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Literature summary extracted from

  • Merino, F.; Rivas-Pardo, J.A.; Caniuguir, A.; Garcia, I.; Guixe, V.
    Catalytic and regulatory roles of divalent metal cations on the phosphoryl-transfer mechanism of ADP-dependent sugar kinases from hyperthermophilic archaea (2012), Biochimie, 94, 516-524.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.147 expressed in Escherichia coli Pyrococcus furiosus
2.7.1.147 expressed in Escherichia coli Pyrococcus horikoshii
2.7.1.147 expressed in Escherichia coli Thermococcus litoralis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.147 ADP
-
 Pyrococcus furiosus
2.7.1.147 ADP
-
 Pyrococcus horikoshii
2.7.1.147 ADP
-
 Thermococcus litoralis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.146 0.008
-
 ADP presence of Mg2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.146 0.008
-
 ADP presence of Mn2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.146 0.022
-
 ADP presence of Co2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.147 0.008
-
 ADP in the presence of 1 mM Mg2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.147 0.008
-
 ADP in the presence of 1 mM Mn2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.147 0.014
-
 ADP in the presence of 1 mM Mg2+, pH 7.8, 40°C Pyrococcus furiosus
2.7.1.147 0.015
-
 ADP in the presence of 1 mM Co2+, pH 7.8, 40°C Thermococcus litoralis
2.7.1.147 0.017
-
 ADP in the presence of 1 mM Mn2+, pH 7.8, 40°C Thermococcus litoralis
2.7.1.147 0.022
-
 ADP in the presence of 1 mM Co2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.147 0.022
-
 ADP in the presence of 1 mM Mn2+, pH 7.8, 40°C Pyrococcus furiosus
2.7.1.147 0.023
-
 ADP in the presence of 1 mM Mg2+, pH 7.8, 40°C Thermococcus litoralis
2.7.1.147 0.025
-
 ADP in the presence of 1 mM Co2+, pH 7.8, 40°C Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.146 additional information 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 Pyrococcus horikoshii
2.7.1.147 Co2+
-
 Pyrococcus furiosus
2.7.1.147 Co2+
-
 Pyrococcus horikoshii
2.7.1.147 Co2+ highest kcat/Km value obtained Thermococcus litoralis
2.7.1.147 Mg2+
-
 Thermococcus litoralis
2.7.1.147 Mg2+ highest kcat/Km value obtained Pyrococcus furiosus
2.7.1.147 Mg2+ highest kcat/Km value obtained Pyrococcus horikoshii
2.7.1.147 Mn2+
-
 Pyrococcus furiosus
2.7.1.147 Mn2+
-
 Thermococcus litoralis
2.7.1.147 Mn2+ highest kcat/Km value obtained Pyrococcus horikoshii
2.7.1.147 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 Pyrococcus furiosus
2.7.1.147 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 Pyrococcus horikoshii
2.7.1.147 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 Thermococcus litoralis

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.146 Pyrococcus horikoshii
-
-
-
2.7.1.147 Pyrococcus furiosus
-
-
-
2.7.1.147 Pyrococcus horikoshii
-
-
-
2.7.1.147 Thermococcus litoralis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.146 ADP + D-fructose 6-phosphate
-
 Pyrococcus horikoshii AMP + D-fructose 1,6-bisphosphate
-
 ?
2.7.1.147 ADP + D-fructose 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 Pyrococcus horikoshii AMP + D-fructose 6-phosphate
-
 ?
2.7.1.147 ADP + D-glucose 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 Pyrococcus furiosus AMP + D-glucose 6-phosphate
-
 ?
2.7.1.147 ADP + D-glucose 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 Thermococcus litoralis AMP + D-glucose 6-phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.147 pfGK
-
 Pyrococcus furiosus
2.7.1.147 PhPFK
-
 Pyrococcus horikoshii
2.7.1.147 tlGK
-
 Thermococcus litoralis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.147 40
-
 assay at Pyrococcus furiosus
2.7.1.147 40
-
 assay at Thermococcus litoralis
2.7.1.147 50
-
 assay at Pyrococcus horikoshii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.146 52
-
 ADP presence of Mg2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.146 67
-
 ADP presence of Mn2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.146 98
-
 ADP presence of Co2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.147 21
-
 ADP in the presence of 1 mM Mn2+, pH 7.8, 40°C Thermococcus litoralis
2.7.1.147 35
-
 ADP in the presence of 1 mM Mg2+, pH 7.8, 40°C Thermococcus litoralis
2.7.1.147 44
-
 ADP in the presence of 1 mM Co2+, pH 7.8, 40°C Thermococcus litoralis
2.7.1.147 52
-
 ADP in the presence of 1 mM Mg2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.147 67
-
 ADP in the presence of 1 mM Mn2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.147 98
-
 ADP in the presence of 1 mM Co2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.147 104
-
 ADP in the presence of 1 mM Mg2+, pH 7.8, 40°C Pyrococcus furiosus
2.7.1.147 114
-
 ADP in the presence of 1 mM Co2+, pH 7.8, 40°C Pyrococcus furiosus
2.7.1.147 116
-
 ADP in the presence of 1 mM Mn2+, pH 7.8, 40°C Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.147 6.5
-
 assay at Pyrococcus furiosus
2.7.1.147 6.5
-
 assay at Pyrococcus horikoshii
2.7.1.147 6.5
-
 assay at Thermococcus litoralis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.1.147 0.3
-
 ADP pH 7.8, 40°C Thermococcus litoralis
2.7.1.147 0.58
-
 ADP pH 7.8, 40°C Pyrococcus furiosus
2.7.1.147 3.4
-
 ADP pH 6.5, 40°C Pyrococcus horikoshii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.1.146 4400
-
 ADP presence of Co2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.146 6500
-
 ADP presence of Mg2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.146 8400
-
 ADP presence of Mn2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.147 1200
-
 ADP in the presence of 1 mM Mn2+, pH 7.8, 40°C Thermococcus litoralis
2.7.1.147 1500
-
 ADP in the presence of 1 mM Mg2+, pH 7.8, 40°C Thermococcus litoralis
2.7.1.147 2900
-
 ADP in the presence of 1 mM Co2+, pH 7.8, 40°C Thermococcus litoralis
2.7.1.147 4400
-
 ADP in the presence of 1 mM Co2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.147 4600
-
 ADP in the presence of 1 mM Co2+, pH 7.8, 40°C Pyrococcus furiosus
2.7.1.147 5300
-
 ADP in the presence of 1 mM Mn2+, pH 7.8, 40°C Pyrococcus furiosus
2.7.1.147 6500
-
 ADP in the presence of 1 mM Mg2+, pH 6.5, 50°C Pyrococcus horikoshii
2.7.1.147 7400
-
 ADP in the presence of 1 mM Mg2+, pH 7.8, 40°C Pyrococcus furiosus
2.7.1.147 8400
-
 ADP in the presence of 1 mM Mn2+, pH 6.5, 50°C Pyrococcus horikoshii