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Information on EC 1.4.1.4 - glutamate dehydrogenase (NADP+) and Organism(s) Thermococcus litoralis and UniProt Accession Q56304

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Thermococcus litoralis
UNIPROT: Q56304 not found.
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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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NADP(+)-dependent glutamate dehydrogenase
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dehydrogenase, glutamate (nicotinamide adenine dinucleotide phosphate)
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-
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glutamic acid dehydrogenase
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-
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glutamic dehydrogenase
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-
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L-glutamate dehydrogenase
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-
-
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NAD(P)H-dependent glutamate dehydrogenase
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-
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NADP-GDH
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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-
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reduction
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oxidative deamination
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reductive amination
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-
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NADP+ oxidoreductase (deaminating)
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CAS REGISTRY NUMBER
COMMENTARY hide
9029-11-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
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-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
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-
-
-
?
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
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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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
glutamate dehydrogenase represents an enzymatic link between major catabolic and biosynthetic pathways via the tricarboxylic acid cycle intermediate 2-oxoglutarate
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.0098 - 0.029
NADP+
0.14
NADPH
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reductive amination at 80°C
0.00056 - 0.00065
NH3
0.63
NH4+
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reductive amination at 80°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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oxidative deamination at 80°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
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oxidative deamination
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
270000
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gel filtration, expressed in Escherichia coli
350000
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gel filtration
45000
47000
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x * 47000, gel filtration
47169
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x * 47169, amino acid analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team