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EC Tree
The taxonomic range for the selected organisms is: Thermococcus litoralis The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nadp-gdh, nadp-dependent glutamate dehydrogenase, nadp-glutamate dehydrogenase, nadp-specific glutamate dehydrogenase, nadp-linked glutamate dehydrogenase, nadph-dependent glutamate dehydrogenase, glutamate dehydrogenase (nadp+), nadp+-dependent glutamate dehydrogenase, nadp+-dependent gdh, nadp-dependent gdh,
more
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NADP(+)-dependent glutamate dehydrogenase
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dehydrogenase, glutamate (nicotinamide adenine dinucleotide phosphate)
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glutamic acid dehydrogenase
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glutamic dehydrogenase
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L-glutamate dehydrogenase
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NAD(P)H-dependent glutamate dehydrogenase
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oxidative deamination
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reductive amination
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L-glutamate:NADP+ oxidoreductase (deaminating)
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L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
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?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
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L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
additional information
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glutamate dehydrogenase represents an enzymatic link between major catabolic and biosynthetic pathways via the tricarboxylic acid cycle intermediate 2-oxoglutarate
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L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
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r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
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r
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L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
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r
additional information
?
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glutamate dehydrogenase represents an enzymatic link between major catabolic and biosynthetic pathways via the tricarboxylic acid cycle intermediate 2-oxoglutarate
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?
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0.16
2-oxoglutarate
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reductive amination at 80°C
0.22
L-glutamate
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oxidative deamination at 80°C
0.14
NADPH
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reductive amination at 80°C
0.63
NH4+
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reductive amination at 80°C
0.0098
NADP+
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recombinant enzyme, oxidative deamination
0.0102
NADP+
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wild-type enzyme, oxidative deamination
0.029
NADP+
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oxidative deamination at 80°C
0.00056
NH3
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recombinant enzyme, reductive amination
0.00065
NH3
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wild-type enzyme, reductive amination
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194.3
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oxidative deamination at 75°C
85
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oxidative deamination at 80°C and pH 8.0
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8
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oxidative deamination at 80°C
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95
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oxidative deamination
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SwissProt
brenda
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270000
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gel filtration, expressed in Escherichia coli
47000
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x * 47000, gel filtration
47169
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x * 47169, amino acid analysis
45000
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alpha6, 6 * 45000, SDS-PAGE, expressed in Escherichia coli
45000
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alpha6, 6 * 45000, SDS-PAGE
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?
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x * 47000, gel filtration
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x * 47169, amino acid analysis
homohexamer
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alpha6, 6 * 45000, SDS-PAGE, expressed in Escherichia coli
homohexamer
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alpha6, 6 * 45000, SDS-PAGE
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hanging-drop method of vapour diffusion using an ammonium sulfate and PEG mixture as the precipitant. The crystals belong to the monoclinic system and are in space group C2 with unit-cell dimensions a = 142.7, b = 202.0, c = 125.8 A with beta = 113.1 degrees with a hexamer in the asymmetric unit
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D167T
the mutant enzyme is slightly more thermostable than the wild-type enzyme
T138E
the mutant enzyme is much less thermostable than the wild-type enzyme
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101
t1/2 at 5 atm at 101.4°C is 29 min, wild-type enzyme
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
103
t1/2 at 5 atm at 102.9°C is 67 min, mutant enzyme D167T
104
t1/2 at 5 atm at 104°C is 32 min, mutant enzyme D167T
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
87
t1/2 at 5 atm at 87°C is 60 min, mutant enzyme T138E
90
t1/2 at 5 atm at 90°C is 22 min, mutant enzyme T138E
92
t1/2 at 5 atm at 92°C is 10 min, mutant enzyme T138E
99
t1/2 at 5 atm at 98.8°C is 97 min, wild-type enzyme
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
100
half-life: 2 h
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
85
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wild-type enzyme retains 100% activity after 3 h of incubation
85
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recombinant enzyme retains 90% activity after 3 h of incubation
85
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no activity loss after 5 h
98
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recombinant enzyme retains 50% activity after 1.5 h of incubation
98
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wild-type enzyme retains 50% activity after 6.4 h of incubation
98
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50% activity after 2 h
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wild-type enzyme and mutant enzymes D167T and T138E are thermostabilized by threhalose.
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
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expression in Escherichia coli BL21
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Ma, K.; Robb, F.T.; Adams, M.W.
Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis
Appl. Environ. Microbiol.
60
562-568
1994
Thermococcus litoralis
brenda
Robb, F.T.; Maeder, D.L.; DiRuggiero, J.; Borges, K.M.; Tolliday, N.
Glutamate dehydrogenases from hyperthermophiles
Methods Enzymol.
331
26-41
2001
Thermococcus litoralis
brenda
Sedelnikova, S.E.; Yip, K.S.; Stillman, T.J.; Ma, K.; Adams, M.W.; Robb, F.T.; Rice, D.W.
Crystallization of the glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis
Acta Crystallogr. Sect. D
52
1185-1187
1996
Thermococcus litoralis (Q56304), Thermococcus litoralis, Thermococcus litoralis DSM 5473 (Q56304)
brenda
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
Protein Sci.
10
1750-1757
2001
Thermococcus litoralis (Q56304), Thermococcus litoralis DSM 5473 (Q56304)
brenda