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Information on EC 1.4.1.3 - glutamate dehydrogenase [NAD(P)+] and Organism(s) Thermococcus profundus and UniProt Accession O74024

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Thermococcus profundus
UNIPROT: O74024 not found.
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The taxonomic range for the selected organisms is: Thermococcus profundus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
hgdh2, glutamate dehydrogenase 1, gdhii, nad(p)-dependent glutamate dehydrogenase, nad(p)+-dependent glutamate dehydrogenase, legdh1, nad(p)h-dependent glutamate dehydrogenase, nad(p)-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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHE3_THEPR
419
0
46700
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
6 * 46000
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method at 20°C, the enzyme is crystallized in the presence of both polyethylene glycol 8000 and lithium sulfate. Four types of crystals having different morphologies appeared in the crystallization trials. One type is suitable for X-ray crystal structure analysis. The crystal belongs to the monoclinic space group P2(1) and the unit-cell parameters were a = 112.99, b = 163.70, c = 133.07 A, beta = 113.46°
the active-site cleft of unligated glutamate dehydrogenase from Thermococcus profundus studied by cryogenic X-ray crystal structure analysis and small-angle X-ray scattering
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Higuchi, S.; Nakasako, M.; Kudo, T.
Crystallization and preliminary x-ray diffraction studies of hyperthermostable glutamate dehydrogenase from Thermococcus profundus
Acta Crystallogr. Sect. D
55
1917-1919
1999
Thermococcus profundus (O74024)
Manually annotated by BRENDA team
Nakasako, M.; Fujisawa, T.; Adachi, S.; Kudo, T.; Higuchi, S.
Large-scale domain movements and hydration structure changes in the active-site cleft of unligated glutamate dehydrogenase from Thermococcus profundus studied by cryogenic X-ray crystal structure analysis and small-angle X-ray scattering
Biochemistry
40
3069-3079
2001
Thermococcus profundus (O74024)
Manually annotated by BRENDA team