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Literature summary for 1.4.1.4 extracted from

  • Sun, M.M.; Tolliday, N.; Vetriani, C.; Robb, F.T.; Clark, D.S.
    Pressure-induced thermostabilization of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus (1999), Protein Sci., 8, 1056-1063.
    View publication on PubMedView publication on EuropePMC

General Stability

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

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Pyrococcus furiosus

Substrates and Products (Substrate)

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
85
-
assay at Pyrococcus furiosus

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Pyrococcus furiosus