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Information on EC 1.4.1.3 - glutamate dehydrogenase [NAD(P)+] and Organism(s) Arabidopsis thaliana and UniProt Accession Q38946

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Arabidopsis thaliana
UNIPROT: Q38946 not found.
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
At5g07440
gene name, beta-subunit
At5g18170
gene name, alpha-subunit
dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate))
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GDH
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GDH2
gene name, beta-subunit
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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NADH-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 + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
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r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
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r
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 + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
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r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in the nitrogen distribution during primary assimilation, photorespiratory re-assimilation and translocation in Arabidopsis thaliana, overview. Traditional route of glutamate formation via the 2-oxoglutarate amination with NH4+ is persued by mitochondrial NADH-glutamate dehydrogenase
physiological function
in vitro, GDH catalyzes the reversible deamination of Glu to NH4 +, 2-oxoglutarate forming NADH. The reversible lethal phenotype of gltS mutants reveals that mitochondrial NADH-GDH is unable to re-assimilate photorespiratory NH3 produced within the same organelle although its amination activity. In vitro is several fold higher than the glutamate synthase isozyme Fd-GOGAT (EC 1.4.7.1) activity. The in vivo direction of reversible NADH-GDH reaction is controversial. NADH-GDH can exist as two homohexamers of either alpha subunit encoded by GDH1 or beta subunit encoded by GDH2 and five heterohexamers containing both alpha and beta subunits in Arabidopsis thaliana as observed in other plants
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHE2_ARATH
411
0
44699
Swiss-Prot
Mitochondrion (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of the hexameric structure of the GDH3 isoenzyme, it is highly symmetric and is formed by the assembly of two equivalent trimers with a three-fold symmetry
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I397V/I406L/S411A
mutation to residues found in isoforms Gdh1 and Gdh2, increase in thermal stability
I406L/S411A
mutation to residues found in isoforms Gdh1 and Gdh2, increase in thermal stability
S411A
mutation to residue found in isoforms Gdh1 and Gdh2, increase in thermal stability
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
20 min, the Gdh2 homohexamer and the Gdh2/Gdh1 heterohexamers remain active
75
20 min, the Gdh1homohexamer and the Gdh2/Gdh1 heterohexamers remain active
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Marchi, L.; Polverini, E.; Degola, F.; Baruffini, E.; Restivo, F.M.
Glutamate dehydrogenase isoenzyme 3 (GDH3) of Arabidopsis thaliana is less thermostable than GDH1 and GDH2 isoenzymes
Plant Physiol. Biochem.
83
225-231
2014
Arabidopsis thaliana (Q38946), Arabidopsis thaliana (Q43314), Arabidopsis thaliana (Q9S7A0)
Manually annotated by BRENDA team
Suzuki, A.
Glutamate synthase and amino acid synthesis in higher plants
Adv. Bot. Res.
100
129
2021
Arabidopsis thaliana (Q43314 AND Q38946)
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Manually annotated by BRENDA team