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Literature summary extracted from

  • Sun, M.M.; Caillot, R.; Mak, G.; Robb, F.T.; Clark, D.S.
    Mechanism of pressure-induced thermostabilization of proteins: studies of glutamate dehydrogenases from the hyperthermophile Thermococcus litoralis (2001), Protein Sci., 10, 1750-1757.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.4.1.4 D167T the mutant enzyme is slightly more thermostable than the wild-type enzyme Thermococcus litoralis
1.4.1.4 T138E the mutant enzyme is much less thermostable than the wild-type enzyme Thermococcus litoralis

General Stability

EC Number General Stability Organism
1.4.1.4 wild-type enzyme and mutant enzymes D167T and T138E are thermostabilized by threhalose. Thermococcus litoralis
1.4.1.4 wild-type enzyme and mutant enzymes D167T and T138E are thermostabilized, although to different degrees, by the application of 500 atm. The degree of pressure stabilization correlated with GDH stability as well as the magnitude of electrostatic repulsion created by residues at positions 138 and 167 Thermococcus litoralis

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.4 Thermococcus litoralis Q56304
-
-
1.4.1.4 Thermococcus litoralis DSM 5473 Q56304
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.4
-
 Thermococcus litoralis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.4 L-glutamate + H2O + NADP+
-
 Thermococcus litoralis 2-oxoglutarate + NH3 + NADPH + H+
-
 ?
1.4.1.4 L-glutamate + H2O + NADP+
-
 Thermococcus litoralis DSM 5473 2-oxoglutarate + NH3 + NADPH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.1.4 hexamer
-
 Thermococcus litoralis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.1.4 additional information
-
 wild-type enzyme and mutant enzymes D167T and T138E are thermostabilized, although to different degrees, by the application of 500 atm. The degree of pressure stabilization correlated with GDH stability as well as the magnitude of electrolyte is proposed that pressure stabilizes against thermoinactivation by shifting the equilibrium between conformational substrates of the glutamate dehydrogenase hexamer, thus inhibiting irreversible aggregation Thermococcus litoralis
1.4.1.4 86
-
 t1/2 at 5 atm at 86°C is 68 min withjout trehalose and 50 min in presence of 0.5 M trehalose, mutant enzyme T138E Thermococcus litoralis
1.4.1.4 87
-
 t1/2 at 5 atm at 87°C is 60 min, mutant enzyme T138E Thermococcus litoralis
1.4.1.4 90
-
 t1/2 at 5 atm at 90°C is 22 min, mutant enzyme T138E Thermococcus litoralis
1.4.1.4 92
-
 t1/2 at 5 atm at 92°C is 10 min, mutant enzyme T138E Thermococcus litoralis
1.4.1.4 99
-
 t1/2 at 5 atm at 98.8°C is 97 min, wild-type enzyme Thermococcus litoralis
1.4.1.4 100
-
 t1/2 at 5 atm at 100°C is 79 min without trehalose and 185 min in presence of 0.5 M trehalose, wild-type enzyme Thermococcus litoralis
1.4.1.4 101
-
 t1/2 at 5 atm at 101.4°C is 29 min, wild-type enzyme Thermococcus litoralis
1.4.1.4 102
-
 t1/2 at 5 atm at 101.5°C is 80 min without trehalose and 129 min in presence of 0.5 M trehalose, mutant enzyme D167T Thermococcus litoralis
1.4.1.4 103
-
 t1/2 at 5 atm at 102.9°C is 67 min, mutant enzyme D167T Thermococcus litoralis
1.4.1.4 104
-
 t1/2 at 5 atm at 104°C is 32 min, mutant enzyme D167T Thermococcus litoralis