+
Tequatrovirus T4
-
25% as effective as Mg2+ in activation
Mn2+
Tequatrovirus T4
-
divalent cation required for activity
Mn2+
-
65% of activity with Mg2+, maximal activity at 25 mM
Mn2+
-
the enzyme is most active when Mn2+ is present as divalent metal cofactor rather than Mg2+ and Ca2+ etc.
Mn2+
-
required for activity
Na+
-
KCl is required for optimal activity, 3fold stimulation at 30 mM NaCl, 4fold stimulation at 150 mM NaCl
Na+
-
in 80 mM NaCl LigIII binds non-specifically to DNA, showing equal affinity for nicked and intact DNA, in 250 mM NaCl LigIII binds specifically to nicked DNA does not bind measurably to duplex DNA
Na+
Tequatrovirus T4
-
polyethylene glycol 6000, 15%, stimulates, when NaCl and KCl are both absent. With 10% polyethylene glycol 6000, both cohesive end ligation and blunt end ligation are increased at high concentrations of salt, 150-200 mM NaCl, or 200-250 mM KCl. With 10% polyethylene glycol 6000, intermolecular and intramolecular ligation occurs at low salt concentrations, 0.1 mM NaCl or 0-150 mM KCl. Only linear oligomers are formed by intermolecular ligation at the high concentrations
Na+
optimum concentration at 100 mM
NaCl
-
rate of ligation is inhibited by concentrations of more than 100 mM NaCl
NaCl
-
promotes enzyme activity, optimal concentration: 300 mM
Ni2+
-
approx. 18% of activity with Mg2+
Ni2+
-
1 mM, supports autoadenylation reaction. Does not support nick-joining activity at 2-5 mM
Zn2+
-
the enzyme contains a PARP-like zinc finger
Zn2+
-
Lig3 contains a zinc finger
Zn2+
-
1 mM, supports autoadenylation reaction. Does not support nick-joining activity at 2-5 mM
additional information
-
DNA ligase I is active at low salt concentrations, 0-30 mM KCl, DNA ligase II is active at high salt concentrations, 50-100 mM KCl
additional information
catalytic activity neither depends on nor is stimulated by added Mg2+ or K+
additional information
-
catalytic activity neither depends on nor is stimulated by added Mg2+ or K+
6.5.1.1 DNA ligase (ATP)
results (
results (
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