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Cd2+
-
4 Cd2+ sites per subunit, enzyme activity lower compared to Mg2+
CdCl2
20 mM, 155% stimulation
lanthanum
-
results in a slow substrate binding to diphosphate
Li+
Li+ can substitute for Na+ as activator. In the presence of K+, Li+ iss a less potent activator than Na+
MgCl2
20 mM, 163% stimulation
Na+
the enzyme absolutely requires Na+ for activity, whereas both Na+ and K+ are needed for maximal activity
NH4+
activity increases more than 6fold in the presence of KCl and NH4Cl in comparison with the activity measured in the absence of any monovalent cation
NiCl2
20 mM, 156% stimulation
Ca2+
Ca2+, a strong antagonist of Mg2+ and inhibitor of all other PPases, can replace Mg2+ as activator of Mn2+-bound canonical Family II PPases, conferring about 10% of their maximal activity
Ca2+
-
hydrolysis of nucleoside triphosphates stimulated
Ca2+
-
activates at up to 1 mM, inhibits at higher concentrations, complete inhibition at 2 mM, overview
Ca2+
-
alkaline enzyme activated
Ca2+
-
most potent activator
Ca2+
Ca2+, a strong antagonist of Mg2+ and inhibitor of all other PPases, can replace Mg2+ as activator of Mn2+-bound canonical Family II PPases, conferring about 10% of their maximal activity
Ca2+
-
2% of the activity with Mg2+
Co2+
-
25% relative activity compared to Mg2+
Co2+
activates to 50% of the activity with Mg2+ at 2 mM
Co2+
-
increases hydrolysis of imidophosphate
Co2+
required, cobalt-dependent enzyme
Co2+
required, cobalt-dependent enzyme
Co2+
-
24% relative activity compared to Mg2+
Co2+
-
activation of enzyme with acid pH
Co2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
Co2+
-
60.1% of the activity with Mg2+
Co2+
-
about 20% relative activity to Mg2+ when above 3 mM
Co2+
-
protects against fluoride inhibition
Co2+
-
can partially replace Mg2+, 15%
Co2+
-
CBS-PPase requires transition metal ions, Co2+ or Mn2+, for activity
Co2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Co2+
-
alkaline enzyme activated
Co2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Co2+
-
6.7% relative activity compared to Mg2+, no activity in the absence of divalent cations
Co2+
-
lower activation than Mg2+
Co2+
-
88% of the activity with Mg2+
Co2+
-
about 15% activity in the presence of 50 mM Co2+ compared to 50 mM Mg2+
Co2+
Mg2+ is 72% less effective when compared with Ni2+, maximum activity occurs at 0.5 mM Co2+
Co2+
absolute requirement for divalent cations, 2.5 mM Mn2+ activates 37% compared to 2.5 mM Mg2+
Co2+
-
preferred cofactor for hydrolysis of triphosphate
Cu2+
-
activates
Cu2+
can partially, upt to 30%, substitute for Mg2+
Fe2+
activates to 88% of the activity with Mg2+ at 2 mM
Fe2+
can partially, upt to 30%, substitute for Mg2+
Fe3+
bound in in sites M1 and M2, the Fe3+:Mn2+ ratio is about 6:1 in site M1 and about 2:1 in site M2
Fe3+
activates to a lesser extent than Mg2+
K+
determination of K+-binding sites
K+
activity increases more than 6fold in the presence of KCl and NH4Cl in comparison with the activity measured in the absence of any monovalent cation
K+
the enzyme absolutely requires Na+ for activity, whereas both Na+ and K+ are needed for maximal activity
K+
-
required, highly activating
Mg2+
-
maximum activity
Mg2+
-
required for activity
Mg2+
activates, Mg2+ is the highly preferred cofactor for family I sPPases
Mg2+
dependent on, can be partially substituted by Mn2+, both isozymes show similar catalytic constants and affinities for the Mg-pyrophosphate complex, while differed in their affinity for free Mg2+,
Mg2+
-
magnesium ions confer the highest activity
Mg2+
required, natural cofactor of AtPPA1, metal coordination and binding site
Mg2+
Aranda Christine
-
required for activity and stability
Mg2+
Aranda Christine
-
no other divalent cations can substitute for Mg2+
Mg2+
-
free Mg2+ ions are not required
Mg2+
required, functions in catalysis and binding structure, overview
Mg2+
-
activates, Mg2+ is the preferred cofactor for family I sPPases
Mg2+
-
increases hydrolysis of imidophosphate
Mg2+
-
or other divalent cation required for hydrolysis of diphosphate
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
required, best divalent cation
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
-
maximum activation compared to other divalent ion activators
Mg2+
-
activation of enzyme with alkaline pH
Mg2+
-
required for activity and stability
Mg2+
-
wild type: two Mg2+ ions per active site required for catalysis
Mg2+
-
stabilization of the hexameric E20D enzyme
Mg2+
-
four Mg2+ ions per active site required for catalysis
Mg2+
-
required, inhibitory for the native hexamer above 5 mM, no inhibition of the dimeric form
Mg2+
-
required, three binding sites in the absence of substrate
Mg2+
-
required, substrate is magnesium diphoshate
Mg2+
binding depends highly on the pH, binds to the active site, binding structure, overview
Mg2+
-
dependent on, activates, bound to the substrate as magnesium diphosphate
Mg2+
-
dependent on, bound to the enzyme
Mg2+
dependent on, the active site contains four Mg2+ ions
Mg2+
-
required, one of the three active site Mg2+ ions is bound along with phosphate
Mg2+
dependent on, Mg2+ concentration-dependence of kinetic cooperativity in wild-type ehPPase and mutant S213N-ehPPase, overview
Mg2+
metal-binding protein
Mg2+
-
7-8fold activation
Mg2+
-
activates by decreasing the value of the Michaelis-Menten constant, dependent on, highest activity at pH 7.4 and 5.0 mM, Mg2+ shifts the pH optimum, Mg2+ associates rather weakly with the pyrophosphatase active center and can be readily displaced by Ca2+ , overview
Mg2+
requires Mg2+ or Mn2+, Km at 25°C and pH 8.5 is 13.4 mM. Sigmoidal kinetic profiles indicative of positive cooperative binding are detected for Mg2+
Mg2+
-
required, best divalent cation, binding site structure
Mg2+
dependent on, other divalent cations substituted poorly for Mg2+
Mg2+
required, binds to diphosphate, effects on enzyme activity and kinetics, pH-dependence, overview
Mg2+
-
required for activity
Mg2+
required, optimal at 5 mM
Mg2+
-
most effetive divalent cation, can partially be replaced by other divalent cations
Mg2+
-
maximum activity at 3 mM
Mg2+
much less effective than Ca2+, 20% of the activity with Ca2+
Mg2+
required, metal coordination and binding site
Mg2+
-
required for activity
Mg2+
required for catalysis
Mg2+
the activity of the enzyme is strongly dependent on Mg2+. High enzyme activity is found between 1 and 100 mM Mg2+ with a maximum activity at 10 mM. At pH 7.5, the maximum PPase activity is at 50 mM Mg2+
Mg2+
-
required for activity and stability
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
-
activity enhanced of the mitochondrial enzyme
Mg2+
-
dependent on, cannot be substituted by Mn2+ or Ca2+
Mg2+
activates, Mg2+ is the highly preferred cofactor for family I sPPases
Mg2+
required, best divalent cation, 5 mM, Km is 0.303 mM
Mg2+
maximum activity in the presence of Mg2+, influence of other metal cations is negligible
Mg2+
-
activation of enzyme with alkaline pH
Mg2+
-
alkaline enzyme activated
Mg2+
-
maximum activation at 4 mM
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
required, family I diphosphatases are Mg2+-dependent, activates
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
maximum activation compared to other divalent ion activators
Mg2+
-
required, serves as physiological cofactor
Mg2+
the pyrophosphatase requires four divalent metal cations for catalysis, magnesium provides the highest activity
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
-
the enzyme utilizes Mn2+ over Mg2+ for activity
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
binding structure, overview
Mg2+
the enzyme requires divalent cations, 5 mM
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
one Mg2+ per active site
Mg2+
-
preferred divalent cation, Km value 0.9 mM
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
activates, Mg2+ is the highly preferred cofactor for family I sPPases
Mg2+
-
maximal activity in the presence of 0.2 mM Mg2+
Mg2+
Mg2+ is 9% less effective when compared with Ni2+, maximum activity occurs at 2 mM Mg2+
Mg2+
absolute requirement for divalent cations for catalytic action, Mg2 + (2.5 mM) conferring the highest activity. KM for Mg2+ is approximately 1.7 mM
Mg2+
the enzyme shows maximal activity with magnesium pyrophosphate, the physiological substrate of the protein. The enzyme strongly binds magnesium ions to acquire the right conformation and that it is isolated in a stable magnesium-containing form, unless cations are removed by a harsh treatment with a potent chelator
Mg2+
-
required, the active site of TgPPase contains two bound Mg2+ ions. One Mg2+ is bound at M1 site coordinated by Asp190, Asp195, and Asp227. The Mg2+ is bound to protein in M2 site predominantly through water molecules and Asp195. The observed conformation in the active site represents a state where both phosphates have already dissociated
Mg2+
-
preferred cofactor for the hydrolysis of diphosphate, highest stimulation of activity at about 0.5 mM
Mg2+
-
required for activity
Mg2+
-
preferred by family I PPase, 20 mM
Mg2+
-
required for activity
Mn2+
-
10.6% relative activity compared to Mg2+
Mn2+
can partially substitute for Mg2+
Mn2+
activates to 39% of the activity with Mg2+ at 2 mM
Mn2+
-
conversion of the enzyme from inactive dimer to active trimer
Mn2+
bound in in sites M1 and M2, the Fe3+:Mn2+ ratio is about 6:1 in site M1 and about 2:1 in site M2
Mn2+
required, a Mn2+-bound canonical Family II PPase
Mn2+
-
increases hydrolysis of imidophosphate
Mn2+
can partially, upt to 30%, substitute for Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Mn2+
binding depends highly on the pH, four ions bound per enzyme molecule, binds to the active site, binding structure, overview
Mn2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
Mn2+
requires Mg2+ or Mn2+
Mn2+
-
32.8% of the activity with Mg2+
Mn2+
-
protects against fluoride inhibition
Mn2+
-
CBS-PPase requires transition metal ions, Co2+ or Mn2+, for activity
Mn2+
substitution of Mg2+ cations with Mn2+ results in significantly lower activity of 25.34% of the Mg2+-induced activity
Mn2+
activates to a lesser extent than Mg2+
Mn2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Mn2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Mn2+
-
can partially replace for Mg2+
Mn2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Mn2+
-
7.3% relative activity compared to Mg2+, no activity in the absence of divalent cations
Mn2+
-
Mn2+ ions influence the activity, temperature dependence, and thermostability of the enzyme and are required to function in cold environments
Mn2+
-
the enzyme utilizes Mn2+ over Mg2+ for activity, Mn2+ activation increases the enzyme's activity at low temperatures
Mn2+
dependent on, the active site contains two catalytic Mn2+ binding sites
Mn2+
required, a Mn2+-bound canonical Family II PPase
Mn2+
required, a Mn2+-bound canonical Family II PPase
Mn2+
the enzyme requires divalent cations
Mn2+
required, activates at 2 mM
Mn2+
required, a Mn2+-bound canonical Family II PPase
Mn2+
-
lower activation than Mg2+
Mn2+
-
32% of the activity with Mg2+
Mn2+
absolute requirement for divalent cations, 2.5 mM Mn2+ activates 17% compared to 2.5 mM Mg2+
Mn2+
-
required for activity
Mn2+
-
preferred by family II PPase, 50 mM
NaCl
the enzyme is fully active up to 3 M
NaCl
NaCl produces a slight increase in activity
Ni2+
activates to 83% of the activity with Mg2+ at 2 mM
Ni2+
activates to a lesser extent than Mg2+
Ni2+
-
3% of the activity with Mg2+
Ni2+
dependent on, divalent metal cation with highest efficiency on enzymatic activity, maximum activity occurs at 0.5 mM Ni2+
Zn2+
about the same activation as with Mg2+
Zn2+
can partially, upt to 30%, substitute for Mg2+
Zn2+
-
highly activates at up to 1 mM, inhibits at higher concentrations, overview
Zn2+
substitution of Mg2+ cations with Zn2+ results in significantly lower activity of 14.3% of the Mg2+-induced activity
Zn2+
stimulates, Zn2+ is the preferred co-factor for hydrolysis of polyP3 and ATP
Zn2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Zn2+
-
alkaline enzyme activated
Zn2+
-
required for activity
Zn2+
-
required for activity
Zn2+
-
required for activity
Zn2+
-
higher activation than Co2+, Mn2+
Zn2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Zn2+
-
95% of the activity with Mg2+
Zn2+
13% of the activity with Mg2+
Zn2+
absolute requirement for divalent cations, 2.5 mM Mn2+ activates 21% compared to 2.5 mM Mg2+
Zn2+
-
preferred cofactor for hydrolysis of polyphosphate 75
additional information
the enzyme is absolutely dependent on divalent cations, poor activity with Mn2+, Cu2+, Fe2+, Zn2+, and Co2+
additional information
the enzyme contains a unique trinuclear metal center, detailed structure analysis, overview. Mn2+ and Fe3+ do not exchange for Mg2+ even in the presence of a large excess of Mg2+
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by the enzyme requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion. One or two additional sites that bind Mn2+ and Mg2+ with millimolar affinities have been detected in canonical Family II PPases of Bacillus subtilis. An additional Mg2+ ion is brought to the enzyme as part of a Mg-phosphate complex, the true substrate. In the cell, Mg2+ ions appear to occupy all sites except that containing a transition metal ion
additional information
the metal binding residues are Asp171, Asn172, and Glu47
additional information
-
the metal binding residues are Asp171, Asn172, and Glu47
additional information
-
the enzyme is absolutely dependent on divalent cations
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by the enzyme requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by the enzyme requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion
additional information
-
no divalent cations required for activity
additional information
no effect by Ca2+, Cd2+, and Ni2+
additional information
-
no effect by Ca2+, Cd2+, and Ni2+
additional information
-
no divalent cations required for activity
additional information
-
no effect by Ca2+, Cu2+, and Fe2+
additional information
other metal ions can partially replace Ca+, activation decreases in the order Ca2+> Cu2+> Mn2+> Fe2+> Mg2+> Zn2+> Co2+
additional information
-
other metal ions can partially replace Ca+, activation decreases in the order Ca2+> Cu2+> Mn2+> Fe2+> Mg2+> Zn2+> Co2+
additional information
the enzyme activity depends on Mg2+. Other divalent cations such as Co2+, Zn2+ and Mn2+ stimulate diphosphate hydrolysis but with lower efficiency. The relative PfPPase diphosphate activity confers by divalent metal ions fell in the descending order Mg2+, Co2+ and Zn2+, Mn2+. But Zn2+ is the preferred cofactor for hydrolysis of polyP3 and ATP
additional information
-
the enzyme activity depends on Mg2+. Other divalent cations such as Co2+, Zn2+ and Mn2+ stimulate diphosphate hydrolysis but with lower efficiency. The relative PfPPase diphosphate activity confers by divalent metal ions fell in the descending order Mg2+, Co2+ and Zn2+, Mn2+. But Zn2+ is the preferred cofactor for hydrolysis of polyP3 and ATP
additional information
the enzyme is absolutely dependent on divalent cations, poor activity with Mn2+, Cu2+, Fe2+, Zn2+, and Co2+
additional information
not activated by Zn2+
additional information
no activation by Ni2+
additional information
-
no activation by Ni2+
additional information
no effect on activity by Mn2+ and Zn2+
additional information
-
no effect on activity by Mn2+ and Zn2+
additional information
-
no activity in the absence of divalent cations
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by the enzyme requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by the enzyme requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by s requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion. One or two additional sites that bind Mn2+ and Mg2+ with millimolar affinities have been detected in canonical Family II PPases of Streptococcus gordonii. An additional Mg2+ ion is brought to the enzyme as part of a Mg-phosphate complex, the true substrate. In the cell, Mg2+ ions appear to occupy all sites except that containing a transition metal ion
additional information
-
no divalent cation required
additional information
-
divalent cation required. Activity in decreasing order: Mg2+, Zn2+, Co2+, Mn2+, Ni2+, Ca2+
additional information
divalent cations are not essential for the acid PPase activity
additional information
the enzyme is absolutely dependent on divalent cations, poor activity with Mn2+, Cu2+, Fe2+, and Co2+
additional information
little or no activity is observed in the presence of Cu2+, Zn2+, Ca2+, or Mn2+
additional information
-
not affected by 50 mM Mn2+, Ni2+, Ca2+, Zn2+, and Cu2+
additional information
PPase has an absolute dependence on divalent metal cations because no measurable activity is observed in their absence
additional information
-
the enzyme retains measurable activity up to 0.7-0.8 M NaCl, KCl, or NH4Cl