Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Pyrococcus furiosus |
expressed in Escherichia coli | Pyrococcus horikoshii |
expressed in Escherichia coli | Thermococcus litoralis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Pyrococcus furiosus | |
ADP | - |
Pyrococcus horikoshii | |
ADP | - |
Thermococcus litoralis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.008 | - |
ADP | in the presence of 1 mM Mg2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
0.008 | - |
ADP | in the presence of 1 mM Mn2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
0.014 | - |
ADP | in the presence of 1 mM Mg2+, pH 7.8, 40°C | Pyrococcus furiosus | |
0.015 | - |
ADP | in the presence of 1 mM Co2+, pH 7.8, 40°C | Thermococcus litoralis | |
0.017 | - |
ADP | in the presence of 1 mM Mn2+, pH 7.8, 40°C | Thermococcus litoralis | |
0.022 | - |
ADP | in the presence of 1 mM Co2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
0.022 | - |
ADP | in the presence of 1 mM Mn2+, pH 7.8, 40°C | Pyrococcus furiosus | |
0.023 | - |
ADP | in the presence of 1 mM Mg2+, pH 7.8, 40°C | Thermococcus litoralis | |
0.025 | - |
ADP | in the presence of 1 mM Co2+, pH 7.8, 40°C | Pyrococcus furiosus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | - |
Pyrococcus furiosus | |
Co2+ | - |
Pyrococcus horikoshii | |
Co2+ | highest kcat/Km value obtained | Thermococcus litoralis | |
Mg2+ | - |
Thermococcus litoralis | |
Mg2+ | highest kcat/Km value obtained | Pyrococcus furiosus | |
Mg2+ | highest kcat/Km value obtained | Pyrococcus horikoshii | |
Mn2+ | - |
Pyrococcus furiosus | |
Mn2+ | - |
Thermococcus litoralis | |
Mn2+ | highest kcat/Km value obtained | Pyrococcus horikoshii | |
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 | |
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 | |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | - |
- |
- |
Pyrococcus horikoshii | - |
- |
- |
Thermococcus litoralis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? | |
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 | - |
? | |
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 | Comment | Organism |
---|---|---|
pfGK | - |
Pyrococcus furiosus |
PhPFK | - |
Pyrococcus horikoshii |
tlGK | - |
Thermococcus litoralis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
assay at | Pyrococcus furiosus |
40 | - |
assay at | Thermococcus litoralis |
50 | - |
assay at | Pyrococcus horikoshii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
21 | - |
ADP | in the presence of 1 mM Mn2+, pH 7.8, 40°C | Thermococcus litoralis | |
35 | - |
ADP | in the presence of 1 mM Mg2+, pH 7.8, 40°C | Thermococcus litoralis | |
44 | - |
ADP | in the presence of 1 mM Co2+, pH 7.8, 40°C | Thermococcus litoralis | |
52 | - |
ADP | in the presence of 1 mM Mg2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
67 | - |
ADP | in the presence of 1 mM Mn2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
98 | - |
ADP | in the presence of 1 mM Co2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
104 | - |
ADP | in the presence of 1 mM Mg2+, pH 7.8, 40°C | Pyrococcus furiosus | |
114 | - |
ADP | in the presence of 1 mM Co2+, pH 7.8, 40°C | Pyrococcus furiosus | |
116 | - |
ADP | in the presence of 1 mM Mn2+, pH 7.8, 40°C | Pyrococcus furiosus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Pyrococcus furiosus |
6.5 | - |
assay at | Pyrococcus horikoshii |
6.5 | - |
assay at | Thermococcus litoralis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.3 | - |
ADP | pH 7.8, 40°C | Thermococcus litoralis | |
0.58 | - |
ADP | pH 7.8, 40°C | Pyrococcus furiosus | |
3.4 | - |
ADP | pH 6.5, 40°C | Pyrococcus horikoshii |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1200 | - |
ADP | in the presence of 1 mM Mn2+, pH 7.8, 40°C | Thermococcus litoralis | |
1500 | - |
ADP | in the presence of 1 mM Mg2+, pH 7.8, 40°C | Thermococcus litoralis | |
2900 | - |
ADP | in the presence of 1 mM Co2+, pH 7.8, 40°C | Thermococcus litoralis | |
4400 | - |
ADP | in the presence of 1 mM Co2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
4600 | - |
ADP | in the presence of 1 mM Co2+, pH 7.8, 40°C | Pyrococcus furiosus | |
5300 | - |
ADP | in the presence of 1 mM Mn2+, pH 7.8, 40°C | Pyrococcus furiosus | |
6500 | - |
ADP | in the presence of 1 mM Mg2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
7400 | - |
ADP | in the presence of 1 mM Mg2+, pH 7.8, 40°C | Pyrococcus furiosus | |
8400 | - |
ADP | in the presence of 1 mM Mn2+, pH 6.5, 50°C | Pyrococcus horikoshii |