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KCl
optimal activity between 50 and 100 mM. 85% of maximal activity when the KCl concentration is 500 mM
Na+
-
activity can be enhanced by the addition of a monovalent cation (50 mM), Na+ (relative activity 133%), K+ (117%), and NH4+ (114%) in the presence of Mg2+. Activity is significantly increased with the increased concentration of NaCl up to 50 mM
NH4+
-
activity can be enhanced by the addition of a monovalent cation (50 mM), Na+ (relative activity 133%), K+ (117%), and NH4+ (114%) in the presence of Mg2+
Ca2+
contains Ca2+ ions
Ca2+
-
calmodulin binding to the enzyme is stimulated by 0.01 mM Ca2+
Co2+
-
Co2+
-
12% of activity with Mg+
Co2+
-
50% of activity with Mg2+-
Co2+
-
no enzyme activity in the absence of divalent cations. Co2+ can replace Mg2+ with 35% of the maximal activity obtained in presence of Mg2+
Co2+
metal-ion dependent enzyme, highest activity (5.09 mM/min*mg) in presence of Co2+ followed by Mg2+ (3.28 mM/min*mg) at 90°C and pH 7.5
Fe2+
-
activation, less effective than Mg2+
Fe2+
-
34% of activity with Mg2+
Fe2+
-
30% of activity with Mg2+
K+
-
-
K+
-
kinetics, Km-value: 11.1 mM
K+
-
required for activity, inhibition at high concentrations is reversed by increased concentrations of ATP
K+
-
slight activation at low concentrations
K+
-
required for activity, inhibition at high concentrations is reversed by increased concentrations of ATP
K+
-
required for activity, inhibition at high concentrations is reversed by increased concentrations of ATP
K+
-
activation at low concentrations
K+
-
activity can be enhanced by the addition of a monovalent cation (50 mM), Na+ (relative activity 133%), K+ (117%), and NH4+ (114%) in the presence of Mg2+
K+
-
required for activity, maximal activity at 175 mM, 50% lower activity in the absence of K+
Mg2+
required for activity
Mg2+
the optimal MgCl2 concentration for activity is 20-30 mM and the enzyme possesses 6, 36 and 74% activity compared to the maximal activity when the MgCl2 concentrations are 1.25, 2.5 and 5.0 mM, respectively
Mg2+
required for activity
Mg2+
-
required for activity
Mg2+
-
Km-values: 0.83-1.1 mM
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
Km-values: 0.83-1.1 mM
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
can be partially replaced by Ni2+, Mn2+ and Co2+
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
Dunaliella marina
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
required for activity, bound to ATP
Mg2+
-
required to obtain full activity of the enzyme
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
maximal activity at 2-5 mM
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
substrate activator and enzyme protein modulator
Mg2+
-
MgATP is the active substrate
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
1-10 mM are required for maximal activity
Mg2+
-
required for activity
Mg2+
-
Km-values: 0.83-1.1 mM
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
maximal activity at 5 mM, Km-value: 0.84 mM
Mg2+
-
MgATP is the active substrate
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgNTP2- is the active substrate
Mg2+
-
MgATP is the active substrate
Mg2+
-
no enzyme activity can be detected in the absence of divalent cations. Mg2+ is the most efficient divalent tested to support the reaction. The enzyme is absolutely dependent on divalent cations, forming a complex with a phosphoryl donor
Mg2+
-
required for activity
Mg2+
metal-ion dependent enzyme, highest activity (5.09 mM/min*mg) in presence of Co2+ followed by Mg2+ (3.28 mM/min*mg) at 90°C and pH 7.5
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
maximal activity approx. above 2 mM
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate
Mg2+
-
most effective ion
Mn2+
9% of activity with Mg2+
Mn2+
-
24% of activity with Mg2+
Mn2+
-
as effective as Mg2+
Mn2+
-
active substrate: MnATP2-, isoenzyme PFK2
Mn2+
-
required to obtain full activity of the enzyme. The affinity for Mn2+ is 13fold higher compared to that of Mg2+
Mn2+
-
75% of activity with Mg2+
Mn2+
-
60% of activity with Mg2+, above 3 mM
Mn2+
-
as effective as Mg2+
Mn2+
-
no enzyme activity in the absence of divalent cations. Co2+ can replace Mg2+ with 79% of the maximal activity obtained in presence of Mg2+
Mn2+
dependent on divalent metal cations. Highest activity in the presence of Co2+ (100%) followed by Mg2+ (64%), Mn2+ (64%) and Ni2+ (34%)
Mn2+
-
90% of activity with Mg2+
Ni2+
15% of activity with Mg2+
Ni2+
-
65% of activity with Mg2+
Ni2+
-
activation, 12% of activity with
Ni2+
dependent on divalent metal cations. Highest activity in the presence of Co2+ (100%) followed by Mg2+ (64%), Mn2+ (64%) and Ni2+ (34%)
Zn2+
46% of activity with Mg2+
Zn2+
-
35% of activity with Mg2+
Zn2+
-
70% of activity with Mg2+
additional information
-
not activated by Li+
additional information
-
not activated by Li+
additional information
-
Na+ has little or no effect at 140 nM PFK-1
additional information
-
Cu2+, Zn2+ and Cd2+ do not significantly support the enzymatic activity
additional information
-
Na+ has little or no effect at 140 nM PFK-1
additional information
-
K-type allosteric enzyme
additional information
-
not activated by Na+ and Rb+
additional information
-
no effect: Ni2+, Zn2+, Cu2+, Ca2+, and Fe2+