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Literature summary for 1.4.1.4 extracted from

  • Lee, W.H.; Oh, J.Y.; Maeng, P.J.
    The NADP+-dependent glutamate dehydrogenase Gdh1 is subjected to glucose starvation-induced reversible aggregation that affects stress resistance in yeast (2019), J. Microbiol., 57, 884-892 .
    View publication on PubMed
Search for more literature for 1.4.1.4

Cloned(Commentary)

Cloned (Comment) Organism
GDH1, cloning and expression of wild-type and mutant enzymes in Escherichia coli, recombinant expression of GFP-tagged Gdh1 in Saccharomyces cerevisiae Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP1 is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Saccharomyces cerevisiae 5739
-
additional information altered localization to the mitochondria or peroxisomes prevents Gdh1, which was originally localized in the cytoplasm, from stationary phase-specific aggregation, suggesting that some cytosolic factors are involved in the process of Gdh1 aggregation Saccharomyces cerevisiae
-
-
peroxisome
-
 Saccharomyces cerevisiae 5777
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate + H2O + NADP+ Saccharomyces cerevisiae
-
 2-oxoglutarate + NH3 + NADPH + H+
-
 r
L-glutamate + H2O + NADP+ Saccharomyces cerevisiae ATCC 204508
-
 2-oxoglutarate + NH3 + NADPH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P07262
-
-
Saccharomyces cerevisiae ATCC 204508 P07262
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + H2O + NADP+
-
 Saccharomyces cerevisiae 2-oxoglutarate + NH3 + NADPH + H+
-
 r
L-glutamate + H2O + NADP+
-
 Saccharomyces cerevisiae ATCC 204508 2-oxoglutarate + NH3 + NADPH + H+
-
 r

Synonyms

Synonyms Comment Organism
GDH1
-
 Saccharomyces cerevisiae
NADP+-dependent glutamate dehydrogenase
-
 Saccharomyces cerevisiae
NADP-dependent glutamate dehydrogenase 1
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NADP+ beta-NADP+ Saccharomyces cerevisiae
NADPH beta-NADPH Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution altered localization to the mitochondria or peroxisomes prevents Gdh1, which was originally localized in the cytoplasm, from stationary phase-specific aggregation, suggesting that some cytosolic factors are involved in the process of Gdh1 aggregation Saccharomyces cerevisiae
malfunction mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3 Saccharomyces cerevisiae
malfunction mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP1 is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3 Saccharomyces cerevisiae
additional information glucose starvation triggers the transition of the soluble form of Gdh1 into the insoluble aggregate form, which can be redissolved by replenishing glucose, without any requirement for protein synthesis Saccharomyces cerevisiae
physiological function NADP-GDH isozyme Gdh3, but not Gdh1, mainly contributes to the oxidative stress resistance of stationary-phase cells. The insignificance of Gdh1 to stress resistance possibly results from conditional and reversible aggregation of Gdh1 into punctuate foci initiated in parallel with postdiauxic growth Saccharomyces cerevisiae