2.7.1.147: ADP-specific glucose/glucosamine kinase
This is an abbreviated version!
For detailed information about ADP-specific glucose/glucosamine kinase, go to the full flat file.
Word Map on EC 2.7.1.147
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2.7.1.147
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hyperthermophilic
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thermococcus
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embden-meyerhof
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litoralis
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phosphofructokinases
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jannaschii
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furiosus
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glucokinases
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ribokinase
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methanococcales
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thermococcales
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6-phosphofructokinase
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hexokinases
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atp-pfks
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methanosarcinales
- 2.7.1.147
-
hyperthermophilic
- thermococcus
-
embden-meyerhof
- litoralis
-
phosphofructokinases
- jannaschii
- furiosus
- glucokinases
- ribokinase
- methanococcales
- thermococcales
- 6-phosphofructokinase
- hexokinases
- atp-pfks
- methanosarcinales
Reaction
Synonyms
ADP-dependent glucokinase, ADP-dependent hexokinase, ADP-dependent kinase, ADP-GK, ADP-HK, ADP-Pfk, ADP-specific glucokinase, ADP:D-glucose 6-phosphotransferase, ADPGK, ancGK/PFK, AncMsPFK/GK, bifunctional ADP-dependent phosphofructokinase/glucokinase, GlcN kinase, glucosamine kinase, MevePFK/GK, MjPFK/GK, MmazPFK/GK, MmPFK/GK, More, NagC4, pfGK, pfkC, PhPFK, TK1110, tlGK
ECTree
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Metals Ions
Metals Ions on EC 2.7.1.147 - ADP-specific glucose/glucosamine kinase
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Ca2+
Co2+
KCl
Mg2+
Mn2+
Ni2+
additional information
Co2+
activates to less than 50% activity compared to Mg2+ activation
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+
activates to less than 50% activity compared to Mg2+ activation
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+
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+
Mn2+
activates to less than 50% activity compared to Mg2+ activation
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+
activates to less than 50% activity compared to Mg2+ activation
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+
Ni2+
activates to less than 50% activity compared to Mg2+ activation
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+
activates to less than 50% activity compared to Mg2+ activation
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+
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divalent cations are required, Mg2+, Mn2+, and Ca2+ are most effective, Cu2+, Zn2+, Ni2+, and Cu2+ can partially substitute
additional information
Ca2+ or Cu2+ cannot substitute for Mg2+
additional information
poor activation by Ca2+ probably due to steric hindrance
additional information
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poor activation by Ca2+ probably due to steric hindrance
additional information
divalent cation required, with highest activity in the presence of Mg2+
additional information
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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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poor activation by Ca2+ probably due to steric hindrance
additional information
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ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant
additional information
-
ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant
additional information
-
ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant