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Literature summary for 1.4.1.4 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
Search for more literature for 1.4.1.4

Protein Variants

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

General Stability

General Stability Organism
wild-type enzyme and mutant enzymes D167T and T138E are thermostabilized by threhalose. Thermococcus litoralis
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

Organism UniProt Comment Textmining
Thermococcus litoralis Q56304
-
-
Thermococcus litoralis DSM 5473 Q56304
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermococcus litoralis

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
hexamer
-
 Thermococcus litoralis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
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
87
-
 t1/2 at 5 atm at 87°C is 60 min, mutant enzyme T138E Thermococcus litoralis
90
-
 t1/2 at 5 atm at 90°C is 22 min, mutant enzyme T138E Thermococcus litoralis
92
-
 t1/2 at 5 atm at 92°C is 10 min, mutant enzyme T138E Thermococcus litoralis
99
-
 t1/2 at 5 atm at 98.8°C is 97 min, wild-type enzyme Thermococcus litoralis
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
101
-
 t1/2 at 5 atm at 101.4°C is 29 min, wild-type enzyme Thermococcus litoralis
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
103
-
 t1/2 at 5 atm at 102.9°C is 67 min, mutant enzyme D167T Thermococcus litoralis
104
-
 t1/2 at 5 atm at 104°C is 32 min, mutant enzyme D167T Thermococcus litoralis