EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.1.40 | - |
Thermofilum pendens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.40 | AMP | dead-end inhibitor | Thermofilum pendens | |
2.7.1.40 | oxalate | dead-end inhibitor | Thermofilum pendens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.1.40 | additional information | - |
additional information | the kinetic mechanism is random order with a rapid equilibrium | Thermofilum pendens | |
2.7.1.40 | 0.092 | - |
ADP | pH 6.0, 45°C, recombinant enzyme with His6 tag | Thermofilum pendens | |
2.7.1.40 | 0.14 | - |
ADP | pH 6.0, 45°C, recombinant enzyme without His6 tag | Thermofilum pendens |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.40 | Mg2+ | although the maximum activity is 3.8-fold higher with Mg2+ than with Mn2+, the K0.5 for Mn2+ is 250fold lower than the K0.5 for Mg2+, with no significant change in the constants for the substrates. This finding shows that Mn2+ is the preferred divalent cation, consistent with the geochemistry of the Archaean ocean | Thermofilum pendens | |
2.7.1.40 | Mn2+ | although the maximum activity is 3.8-fold higher with Mg2+ than with Mn2+, the K0.5 for Mn2+ is 250fold lower than the K0.5 for Mg2+, with no significant change in the constants for the substrates. This finding shows that Mn2+ is the preferred divalent cation, consistent with the geochemistry of the Archaean ocean | Thermofilum pendens | |
2.7.1.40 | additional information | the enzyme from Thermofilum pendens is K+-independent. Eukarya pyruvate kinases have glutamate at position 117 (numbered according to the rabbit muscle enzyme), whereas in Bacteria have either glutamate or lysine and in Archaea have other residues. Glutamate at this position makes pyruvate kinases K+-dependent, whereas lysine confers K+-independence because the positively charged residue substitutes for the monovalent cation charge. The enzyme from Thermofilum pendens has Val70 at the corresponding position | Thermofilum pendens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.1.40 | Thermofilum pendens | A1RX09 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.1.40 | - |
Thermofilum pendens |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.7.1.40 | ATP + pyruvate = ADP + phosphoenolpyruvate | the kinetic mechanism is random order with a rapid equilibrium | Thermofilum pendens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.40 | ADP + phosphoenolpyruvate | the substrate binding order of the Thermofilum pendens enzyme is independent despite lacking an internal positive charge | Thermofilum pendens | ATP + pyruvate | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.1.40 | 45 | - |
assay at | Thermofilum pendens |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.1.40 | 99 | - |
thermal stability studies of this enzyme show two calorimetric transitions, one attributable to the A and C domains (Tm of 99.2°C), and the other (Tm of 105.2°C) associated with the B domain. The calorimetric and kinetic data indicate that the B domain of the hyperthermophilic enzyme is more stable than the rest of the protein with a conformation that induces the catalytic readiness of the enzyme. Intra- and interdomain interactions of the crenarchaeota enzymes may account for their higher B domain stability | Thermofilum pendens |
2.7.1.40 | 105 | - |
thermal stability studies of this enzyme show two calorimetric transitions, one attributable to the A and C domains (Tm of 99.2°C), and the other (Tm of 105.2°C) associated with the B domain. The calorimetric and kinetic data indicate that the B domain of this hyperthermophilic enzyme is more stable than the rest of the protein with a conformation that induces the catalytic readiness of the enzyme. Intra- and interdomain interactions of the crenarchaeota enzymes may account for their higher B domain stability | Thermofilum pendens |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.1.40 | additional information | - |
additional information | the kinetic mechanism is random order with a rapid equilibrium | Thermofilum pendens | |
2.7.1.40 | 0.16 | - |
ADP | pH 6.0, 45°C, in presence of Mg2+ | Thermofilum pendens | |
2.7.1.40 | 0.2 | - |
ADP | pH 6.0, 45°C, in presence of Mn2+ | Thermofilum pendens | |
2.7.1.40 | 0.38 | - |
phosphoenolpyruvate | pH 6.0, 45°C, in presence of Mg2+ | Thermofilum pendens | |
2.7.1.40 | 1 | - |
phosphoenolpyruvate | pH 6.0, 45°C, in presence of Mn2+ | Thermofilum pendens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.1.40 | 6 | - |
assay at | Thermofilum pendens |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.1.40 | 35 | - |
AMP | pH 6.0, 45°C | Thermofilum pendens |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.1.40 | additional information | - |
additional information | the kinetic mechanism is random order with a rapid equilibrium | Thermofilum pendens |