Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+
-
in the presence of Ca2+, the activity is about 20% of levels with Mg2+
Cd2+
-
stimulated in the micromolar range to a lower extent than Cu2+ and Mn2+
Cs+
-
activates wild-type, full-length enzyme paPpx(1-506)
Cu2+
-
0.01 mM, stimulates
NaCl
-
50 and 200 mM, 46 and 42% activity enhancement, respectively
NH4Cl
-
50 and 200 mM, 42 and 67% activity enhancement, respectively
Rb+
-
activates wild-type, full-length enzyme paPpx(1-506)
Co2+
KD: 46.9 +/- 5.66 micorM Co2+ with p-nitrophenyl phosphate, KD: 10.7 +/- 1.07 microM Co2+ with 5'-AMP
Co2+
-
reaction requires a divalent metal cofactor
Co2+
-
little effect on polyP15 hydrolysis
Co2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Co2+
-
activates 4.4fold polyphosphatase II and activates 1.5fold polyphosphatase I both at 0.15 mM
Co2+
-
0.1 mM Co2+, PPX activity is stimulated by a factor of two in the nuclear fraction, but not in the mitochondrial fraction
Co2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Co2+
-
2 mM CoCl2, 2.5fold stimulation
Co2+
-
stimulated by divalent cations, Co2+ is the best stimulator, 6fold at 0.05 mM
Co2+
-
5 mM, 108% of the activation by Mg2+
Co2+
-
6fold activation at 0.1 mM
Co2+
0.1 mM, 31fold activity enhancement
Co2+
-
0.1 mM, 6fold activity stimulation
Co2+
-
2.5fold activation
Co2+
best activator, maximum activation at 0.1 mM
Co2+
Co2+ stimulates phosphate release from the polyphosphate chain end
Fe2+
enzyme is stimulated 0.26fold at a concentration of 2 mM
Fe2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Fe2+
-
5 mM, 34% of the activation by Mg2+
K+
20 mM, about 3fold stimulation
K+
PPX2 activity is increased, 25 mM KCl resulting in a 3fold increase in the specific activity
K+
-
activates 2fold polyphosphatase II, but not activates polyphosphatase I
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
K+
100 mM, 30% activity enhancement
KCl
-
175 mM, stimulates
KCl
-
50 and 200 mM, 39 and 38% activity enhancement, respectively
Mg2+
best activator, maximum activity at 5 mM
Mg2+
enzyme requires Mg2+ cations but is inhibited by higher concentrations, Mg2+ shows the highest stimulation at 2 mM
Mg2+
-
divalent cation required, Mg2+ is most effective
Mg2+
KD: 224.7 +/- 35.1 microM Mg2+ with p-nitrophenyl phosphate, KD: 140.0 +/- 9.99 microM Mg2+ with 5'-AMP
Mg2+
-
reaction requires a divalent metal cofactor, bound substrate enhances enzyme affinity for the metal ion
Mg2+
-
best activator at 1 mM using polyP3, polyP4 and polyP15 as substrates
Mg2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Mg2+
may partly substitute for Mn2+
Mg2+
-
the activity of NMB1467 is dependent on Mg2+ with optimal activity observed with between 1 and 2 mM
Mg2+
-
required, values of 0.5(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+
-
2.5 mM Mg2+, PPX activity is stimulated by a factor of two in the nuclear fraction and in the mitochondrial fraction
Mg2+
-
required, family I diphosphatases are Mg2+-dependent, activates
Mg2+
about 50% of the activity with Mn2+
Mg2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Mg2+
-
1-10 mM, about 7fold activation
Mg2+
-
required, optimal activity at 5 mM
Mg2+
-
2fold activation at 0.1 mM
Mg2+
-
0.1 mM MgSO4, 5% activity loss
Mg2+
-
1 mM, 2fold activity enhancement
Mg2+
2.5 mM, 15fold activity enhancement
Mg2+
-
1.6fold activation
Mg2+
-
single tight binding site for Mg2+
Mg2+
-
optimal activity of exopolyphosphatase II in presence of 3 mM
Mg2+
activates, preferred divalent cation
Mn2+
5 mM, about 37% of the activity with Mg2+
Mn2+
5 mM, about 65% of the activity with Mg2+
Mn2+
enzyme is stimulated 0.86fold at a concentration of 2 mM
Mn2+
KD: 7.24 +/- 0.71 microM Mn2+ with p-nitrophenyl phosphate, KD: 2.23 +/- 0.14 micorM Mn2+ with 5'-AMP
Mn2+
-
reaction requires a divalent metal cofactor, Mn2+ confers 50% activity compared to Mg2+ in P3 and P4 hydrolysis
Mn2+
-
best activator for guanosine 5'-tetraphosphate hydrolysis
Mn2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Mn2+
required, optimum concentration 1 mM
Mn2+
preferred divalent cation, required. Optimal concentration about 10 mM
Mn2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Mn2+
-
1-10 mM, 3-5fold stimulation
Mn2+
-
0.5 mM, stimulates
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
NH4+
100 mM, 35% activity enhancement
Ni2+
KD: 72.3 +/- 7.61 microM Ni2+ with p-nitrophenyl phosphate, KD: 29.4 +/- 3.69 microM Ni2+ with 5'-AMP
Ni2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Ni2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Ni2+
-
5 mM, 32% of the activation by Mg2+
Zn2+
enzyme is stimulated 0.11fold at a concentration of 2 mM
Zn2+
-
Mn2+ or Co2+ required. Mg2+, Zn2+, Fe2+, and Ni2+ are less effective
Zn2+
may partly substitute for Mn2+
Zn2+
-
Zn2+ is able to activate the enzyme only 20% compared to Mg2+
Zn2+
-
1.5fold activation at 0.1 mM
Zn2+
-
0.1 mM ZnSO4, 76% activity loss
Zn2+
-
stimulated in the micromolar range to a lower extent than Cu2+ and Mn2+
additional information
presence of divalent cation is absolutely required, Mg2+ is preferred
additional information
presence of divalent cation is absolutely required, Mg2+ is preferred
additional information
-
no activity measured in absence of divalent cations
additional information
no activity with Ca2+, Co2+, Cu2+ or Fe2+ ions
additional information
-
no activity with Ca2+, Co2+, Cu2+ or Fe2+ ions
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
-
no effect on activity by Mn2+ and Zn2+
additional information
-
stimulated by divalent cations to a lesser extent
additional information
-
exopolyphosphatase I does not require divalent cations
additional information
enzyme TbNH2 is able to hydrolyze polyphosphate with Mg2+ and Co2+ as cofactors, but has lower activity with Mn2+
additional information
enzyme TbNH2 is able to hydrolyze polyphosphate with Mg2+ and Co2+ as cofactors, but has lower activity with Mn2+
additional information
Mg2+ or Mn2+ are the preferred cofactors while no activity is detected with Co2+
additional information
Mg2+ or Mn2+ are the preferred cofactors while no activity is detected with Co2+