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KCl
-
maximal activation at 100 mM
NaH2PO4
-
maximal activation at 25-50 mM
NaNO2
-
inhibition at high concentration, acceleration of activity at low concentrations
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
34% of the activity with Mg2+
Ca2+
a significant increase (1.8 times) in enzyme activity is observed in the co-presence of calmodulin (0.001 mM) and CaCl2 (0.01 mM). The enzyme activity remains unaltered in the presence of either calcium or calmodulin alone
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
CaATP2- is the true substrate
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
CaATP2- is the true substrate
Ca2+
Esox sp.
-
can partially replace Mg2+ in activation
Ca2+
Esox sp.
-
CaATP2- is the true substrate
Ca2+
Frog
-
can partially replace Mg2+ in activation
Ca2+
Frog
-
CaATP2- is the true substrate
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
15% of the activity with Mg2+
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
CaATP2- is the true substrate
Ca2+
-
30% of the activity with Mg2+
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
CaATP2- is the true substrate
Ca2+
-
divalent metal ion required: Ca2+, Mg2+ or Mn2+. Mg2+ is the preferred cation
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
CaATP2- is the true substrate
Ca2+
the enzyme is activated up to 85% in the presence of 0.01 mM Ca2+
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
CaATP2- is the true substrate
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
CaATP2- is the true substrate
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
CdATP2- is the true substrate
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
CdATP2- is the true substrate
Cd2+
Esox sp.
-
can partially replace Mg2+ in activation
Cd2+
Esox sp.
-
CdATP2- is the true substrate
Cd2+
Frog
-
can partially replace Mg2+ in activation
Cd2+
Frog
-
CdATP2- is the true substrate
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
CdATP2- is the true substrate
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
CdATP2- is the true substrate
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
CdATP2- is the true substrate
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
CdATP2- is the true substrate
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
CdATP2- is the true substrate
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
77% of the activity with Mg2+
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
CoATP2- is the true substrate
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
CoATP2- is the true substrate
Co2+
Esox sp.
-
can partially replace Mg2+ in activation
Co2+
Esox sp.
-
CoATP2- is the true substrate
Co2+
Frog
-
can partially replace Mg2+ in activation
Co2+
Frog
-
CoATP2- is the true substrate
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
58% of the activity with Mg2+
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
CoATP2- is the true substrate
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
CoATP2- is the true substrate
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
CoATP2- is the true substrate
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
CoATP2- is the true substrate
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
CoATP2- is the true substrate
divalent cation
-
absolute requirement
divalent cation
-
absolute requirement
divalent cation
Esox sp.
-
absolute requirement
divalent cation
Frog
-
absolute requirement
divalent cation
-
Mg2+ or Mn2+
divalent cation
-
Mg2+ or Mn2+
divalent cation
-
absolute requirement
divalent cation
-
requires Mg2+ or Ca2+
divalent cation
-
descending order of activation potential Mg2+,Mn2+, Zn2+, Co2+, Cd2+, Ca2+, isozyme PGK1 is more activated than PGK2
divalent cation
-
Mg2+ or Mn2+
divalent cation
-
absolute requirement
divalent cation
-
Mg2+ or Mn2+
divalent cation
-
absolute requirement
divalent cation
-
absolute requirement
divalent cation
-
absolute requirement
K+
-
slightly activating
K+
-
significantly increases the activity of the enzyme
K+
monovalent cations are essential for the activity of the archaeal enzyme with K+ being significantly more efficient than Na+
K+
monovalent cations are essential for the activity, with K+ being significantly more efficient than Na+.
K+
monovalent cations are essential for the activity of the archaeal enzyme with K+ being significantly more efficient than Na+. Non-cooperative K+ binding with an apparent Kd (K+) of 88 mM
K+
monovalent cations are essential for the activity, with K+ being significantly more efficient than Na+. Non-cooperative K+ binding with an apparent Kd of 88 mM
K+
Vombatus sp.
-
slightly activating
KH2PO4
-
maximal activation at 25-50 mM
KH2PO4
-
inhibition at high concentration, acceleration of activity at low concentrations
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
10 mM used in assay conditions
Mg2+
essentially required
Mg2+
-
required for activity
Mg2+
required, most effective divalent metal ion
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
required for activity
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
Esox sp.
-
true substrate is the magnesium complexes of ATP
Mg2+
Frog
-
true substrate is the magnesium complexes of ATP
Mg2+
-
required for activity
Mg2+
required for activity
Mg2+
-
5 mM Mg2+ or 10 mM Mn2+ required
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
2 mM used in assay conditions
Mg2+
5 mM used in assay conditions
Mg2+
required for activity
Mg2+
-
at pH 5.5, the catalytic activity of full-length enzyme is increased with increasing concentration of Mg2+
Mg2+
-
required for activity
Mg2+
-
Mg2+ most efficient activator
Mg2+
-
above 10 mM inhibition of isozyme PGK1, not PGK2
Mg2+
-
0.8 m Mg2+ and 0.5 mM Mn2+ are optimal
Mg2+
-
required for activity
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
required for activity
Mg2+
-
divalent metal ion required: Ca2+, Mg2+ or Mn2+. Mg2+ is the preferred cation. Optimal concentration of Mg2+ is 5-15 mM
Mg2+
required for activity
Mg2+
dependent on Mg2+, saturated at 5 mM concentration
Mg2+
-
20 mM used in assay conditions
Mg2+
-
required for activity
Mg2+
required for activity
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
20 mM used in assay conditions
Mg2+
-
5 mM used in assay conditions
Mg2+
-
required for activity
Mg2+
Spirulina geitleri
-
required for activity
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
MgATP2- is the substrate. Mg2+ is liganded to both beta- and gamma-phosphates of ATP
Mg2+
-
required for activity
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
required for activity
Mg2+
required for activity
Mg2+
-
optimum concentration: 8-16 mM
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
required for activity
Mg2+
required for activity
Mg2+
required for activity
Mg2+
2 mM used in assay conditions
Mg2+
Vombatus sp.
-
true substrate is the magnesium complexes of ATP
Mg2+
-
5 mM used in assay conditions
Mg2+
-
required for activity
Mg2+
-
true substrate is the magnesium complexes of ATP
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
67% of the activity with Mg2+
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
5 mM Mg2+ or 10 mM Mn2+ required
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
more effective for isoenzyme PGK1 than for PGK2
Mn2+
-
0.8 mM Mg2+ and 0.5 mM Mn2+ are optimal
Mn2+
-
divalent metal ion required: Ca2+, Mg2+ or Mn2+. Mg2+ is the preferred cation
Mn2+
-
can partially replace Mg2+ in activation
Na+
-
significantly increases the activity of the enzyme
Na+
monovalent cations are essential for the activity of the archaeal enzyme with K+ being significantly more efficient than Na+
Na+
monovalent cations are essential for the activity, with K+ being significantly more efficient than Na+
Na+
monovalent cations are essential for the activity of the archaeal enzyme with K+ being significantly more efficient than Na+
Na+
monovalent cations are essential for the activity, with K+ being significantly more efficient than Na+
NaCl
-
maximal activation at 100 mM
NaCl
-
inhibition at high concentration, acceleration of activity at low concentrations
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
12% of the activity with Mg2+
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
NiATP2- is the true substrate
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
NiATP2- is the true substrate
Ni2+
Esox sp.
-
can partially replace Mg2+ in activation
Ni2+
Esox sp.
-
poor activator
Ni2+
Esox sp.
-
NiATP2- is the true substrate
Ni2+
Frog
-
can partially replace Mg2+ in activation
Ni2+
Frog
-
poor activator
Ni2+
Frog
-
NiATP2- is the true substrate
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
NiATP2- is the true substrate
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
NiATP2- is the true substrate
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
NiATP2- is the true substrate
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
NiATP2- is the true substrate
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
NiATP2- is the true substrate
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
ZnATP2- is the true substrate, free metal ions inhibit
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
ZnATP2- is the true substrate, free metal ions inhibit
Zn2+
Esox sp.
-
can partially replace Mg2+ in activation
Zn2+
Esox sp.
-
ZnATP2- is the true substrate, free metal ions inhibit
Zn2+
Frog
-
can partially replace Mg2+ in activation
Zn2+
Frog
-
ZnATP2- is the true substrate, free metal ions inhibit
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
ZnATP2- is the true substrate, free metal ions inhibit
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
more effective for isoenzyme PGK1 than for PGK2
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
ZnATP2- is the true substrate, free metal ions inhibit
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
ZnATP2- is the true substrate, free metal ions inhibit
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
ZnATP2- is the true substrate, free metal ions inhibit
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
ZnATP2- is the true substrate, free metal ions inhibit
additional information
-
no activation by Fe2+
additional information
-
no activation by Be2+
additional information
-
no activation by Fe2+
additional information
-
no activation by Be2+
additional information
Esox sp.
-
no activation by Fe2+
additional information
Esox sp.
-
no activation by Be2+
additional information
Frog
-
no activation by Fe2+
additional information
Frog
-
no activation by Be2+
additional information
-
no activation by Ba2+
additional information
-
no activation by Fe2+
additional information
-
no activation by: Sr2+
additional information
-
no activation by Be2+
additional information
-
the activity of the enzyme is insensitive to Ca2+ ion
additional information
-
no activation by Fe2+
additional information
-
no activation by Be2+
additional information
-
no activation by Fe2+
additional information
-
no activation by Be2+
additional information
-
no activation by Fe2+
additional information
-
no activation by Be2+
additional information
-
no activation by Fe2+
additional information
-
no activation by Be2+