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Cs+
-
activates wild-type, full-length enzyme paPpx(1-506)
NH4+
-
activates wild-type, full-length enzyme paPpx(1-506). The activity curve obtained with NH4+ is sigmoid and reaches its maximum activity at concentrations of 30 mM. Km(app)NH4+ is 10 mM
Rb+
-
activates wild-type, full-length enzyme paPpx(1-506)
Ca2+
partially active in the presence of 5 mM Ca2+, 25% compared to activity with 5 mM Mg2+
Ca2+
activates, best cation
Co2+
ANU33171.1
activates
Co2+
-
1.5-2.5fold lower activation than with Mg2+, inhibitory with Mg2+ as activator
Co2+
partially active in the presence of 5 mM Co2+, 23% compared to activity with 5 mM Mg2+
K+
-
a nonessential activator of paPpx, presence of K+ does not affect the affinity of the enzyme for Mg2+, activates wild-type, full-length enzyme paPpx(1-506). The activity curve obtained with K+ is sigmoid and reaches its maximum activity at concentrations of 80 mM. Km(app)K+ is 42 mM
KCl
Dictyostelium discoideum also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
Mg2+
-
maximal activity at 10 mM
Mg2+
-
maximal activation at 10 mM
Mg2+
ANU33171.1
activates
Mg2+
-
optimal at 10 mM, activates
Mg2+
-
required for activity
Mg2+
-
maximal activity at 12-13 mM
Mg2+
-
maximal activity at 10 mM
Mg2+
-
required for activity
Mg2+
-
maximal activity of polyphosphate synthesis, ATP and GTP synthesis, and guanosine 5'-tetraphosphate synthesis at 5.0, 2.0, 1.0 and 0.2 mM
Mg2+
-
maximal activity at 5-10 mM at 1 mM ATP
Mg2+
required, best at 10 mM
Mg2+
optimum concentration 10 mM
Mg2+
Mn2+ is preferred over Mg2+
Mg2+
-
necessary for activity
Mg2+
optimal above 0.5 mM
Mg2+
-
optimum activity at 30 mM Mg2+
Mg2+
-
optimum Mg2+ concentration is 5 mM
Mg2+
-
required for activity
Mg2+
-
maximal activity at 2 mM
Mg2+
the enzyme requires Mg2+ or Mn2+ for maximum activity. Optimal concentration for polyphosphate synthesis is between 1 and 2.5 mM
Mg2+
polyphosphate kinase 2, preferred in ATP synthesis over Mn2+
Mg2+
-
5fold higher activation than Mn2+, at optimal concentration of 10 mM
Mg2+
-
no activity in the absence of a divalent metal cation, Mg2+ is the most effective metal, whereas low activity is observed with Co2+ or Ni2+ and no activity is observed in the presence of Mn2+ or Ca2+
Mg2+
preference for Mn2+ over Mg2+
Mg2+
-
required, values of Km(app)Mg2+ in paPpx(1-506) and NpaPpx(1-314) are 0.30 mM and 0.28 mM, respectively. The interaction between paPpx(1-506) and Mg2+ occurs in the N-terminal domain
Mg2+
Mg2+ is favored over Mn2+ by 5fold at optimal concentration of 10 mM
Mg2+
recombinant polyphosphate kinase, maximal activity at 10 mM
Mg2+
activates, best cation
Mg2+
-
required for activity
Mg2+
-
inhibitory above 6 mM
Mg2+
-
active substrate: MgATP
Mg2+
no activity in the absence of a divalent metal cation, Mg2+ is the most effective metal, whereas low activity is observed with Co2+ or Ni2+ and no activity is observed in the presence of Mn2+ or Ca2+
Mg2+
-
50% as effective as Mn2+
Mg2+
Thermosynechococcus vestitus
-
Mg2+
Thermosynechococcus vestitus
optimal above 0.5 mM
Mn2+
-
can replace Mg2+ to some extent
Mn2+
ANU33171.1
activates
Mn2+
-
optimal at 10 mM, activates highly
Mn2+
-
activation, can replace Mg2+
Mn2+
-
1.5-2.5fold lower activation than with Mg2+
Mn2+
-
2 mM, 22% of activation with Mg2+
Mn2+
required, best at 1 mM
Mn2+
optimum concentration 1 mM
Mn2+
Mn2+ is preferred over Mg2+
Mn2+
-
necessary for activity
Mn2+
-
optimum activity at 1 mM Mn2+
Mn2+
-
activation, can replace Mg2+
Mn2+
the enzyme requires Mg2+ or Mn2+ for maximum activity. Optimal concentration for polyphosphate synthesis is 1 mM
Mn2+
polyphosphate kinase 2, 10 mM preferred in polyphosphate synthesis over Mg2+
Mn2+
-
Mg2+ shows 5fold higher activation than Mn2+, at optimal concentration of 10 mM
Mn2+
preference for Mn2+ over Mg2+
Mn2+
Mg2+ is favored over Mn2+ by 5fold at optimal concentration of 10 mM
Mn2+
activates, best cation
Mn2+
-
activation, can replace Mg2+
Mn2+
-
maximal activity at 1.0-2.0 mM, inhibition above 2 mM
Mn2+
-
active substrate: MnATP
Mn2+
-
maximal activity at 2 mM
Mn2+
-
stimulates, preferred metal ion
Zn2+
ANU33171.1
activates
Zn2+
-
activation, 0.4 mM, 10% as effective as Mg2+
Zn2+
partially active in the presence of 5 mM Zn2+, 21% compared to activity with 5 mM Mg2+
Zn2+
-
Zn2+ is able to activate the enzyme only 20% compared to Mg2+
additional information
-
not activated by Ca2+
additional information
-
not activated by Ca2+
additional information
lower optimal concentration for Mn2+ ions than Mg2+ ions
additional information
-
not activated by Na+ and polyphosphate
additional information
-
Fe2+, Zn2+, Cu2+ cannot be used by the enzyme
additional information
-
not activated by Ca2+
additional information
-
behavior of the full-length paPpx(1-506) and N-paPpx(1-314) against different concentration of divalent ions such as Mg2+, Zn2+, Ca2+, and Mn2+ as effectors, in presence of a saturating concentration (0.008 mM) for the substrate polyphosphate65. The activation of both enzyme variants by Mg2+ is similar and shows no inhibition at high concentrations of this ion. The activation by Ca2+ and Mn2+ is negligible. Li+ and Na+ have no effects on enzyme activity, while NH4+, K+, Rb+, and Cs+ are activators of paPpx(1-506). Tetramethylammonium is not an activator of paPpx(1-506)
additional information
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
not activated by NH4Cl