EC Number   |
General Information |
Reference |
|---|
    1.4.1.4 | 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 |
-, 763355 |
| 1.4.1.4 | evolution |
the BpNADPGDH I and II sequences from Benjaminiella poitrasii include the three typical motifs of the family I hexameric GDHs: 84 PSVNL88, 92KFLGFEQ98 and 184RPEATGY/F 190. One of the conserved regions in the sequences includes the putative NADP-binding motif GSGNVAQYAALKVIELG, located between the residues 219 and 235. BpNADPGDH I and BpNADPGDH II share 70% homology with each other, and BpNADPGDH I and BpNADPGDH II give over 70% identity scores with fungal NADP-dependent GDHs |
763046 |
| 1.4.1.4 | malfunction |
contradictory roles of GDH1 and GDH2 (EC 1.4.1.2) in cold-growth defects in yeast strains. Concurrent ectopic overexpression of GDH1 and GDH2 compensate the observed accumulation of ROS. Specifically, glutamate can prevent cold-induced ROS accumulation through the synthesis of glutathione that requires glutamate as a precursor molecule and serves in ROS removal. The role of Gdh1p in transcriptional silencing is crucial through the proteolysis of H3 histone in yeast (H3-clipping in the N-tail). GDH1 deletion leads to decreased binding of Sir2 protein on the telomeres, causing elevated transcript levels of genes affected by the loss of the SIR complex. Upon GDH1 deletion, the elevated levels of 2-oxoglutarate, and not those of NADH, result in the observed telomeric silencing defects. Upon GDH1 deletion, a highly derepressed expression of DAL5, a NCR-sensitive gene that requires both Gat1 and Gln3 for its expression, is observed. GDH1 deletion causes ammonium accumulation, but surprisingly does not affect the subcellular distribution and the concentrations of glutamine as well as glutamate |
-, 763438 |
| 1.4.1.4 | malfunction |
Gdh3-null cells show accelerated chronological aging and hypersusceptibility to thermal and oxidative stress during stationary phase. Upon exposure to oxidative stress, Gdh3-null strains display a rapid loss in viability associated with typical apoptotic hallmarks, i.e. reactive oxygen species accumulation, nuclear fragmentation, DNA breakage, and phosphatidylserine translocation. In addition, Gdh3-null cells, but not Gdh1-null cells, have a higher tendency toward GSH depletion and subsequent reactive oxygen species accumulation than did wild-type cells. GSH depletion is rescued by exogenous GSH or glutamate. The hypersusceptibility of stationary phase Gdh3-null cells to stress-induced apoptosis is suppressed by deletion of GDH2. Gdh1, but not Gdh3, is subjected to stationary phase-specific degradation in which the Lys-426 residue in the Box420Gdh1 region plays an essential role |
-, 725506 |
| 1.4.1.4 | 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 |
-, 763355 |
| 1.4.1.4 | 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 |
-, 763355 |
| 1.4.1.4 | malfunction |
propylselen inhibits cancer cell growth by targeting glutamate dehydrogenase at the NADP+ binding site |
762699 |
| 1.4.1.4 | malfunction |
two industrial strains of Penicillium chrysogenum a penicillin (PC-pen)- and a cephalosporin producing (PC-ceph) are used in which the NADPH-dependent GDH is deleted by replacing 0.8 kb of the C-terminus of the gdhA gene with the hygromyin B resistance marker, resulting in PC-pen-DELTAgdhA and PC-ceph-DELTAgdhA. The two strains are isogenic except for the insertion of the Streptomyces clavuligerus expandase gene into the genome of PC-ceph. It is shown that this genetic modification results in a radical change in morphology |
699077 |
| 1.4.1.4 | metabolism |
both NADP(H)-GDH (gdhA) and glutamine synthetase play important roles in ammonium assimilation |
726247 |
| 1.4.1.4 | metabolism |
in Saccharomyces cerevisiae glutamate can be synthesized from 2-oxoglutarate and ammonium through the action of NADP-dependent glutamate dehydrogenase isozymes Gdh1 and Gdh3. Gdh1 and Gdh3 are evolutionarily adapted isoforms and cover the anabolic role of the GDH-pathway, role and function of the GDH pathway in glutamate metabolism, overview. The pleiotropic effects of GDH pathway in yeast biology highlight the importance of glutamate homeostasis in vital cellular processes. Isozyme Gdh1 is the primary (hyperbolic) NADP-GDH enzyme and isozyme Gdh3 the cooperative NADP-GDH enzyme in the GDH pathway of Saccharomyces cerevisiae. The constant expression of GDH1 implies that its transcription proceeds normally during the different growth phases including the diauxic shift, when yeast cells reprogram their metabolism to enter the respiration phase. But during the post-diauxic shift, the Gdh1p/Gdh3p ratio decreases and most of the NADP-GDH activity is attributed to Gdh3p. The decrease of the NADP-GDH activity in ethanol growing cells was initially referred to be controlled through post-translational modifications that can modulate the proportion of Gdh1p versus Gdh3p monomers that constitute the NADP-GDH pool. Synthesis of glutamate occurs through the action of NADP-GDH (encoded by GDH1 and GDH3 genes). NAD-GDH activity (encoded by GDH2, EC 1.4.1.2) is responsible for glutamate degradation and release of ammonium and 2-oxoglutarate |
-, 763438 |
