2.7.1.146: ADP-specific phosphofructokinase
This is an abbreviated version!
For detailed information about ADP-specific phosphofructokinase, go to the full flat file.
Word Map on EC 2.7.1.146
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2.7.1.146
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hyperthermophilic
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embden-meyerhof
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archaeon
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methanococcus
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jannaschii
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amp
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furiosus
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thermococcus
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atp-pfks
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phosphofructokinases
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ppi-dependent
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fructose-1,6-bisphosphate
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sulfate-reducing
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archaeoglobus
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fulgidus
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pyrophosphate-dependent
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zilligii
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thermococcales
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eucarya
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horikoshii
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adp-forming
- 2.7.1.146
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hyperthermophilic
-
embden-meyerhof
- archaeon
-
methanococcus
- jannaschii
- amp
- furiosus
- thermococcus
- atp-pfks
-
phosphofructokinases
-
ppi-dependent
- fructose-1,6-bisphosphate
-
sulfate-reducing
-
archaeoglobus
- fulgidus
-
pyrophosphate-dependent
- zilligii
- thermococcales
- eucarya
- horikoshii
-
adp-forming
Reaction
Synonyms
ADP dependent phosphofructokinase, ADP-6-phosphofructokinase, ADP-dependent 6-phosphofructokinase, ADP-dependent glucokinase, ADP-dependent glucokinase/phosphofructokinase, ADP-dependent PFK, ADP-dependent phosphofructokinase, ADP-GK, ADP-Pfk, ancGK/PFK, AncMsPFK/GK, bifunctional ADP-dependent phosphofructokinase/glucokinase, MevePFK/GK, MJ1604, MjPFK/GK, MmazPFK/GK, MmPFK/GK, More, PFK, PFK-ADP, pfkC, PhPFK, TK0376, TLPFK
ECTree
2.7.1.146 ADP-specific phosphofructokinaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 2.7.1.146 - ADP-specific phosphofructokinase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
CaCl2
2 mM ADP and 2 mM D-fructose 6-phosphate, CaCl2 show the lowest activity with 75% of the activity measured in the presence of MgCl2, activity does not change with the cation concentration in the range of 2.5 to 7 mM
Co2+
KCl
Mg2+
MgSO4
2 mM ADP and 2 mM D-fructose 6-phosphate, magnesium is tested with 2 counter ions to discard any effect of the anion
Mn2+
MnCl2
2 mM ADP and 2 mM D-fructose 6-phosphate, increase in enzyme activity with the increase in MnCl2 concentration from 2.5 to 7 mM is observed
Ni2+
NiSO4
2 mM ADP and 2 mM D-fructose 6-phosphate, highest PhPFK activity is obtained with NiSO4 (97 units/mg), decrease in enzyme activity with the increase in MnCl2 concentration from 2.5 to 7 mM is observed
ZnCl2
2 mM ADP and 2 mM D-fructose 6-phosphate, no significant activity
additional information
Ca2+
activity is highest in the presence of CaCl2, followed by MgCl2, Co2+ and Mn2+
Co2+
activity is highest in the presence of CaCl2, followed by MgCl2, Co2+ and Mn2+
Co2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
Co2+
2 mM, divalent metal ion required, activation of phosphofructokinase activity with Co2+ is about 70% compared to the activation with Mg2+, activation of glucokinase activity is about 35% compared to the activation with Mg2+
Co2+
among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured
Co2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the 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
Mg2+
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most efficient divalent cation, can be replaced by Ni2+, Co2+, and Mn2+
Mg2+
activity is highest in the presence of CaCl2, followed by MgCl2, Co2+ and Mn2+
Mg2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
Mg2+
2 mM, divalent metal ion required, highest activity is observed in the presence of Mg2+
Mg2+
among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured
Mg2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
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
Mn2+
activity is highest in the presence of CaCl2, followed by MgCl2, Co2+ and Mn2+
Mn2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
Mn2+
2 mM, divalent metal ion required, activation of phosphofructokinase activity with Co2+ is about 25% compared to the activation with Mg2+, activation of glucokinase activity is about 20% compared to the activation with Mg2+
Mn2+
among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured
Mn2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the 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%)
Ni2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
Ni2+
2 mM, divalent metal ion required, activation of phosphofructokinase activity with Co2+ is about 30% compared to the activation with Mg2+, activation of glucokinase activity is less than 10% compared to the activation with Mg2+
Ni2+
among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured
Ni2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
Ni2+
dependent on divalent metal cations. Highest activity in the presence of Co2+ (100%) followed by Mg2+ (64%), Mn2+ (64%) and Ni2+ (34%)
additional information
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divalent cations are required for activity, Zn2+, Ca2+, and Cu2+ are poor metal cofactors
additional information
poor activation by Ca2+ probably due to steric hindrance
additional information
divalent cation required, with highest activity in the presence of Mg2+
additional information
poor activation by Ca2+ probably due to steric hindrance
additional information
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no significant activity is detected in the presence of Zn2+
additional information
no significant activity is detected in the presence of Zn2+
additional information
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divalent cation is strictly required for activity, the true substrate seems to be the metal-nucleotide complex. The enzyme is promiscuous in relation to its metal usage where the only considerations for metal assisted catalysis seem to be related to the ionic radii and coordination geometry of the cations. The metal cation is bound to the highly conserved NXXE motif, which constitutes one of the signatures of the ribokinase superfamily. The binding of a second metal to the enzyme produces a complex with a reduced catalytic constant
additional information
the phosphofructokinase activity of the enzyme is metal ion-dependent, the highest activity is found in the presence of Co2+, followed by Mg2+ at 90°C and pH 7.5. 18% of maximal activity is shown in absence of metal ions
additional information
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the phosphofructokinase activity of the enzyme is metal ion-dependent, the highest activity is found in the presence of Co2+, followed by Mg2+ at 90°C and pH 7.5. 18% of maximal activity is shown in absence of metal ions
