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Information on EC 1.4.1.3 - glutamate dehydrogenase [NAD(P)+] and Organism(s) Thermococcus litoralis and UniProt Accession Q56304

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This record set is specific for:
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
hgdh2, glutamate dehydrogenase 1, gdhii, nad(p)-dependent glutamate dehydrogenase, legdh1, nad(p)+-dependent glutamate dehydrogenase, nad(p)-glutamate dehydrogenase, nad(p)h-dependent glutamate dehydrogenase, ttgdh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate))
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GDH
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glutamic acid dehydrogenase
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glutamic dehydrogenase
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L-glutamate dehydrogenase
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L-glutamic acid dehydrogenase
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Legdh1
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Membrane protein 50
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MP50
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NAD(P)-glutamate dehydrogenase
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NAD(P)H-dependent glutamate dehydrogenase
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NAD(P)H-utilizing glutamate dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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reductive amination
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NAD(P)+ oxidoreductase (deaminating)
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CAS REGISTRY NUMBER
COMMENTARY hide
9029-12-3
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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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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
addition of Ca2+ and Mg2+ also shows enhancement of enzyme activity. 1.3fold increase in activity at 10 mM CaCl2 or MgSO4
Mg2+
addition of Ca2+ and Mg2+ also shows enhancement of enzyme activity. 1.3fold increase in activity at 10 mM CaCl2 or MgSO4
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
pH 6.5: about 50% of maximal activity, pH 8.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
97
specific activity increases up to 97°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method of vapour diffusion, crystals belong to space group C2 with a hexamer in the asymmetric unit and have lattice constants a = 141.9 A, b = 197.5 A and c = 125.7 A with beta = 113.6°, the crystal structure of the extremely thermostable glutamate dehydrogenase from Thermococcus litoralis determined at 2.5 A resolution is compared to that from the hyperthermophile Pyrococcus furiosus. The less stable Thermococcus litoralis enzyme has a decreased number of ion pair interactions; modified patterns of hydrogen bonding resulting from isosteric sequence changes; substitutions that decrease packing efficiency; and substitutions which give rise to subtle but distinct shifts in both main-chain and side-chain elements of the structure
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104
half-life: 4.9 min in absence of KCl, 45 min in presence of 1 M KCl
98
half-life: 2 h. alignment of the sequences for the thermophilic glutamate dehydrogenases from Thermococcus litoralis and Pyrococcus furiosus against the sequence and the molecular structure of the glutamate dehydrogenase from the mesophile Clostridium symbiosum provides insights into the molecular basis of their thermostability. A relatively small number of amino acid substitutions is observed between the two thermophilic glutamate dehydrogenase sequences. The most frequent amino acid exchanges involves substitutions which increase the hydrophobicity and sidechain branching in the more thermostable enzyme. Particularly common is the substitution of valine to isoleucine. Examination of the sequence differences suggests that enhanced packing within the buried core of the protein plays an important role in maintaining stability at extreme temperatures. One hot spot for the accumulation of exchanges lies close to a region of the molecule involved in its conformational flexibility and these changes may modulate the dynamics of this enzyme and thereby contribute to increased stability
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Britton, K.L.; Yip, K.S.; Sedelnikova, S.E.; Stillman, T.J.; Adams, M.W.; Ma, K.; Maeder, D.L.; Robb, F.T.; Tolliday, N.; Vetriani, C.; Rice, D.W.; Baker, P.J.
Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus
J. Mol. Biol.
293
1121-1132
1999
Thermococcus litoralis (Q56304)
Manually annotated by BRENDA team
Britton, K.; Baker, P.; Borges, K.; Engel, P.; Pasquo, A.; Rice, D.; Robb, F.; Scandurra, R.; Stillman, T.; Yip, K.
Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis
Eur. J. Biochem.
229
688-695
1995
Pyrococcus furiosus (P80319), Thermococcus litoralis (Q56304), Thermococcus litoralis DSM 5473 (Q56304)
Manually annotated by BRENDA team
Lee, M.; Gonzlez, J.; Robb, F.
Extremely thermostable glutamate dehydrogenase (GDH) from the freshwater archaeon Thermococcus waiotapuensis Cloning and comparison with two marine hyperthermophilic GDHs
Extremophiles
6
151-159
2002
Pyrococcus furiosus (P80319), Thermococcus litoralis (Q56304), Thermococcus litoralis DSM 5473 (Q56304)
Manually annotated by BRENDA team