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Co2+
-
marginally effective in activation
Co2+
-
absolute requirement for divalent metal ion is satisfied by Mn2+, Co2+ or Mg2+
Mg2+
-
divalent cation required, Mg2+ or Mn2+. Mg2+ is much more effective than Mn2+
Mg2+
-
absolutely required, activates at 5 mM
Mg2+
1 mM required for optimal activity
Mg2+
-
maximal activity at 16 mM
Mg2+
-
maximal activity at 2 mM, Mg2+ or Mn2+ required
Mg2+
optimal activity with 2.5-5 mM Mg2+ or 0.1-0.25 mM Mn2+
Mg2+
-
strictly requires Mg2+ (more than 1 mM) or Mn2+ for full activity. Treatment with H2O2 changes the specificity of both ADP-ribose activities for the activating divalent cation, giving them a marked preference for Mn2+ and rendering them virtually inactive with Mg2+
Mg2+
-
5 mM required for optimal activity
Mg2+
-
absolute requirement for divalent metal ion is satisfied by Mn2+, Co2+ or Mg2+
Mg2+
-
ADPRibase-I is highly specific for ADPribose and IDPribose in presence of Mg2+, but active also on non-reducing ADP-hexoses and dinucleotides when Mg2+ is replaced with Mn2+. ADPRibase-Mn is a Mn2+-dependent diphosphatase active on ADPribose and IDPribose, dinucleotides and CDP alcohols. ADPribase-II is a rather unspecific diphosphatase that, with Mg2+, is active on AMP or IMP containing NDP sugars and dinucleotides, and with Mn2+ also active on non-adenine NDP-sugars and CDP-alcohols
Mg2+
divalent cation required, Mg2+ is most effective
Mg2+
-
divalent cation required, Mg2+ is most effective, ADP-ribose pyrophosphatase Sll1054
Mg2+
-
divalent cation required, Mg2+ is most effective, ADP-ribose pyrophosphatase Slr0920
Mg2+
-
divalent cation required, Mg2+ is most effective, ADP-ribose pyrophosphatase Slr1134
Mg2+
dependent on Mg2+ or Zn2+
Mg2+
binding structure, overview
Mn2+
-
divalent cation required, Mg2+ or Mn2+. Mg2+ is much more effective than Mn2+
Mn2+
required for full activity
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors
Mn2+
can partially substitute for Mg2+
Mn2+
-
50% of maximal activity at 5 mM
Mn2+
-
maximal activity at 0.02-0.05 mM with a steep decrease at increasing pH-values, Mg2+ or Mn2+ required
Mn2+
optimal activity with 2.5-5 mM Mg2+ or 0.1-0.25 mM Mn2+
Mn2+
-
strictly requires Mg2+ or Mn2+ (0.05 mM) for full activity. Treatment with H2O2 changes the specificity of both ADP-ribose activities for the activating divalent cation, giving them a marked preference for Mn2+ and rendering them virtually inactive with Mg2+
Mn2+
dependent on, dinuclear metal centre
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors
Mn2+
-
can partially substitute for Mg2+
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors
Mn2+
-
absolute requirement for divalent metal ion is satisfied by Mn2+, Co2+ or Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
ADPRibase-I is highly specific for ADPribose and IDPribose in presence of Mg2+, but active also on non-reducing ADP-hexoses and dinucleotides when Mg2+ is replaced with Mn2+. ADPRibase-Mn is a Mn2+-dependent diphosphatase active on ADPribose and IDPribose, dinucleotides and CDP alcohols. ADPribase-II is a rather unspecific diphosphatase that, with Mg2+, is active on AMP or IMP containing NDP sugars and dinucleotides, and with Mn2+ also active on non-adenine NDP-sugars and CDP-alcohols
Mn2+
divalent cation required, Mn2+ results in 22% of the activity observed in presence of Mg2+
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors. Two Mn2+ ions are inserted consecutively into the catalytic center of the ES-state and ligated by Glu86 and Glu82, which are highly conserved among the Nudix family, in the ESM- and ESMM-states
Zn2+
can partially substitute for Mg2+
Zn2+
-
marginally effective in activation
Zn2+
-
can partially substitute for Mg2+
Zn2+
divalent cation required, Zn2+ results in 9% of the activity observed in presence of Mg2+
Zn2+
dependent on Mg2+ or Zn2+
additional information
-
the ADPR-hydrolysis reaction of ADPRase from Thermus thermophilus strain HB8 (TtADPRase) requires divalent metal cations such as Mn2+, Zn2+, or Mg2+ as cofactors
additional information
the ADPR-hydrolysis reaction of ADPRase from Thermus thermophilus strain HB8 (TtADPRase) requires divalent metal cations such as Mn2+, Zn2+, or Mg2+ as cofactors