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Information on EC 1.4.1.2 - glutamate dehydrogenase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P33327

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Saccharomyces cerevisiae
UNIPROT: P33327 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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L-glutamate
+
H2O
+
NAD+
=
2-oxoglutarate
+
NH3
+
NADH
+
H+
+
+
=
+
+
+
Synonyms
glutamate dehydrogenase, gdh, glud1, hgdh1, glutamic dehydrogenase, nad-gdh, l-glutamate dehydrogenase, nad-dependent glutamate dehydrogenase, nadh-gdh, glutamic acid dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutamate dehydrogenase 2
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NAD-dependent glutamate dehydrogenase
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dehydrogenase, glutamate
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GDH
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glutamate dehydrogenase (NAD)
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glutamate oxidoreductase
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glutamic acid dehydrogenase
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glutamic dehydrogenase
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L-glutamate dehydrogenase
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NAD-dependent glutamate dehydrogenase
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NAD-dependent glutamic dehydrogenase
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NAD-GDH
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-
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NAD-glutamate dehydrogenase
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NAD-linked glutamate dehydrogenase
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NAD-linked glutamic dehydrogenase
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NAD-specific glutamate dehydrogenase
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NAD-specific glutamic dehydrogenase
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NAD:glutamate oxidoreductase
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NADH-dependent glutamate dehydrogenase
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NADH-linked glutamate dehydrogenase
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Surface-associated protein PGAG1
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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+ oxidoreductase (deaminating)
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CAS REGISTRY NUMBER
COMMENTARY hide
9001-46-1
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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
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
additional information
?
-
-
in yeast, NADP+-dependent enzymes, EC 1.4.1.4, encoded by GDH1 and GDH3, are reported to synthesize glutamate from 2-oxtoglutarate, while an NAD+-dependent enzyme, EC 1.4.1.2, encoded by GDH2, catalyzes the reverse reaction. Gdh1p is the primary GDH enzyme and Gdh2p and Gdh3p play evident roles during aerobic glutamate metabolism
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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 + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
ir
additional information
?
-
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in yeast, NADP+-dependent enzymes, EC 1.4.1.4, encoded by GDH1 and GDH3, are reported to synthesize glutamate from 2-oxtoglutarate, while an NAD+-dependent enzyme, EC 1.4.1.2, encoded by GDH2, catalyzes the reverse reaction. Gdh1p is the primary GDH enzyme and Gdh2p and Gdh3p play evident roles during aerobic glutamate metabolism
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the disruption of GDH2 was not deleterious to glutamate homeostasis. Mutant gdh2DELTA cells present wild-type growth and do not display any deficiencies due to glutamate homeostasis impairment neither under glucose nor under non-fermentable carbon sources. Deletion of GDH2 gene in a gdh3DELTA background increases the resistance under thermal or oxidative stress by decreasing ROS accumulation. The apoptosis is suppressed by GDH2 deletion through the elevated levels of glutamate and glutathione present in the double mutant. Under the tested conditions, deletion of GDH2 compensates the depletion of intracellular glutamate and glutathione (GSH) followed by stress-induced apoptotic cell death reinforcing further the idea that Gdh2p is responsible only for glutamate catabolism and not its production
metabolism
through the enzymatic activity of Gdh2p the breakdown of glutamate provides adequate levels of ammonia in yeast cells. The catabolism of glutamate via the NAD-GDH activity is the major pathway of ammonia generation in vivo. Synthesis of glutamate occurs through the action of NADP-GDH (encoded by GDH1 and GDH3 genes, EC 1.4.1.4). NAD-GDH activity (encoded by GDH2) is responsible for glutamate degradation and release of ammonium and 2-oxoglutarate. The role of GDH1 and GDH2 is contradictory when investigated in yeast strains under cold-growth conditions
physiological function
physiological function
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Gdh2p plays an evident role during aerobic glutamate metabolism
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
isozyme Gdh2p can be converted from an active NAD-dependent glutamate dehydrogenase to an inactive form by phosphorylation through cAMP-dependent and cAMP-independent protein kinases
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of an enzyme deletion DELTAgdh2 mutant, the mutant shows less than 15-20% of wild-type activity, but DELTAgdh3 shows 20fold increased NAD+-dependent GDH activity, EC 1.4.1.2, genotypes and phenotypes, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gdh2, GDH2 is encoded on chromosome IV
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in the presence of preferred nitrogen sources, the expression of GDH2 is repressed by the transcriptional regulator Ure2 which sequesters Gln3 into the cytoplasm. The expression of GDH2 is regulated by the concurrent action of Gcn4 and Gln3. These two regulatory networks have been thought to interact, putting forward the existence of a physiological relation between Gln3 and Gcn4. Under nitrogen derepressive conditions and amino acid deprivation, Gcn4 and Gln3 form part of a transcriptional complex that binds on GDH2 promoter and dictates its expression. Overexpression of GDH2 is favoring yeast growth providing a growth advantage
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
a high-copy number of the GDH2-encoded NADH-specific glutamate dehydrogenase gene stimulates growth at 15°C, while overexpression of NADPH-specific GDH1 has detrimental effects. Total cellular NAD levels are a limiting factor for growth at low temperature in Saccharomyces cerevisiae. Increasing NADH oxidation by overexpression of GDH2 may help to avoid perturbations in the redox metabolism induced by a higher fermentative/oxidative balance at low temperature. Overexpression of GDH2 increases notably the cold growth in the wine yeast strain QA23 in both standard growth medium and synthetic grape must
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Smith, E.L.; Austen, B.M.; Blumenthal, K.M.; Nyc, J.F.
Glutamate dehydrogenase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
11
293-367
1975
Achlya sp. (in: Oomycetes), Apodachlya sp., Blastocladiella emersonii, Saccharomyces cerevisiae, Clostridium sp., Micrococcus aerogenes, Neurospora crassa, Peptoniphilus asaccharolyticus, Pisum sativum, Globisporangium debaryanum, Starkeya novella, Clostridium sp. SB4
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Manually annotated by BRENDA team
Tang, Y.; Sieg, A.; Trotter, P.J.
13C-metabolic enrichment of glutamate in glutamate dehydrogenase mutants of Saccharomyces cerevisiae
Microbiol. Res.
166
521-530
2011
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Ballester-Tomas, L.; Randez-Gil, F.; Perez-Torrado, R.; Prieto, J.A.
Redox engineering by ectopic expression of glutamate dehydrogenase genes links NADPH availability and NADH oxidation with cold growth in Saccharomyces cerevisiae
Microb. Cell Fact.
14
100
2015
Saccharomyces cerevisiae (P33327), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mara, P.; Fragiadakis, G.S.; Gkountromichos, F.; Alexandraki, D.
The pleiotropic effects of the glutamate dehydrogenase (GDH) pathway in Saccharomyces cerevisiae
Microb. Cell Fact.
17
170
2018
Saccharomyces cerevisiae (P33327), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P33327)
Manually annotated by BRENDA team