General Stability | Organism |
---|---|
elevated pressures up to 750 atm have a strong stabilizing effect on two extremely thermophilic glutamate dehydrogenases: the native enzyme from the hyperthermophile Pyrococcus furiosus, and a recombinant mutant enzyme containing an extra tetrapeptide at the C-terminus. The presence of the tetrapeptide greatly destabilizes the recombinant mutant at ambient pressure; however, the destabilizing effect is largely reversed by the application of pressure. Destabilization is due to weakened intersubunit ion-pair interactions induced by thermal fluctuations of the tetrapeptide. For both enzymes, the stabilizing effect of pressure increases with temperature as well as pressure, reaching 36fold for recombinant enzyme at 105°C and 750 atm | Pyrococcus furiosus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme | Pyrococcus furiosus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + H2O + NADP+ | - |
Pyrococcus furiosus | 2-oxoglutarate + NH3 + NADPH + H+ | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
85 | - |
assay at | Pyrococcus furiosus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
105 | - |
half-life: 13 min at 5 atm, 170 min at 275 atm, 360 min at 500 atm, 470 min at 750 atm, recombinant enzyme | Pyrococcus furiosus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Pyrococcus furiosus |