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Information on EC 1.4.1.3 - glutamate dehydrogenase [NAD(P)+] and Organism(s) Thermococcus kodakarensis and UniProt Accession O59650

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Thermococcus kodakarensis
UNIPROT: O59650 not found.
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The taxonomic range for the selected organisms is: Thermococcus kodakarensis
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
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
show the reaction diagram
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.3
2-oxoglutarate
0.04 - 0.1
NADPH
2.5 - 13
NH3
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the specific activity of the hexameric form of the recombinant enzyme is much lower than that of the natural enzyme. The structure of the hexameric form of the recombinant enzyme with low specific activity (Type I) is different from that of the natural enzyme with high specific activity (Type II). Upon heat treatment (80°C, 15 min), the Type I structure is effectively converted to Type II structure and the specific activity of the enzyme is increased by 2.6fold
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
oxidative deamination and reductive amination
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 90
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
in a gene disruption strain of GDH, only threonine dehydrogenase activity is detected, indicating that activities toward Gln/Ala/Val/Cys are dependent on GDH. The disruption strain cannot grow in a medium in which growth is dependent on amino acid catabolism, GDH may be the only enzyme that can discharge the electrons (to NADP+/NAD+) released from amino acids in their oxidation to 2-oxoacids. In a medium containing excess pyruvate, the disprution strain displays normal growth, but higher degrees of amino acid catabolism are observed
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
284000
gel filtration
47040
6 * 47040, calculated from sequence, the natural enzyme was purified only as a hexameric form, whereas the recombinant enzyme was purified as both monomeric and hexameric forms. Only the enzyme in a hexameric form is active. Upon heat treatment (70°C for 15 min), the inactive monomeric form of the recombinant enzyme is at least partially associated with the hexameric form
47300
6 * 47300, SDS-PAGE, the natural enzyme was purified only as a hexameric form, whereas the recombinant enzyme was purified as both monomeric and hexameric forms. Only the enzyme in a hexameric form is active. Upon heat treatment (70°C for 15 min), the inactive monomeric form of the recombinant enzyme is at least partially associated with the hexameric form
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. The specific activity of the hexameric form of the recombinant enzyme is much lower than that of the natural enzyme. The structure of the hexameric form of the recombinant enzyme with low specific activity (Type I) is different from that of the natural enzyme with high specific activity (Type II). Upon heat treatment (80°C, 15 min), the Type I structure is effectively converted to Type II structure and the specific activity of the enzyme is increased by 2.6fold
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abd Rahman, R.N.; Fujiwara, S.; Takagi, M.; Kanaya, S.; Imanaka, T.
Effect of heat treatment on proper oligomeric structure formation of thermostable glutamate dehydrogenase from a hyperthermophilic archaeon
Biochem. Biophys. Res. Commun.
241
646-652
1997
Thermococcus kodakarensis (O59650)
Manually annotated by BRENDA team
Yokooji, Y.; Sato, T.; Fujiwara, S.; Imanaka, T.; Atomi, H.
Genetic examination of initial amino acid oxidation and glutamate catabolism in the hyperthermophilic archaeon Thermococcus kodakarensis
J. Bacteriol.
195
1940-1948
2013
Thermococcus kodakarensis (O59650)
Manually annotated by BRENDA team