KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.008 | - |
ADP | presence of Mg2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
0.008 | - |
ADP | presence of Mn2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
0.022 | - |
ADP | presence of Co2+, pH 6.5, 50°C | Pyrococcus horikoshii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + D-fructose 6-phosphate | - |
Pyrococcus horikoshii | AMP + D-fructose 1,6-bisphosphate | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
52 | - |
ADP | presence of Mg2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
67 | - |
ADP | presence of Mn2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
98 | - |
ADP | presence of Co2+, pH 6.5, 50°C | Pyrococcus horikoshii |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4400 | - |
ADP | presence of Co2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
6500 | - |
ADP | presence of Mg2+, pH 6.5, 50°C | Pyrococcus horikoshii | |
8400 | - |
ADP | presence of Mn2+, pH 6.5, 50°C | Pyrococcus horikoshii |