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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
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
evolution
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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
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malfunction
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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
malfunction
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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
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
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
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
malfunction
propylselen inhibits cancer cell growth by targeting glutamate dehydrogenase at the NADP+ binding site
malfunction
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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
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malfunction
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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
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malfunction
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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
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malfunction
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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
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metabolism
NADP+-GDH is involved in nitrogen assimilation due to a constitutive aminating activity, specific activity of the aminating NADP+-GDH reaction is independent of nitrogen availability, it does not change significantly in response to prolonged exposure to nitrogen limitation, in contrast to the deaminating activity, which is 2fold increased exposed to ammonium starvation conditions. The deaminating reaction changes in response to varying ammonium concentrations and is regulated in response to nitrogen availability. NADP+-GDH is not regulated on the transcriptional level. The enzyme is invovled in the additional nitrogen assimilatory pathway via glutamate dehydrogenase, GDH, regulation of NADP+-GDH specific activity, overview
metabolism
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both NADP(H)-GDH (gdhA) and glutamine synthetase play important roles in ammonium assimilation
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
metabolism
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the enzyme is involved in the ammonium assimilation mechanism in submerged macrophytes, ammonium detoxification mechanism in ammonium-tolerant species, overview
metabolism
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the enzyme is involved in the ammonium assimilation mechanism in submerged macrophytes, ammonium detoxification mechanism in ammonium-tolerant species, overview
metabolism
YALI0F17820g (ylGDH, EC 1.4.1.4) encodes a NADP-dependent GDH whereas YALI0E09603g (ylGDH2, EC 1.4.1.2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. Levels of the two enzyme activities are comparable during logarithmic growth on rich medium, but the NADP-ylGDH1p enzyme activity is most highly expressed in stationary and nitrogen starved cells by 3fold to 12fold compared to NAD-ylGDH2p. Replacement of ammonia with glutamate causes a decrease in NADP-ylGdh1p activity, whereas NAD-ylGdh2p activity is increased. When glutamate is both carbon and nitrogen sources, the activity of NAD-ylGDH2p becomes dominant up to 18fold compared with that of NADP-ylGDH1p. ylGDH1 and ylGDH2 are functionally not interchangeable
metabolism
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YALI0F17820g (ylGDH, EC 1.4.1.4) encodes a NADP-dependent GDH whereas YALI0E09603g (ylGDH2, EC 1.4.1.2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. Levels of the two enzyme activities are comparable during logarithmic growth on rich medium, but the NADP-ylGDH1p enzyme activity is most highly expressed in stationary and nitrogen starved cells by 3fold to 12fold compared to NAD-ylGDH2p. Replacement of ammonia with glutamate causes a decrease in NADP-ylGdh1p activity, whereas NAD-ylGdh2p activity is increased. When glutamate is both carbon and nitrogen sources, the activity of NAD-ylGDH2p becomes dominant up to 18fold compared with that of NADP-ylGDH1p. ylGDH1 and ylGDH2 are functionally not interchangeable
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metabolism
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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
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metabolism
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YALI0F17820g (ylGDH, EC 1.4.1.4) encodes a NADP-dependent GDH whereas YALI0E09603g (ylGDH2, EC 1.4.1.2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. Levels of the two enzyme activities are comparable during logarithmic growth on rich medium, but the NADP-ylGDH1p enzyme activity is most highly expressed in stationary and nitrogen starved cells by 3fold to 12fold compared to NAD-ylGDH2p. Replacement of ammonia with glutamate causes a decrease in NADP-ylGdh1p activity, whereas NAD-ylGdh2p activity is increased. When glutamate is both carbon and nitrogen sources, the activity of NAD-ylGDH2p becomes dominant up to 18fold compared with that of NADP-ylGDH1p. ylGDH1 and ylGDH2 are functionally not interchangeable
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physiological function
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carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD
physiological function
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carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60°C are analysed: GDHI from isophthalate- and mHB-grown cells retain 70% and 90% of its activity, respectively
physiological function
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carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60°C are analysed: In Pseudomonas aeruginosa strain PPD, isophthalate-, glucose-, 2YT- or mHB-grown cells retain 100% of the activity of NADP-GDH, while PPD cells grown on pHB and benzoate show 25% and 40% loss of activity
physiological function
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carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60°C are analysed: isophthalate-, glucose-, 2YT- or mHB-grown cells retain 100% of the activity of NADP-GDH
physiological function
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to test the effect of decreased hGDH expression, small interfering hGDH RNAs are expressed intracellularly in BE(2)C human neuroblastoma cells. hGDH mRNA knockdown is confirmed by immunoblotting and RT-PCR. TUNEL and DNA fragmentation assays 48 h after transfection reveal that inhibition of hGDH expression induces cellular apoptosis and activates phospho-ERK1/2 (phospho-extracellular-signal-regulated kinase 1/2)
physiological function
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Gdh1p is the primary GDH enzyme and Gdh3p plays an evident role during aerobic glutamate metabolism
physiological function
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involvement of GDH3-encoded NADP+-dependent glutamate dehydrogenase in yeast cell resistance to stress-induced apoptosis in stationary phase cells, overview. GDH1, but not GDH3, is responsible for the resistance against stress-induced apoptosis in logarithmic phase cells, Necessity of GDH3 for the resistance to stress-induced apoptosis and chronological aging is due to the stationary phase-specific expression of GDH3 and concurrent degradation of Gdh1 in which the Lys-426 residue plays an essential role
physiological function
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. Cells overexpressing GDH1 still display a cold-sensitive phenotype in presence of tryptophan or nictotinic acid in the medium. Total cellular NAD levels are a limiting factor for growth at low temperature in Saccharomyces cerevisiae
physiological function
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expression in Oryza sativa. At the seedling stage, the leaf area and shoot and root dry weights of the high gdhA-expressors are higher than those of control plants under both high (high N) and low nitrogen (low N) conditions. The net photosynthesis rate at the heading stage is higher in transgenic than in control leaves. Under both high and low N conditions, the nitrogen contents in the shoots and roots, at seedling and grain-harvest stages, are significantly higher in high gdhA-expressors than in control plants. At the harvest stage, the high gdhA-expressors exhibit greater panicle and spikelet numbers per plant compared with control plants, resulting in higher grain weight. In addition, gdhA expression in forage rice significantly enhances their tolerance to salt stress compared to control plants
physiological function
AKQ74236
the rocG gene deletion mutant produces intracellular glutamic acid with a concentration of 90 ng/log (CFU), which is only 23.7% that of the wild-type. The poly-gamma.glutamic acid yield of the mutant is 5.37 g/l, a decrease of 45.3% compared to the wild type
physiological function
besides the distinct kinetic properties, the two isozymes in Benjaminiella poitrasii, BpNADPGDH I and BpNADPGDH II, are regulated by cAMP-dependent- and calmodulin (CaM) dependent protein kinases, respectively
physiological function
besides the distinct kinetic properties, the two isozymes in Benjaminiella poitrasii, BpNADPGDH I and BpNADPGDH II, are regulated by cAMP-dependent- and calmodulin (CaM)-dependent protein kinases, respectively
physiological function
gene YALI0F17820g (GDH1) encodes a NADP?dependent GDH whereas YALI0E09603g (GDH2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. NADP-GDH1 enzyme activity is most highly expressed in stationary and nitrogen starved cells. NADP-Gdh1 is required for efficient nitrogen assimilation. GDH1 and GDH2 are not interchangeable
physiological function
glutamate dehydrogenases (GDHs) are fundamental to cellular nitrogen and energy balance. NADP-ylGdh1p is required for efficient nitrogen assimilation. Glutamate dehydrogenase (GDH) activity in gdh-null Saccharomyces cerevisiae mutant cells is restored by introduction of YALI0F17820g (ylGDH1) or YALI0E09603g (ylGDH2, EC 1.4.1.2) from Yarrowia lipolytica
physiological function
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in practical water restoration by aquatic plants, the alternative pathway of GDH is more important than the pathway catalyzed by GS in determining the tolerance of submerged macrophytes to high ammonium concentration. Both NADH-dependent (EC 1.4.1.2) and NADPH-dependent GDH show species-dependent variation, in the ammonium-tolerant species, Myriophyllum spicatum, there is a dose-response curve (from 49.46 to 132.99 nmol/min/mg protein for NADH-dependent GDH and 28.98 to 58.67 nmol/min/mg protein for NADPH-GDH), but in the ammonium-sensitive species, Potamogeton lucens, there is little change in activity
physiological function
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in practical water restoration by aquatic plants, the alternative pathway of GDH is more important than the pathway catalyzed by GS in determining the tolerance of submerged macrophytes to high ammonium concentration. Both NADH-dependent (EC 1.4.1.2) and NADPH-dependent GDH show species-dependent variation, in the ammonium-tolerant species, Myriophyllum spicatum, there is a dose-response curve (from 49.46 to 132.99 nmol/min/mg protein for NADH-dependent GDH and 28.98 to 58.67 nmol/min/mg protein for NADPH-GDH), but in the ammonium-sensitive species, Potamogeton lucens, there is little change in activity
physiological function
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 allosteric regulation of NADP-GDH activity is influenced by 2-oxoglutarate and NADP, and not by small molecules (e.g. GTP, AMP) or amino acids. Role of the GDH path in ROS-mediated apoptosis. GDH2 (EC 1.4.1.2) genetically interacts with GDH3 and controls stress-induced apoptosis. The transcription of GDH3 occurs extensively during the stationary phase. The activity of Gdh3p presents a 20 to 140fold increment when cells are grown under aerobic conditions. Under these conditions the majority of the total NADP-GDH activity is attributed to Gdh3p monomers that can contribute up to 70% to the pool, especially when cells enter or remain in aerobic metabolism for several days. Under acetate/raffinose conditions with ammonia as the only nitrogen source, yeast cells lacking GDH3 gene has a significant impairment in glutamate synthesis. The increase of the NADP-dependent GDH activity observed in gdh1DELTA mutants is presumably due to Gdh3p that seems to play a prominent role in glutamate metabolism under aerobic conditions. Glutamate synthesis under aerobic conditions is insufficient and requires additionally the activity of Gdh1p. The expression of both GDH3 and GDH1 is required to achieve wild-type growth in respiration. The transcriptional regulation of GDH3 is controlled by carbon sources and not by nitrogen catabolite repression as in the case of GDH1. The glucose-repressed expression of GDH3 is attributed to the condensed chromatin organization of its promoter
physiological function
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 allosteric regulation of NADP-GDH activity is influenced by 2-oxoglutarate and NADP, and not by small molecules (e.g. GTP, AMP) or amino acids. Role of the GDH path in ROS-mediated apoptosis. Role of GDH1 and GDH2 (EC 1.4.1.2) in glutamate synthesis and its possible implication to oxidation stress defense through the glutathione system. GDH1 regulates chromatin through its catalytic activity. The expression of both GDH3 and GDH1 is required to achieve wild-type growth in respiration. The transcriptional regulation of GDH3 is controlled by carbon sources and not by nitrogen catabolite repression as in the case of GDH1. The regulation of GDH1 under glucose conditions is performed by nitrogen catabolite repressor (NCR)-sensitive activators, Leu3p and activators exclusive for respiratory growth such as the HAP complex that coordinates nuclear and mitochondrial gene expression. Under ethanol conditions, GDH1 derepression is mediated by the Gcn4 and Hap4 transcriptional activators and is amplified by Gln3
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
physiological function
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the activity of glutamate dehydrogenase in the ammonium-tolerant species Myriophyllum spicatum leaves increases 169% for NADH-dependent GDH and 103% for NADPH-dependent GDH with the [NH4+-N] increasing from 0 to 100 mg/l, performing a dose-response curve while glutamine synthetase activity slightly changes
physiological function
the gdh3/gdh3 mutant is able to grow on either arginine or proline as a sole carbon and nitrogen source, but the strain is locked in the yeast morphology in proline-containing medium. In proline medium, the gdh3/gdh3 mutant strain fails to form filaments, whilst the wild-type develops hyphae. Different concentrations of ATP, NAD+, NADH, NAPD+, NADPH, as well as 62 other metabolites, and 19 isotopically labelled are found metabolites between the mutant and the wild-type strains
physiological function
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involvement of GDH3-encoded NADP+-dependent glutamate dehydrogenase in yeast cell resistance to stress-induced apoptosis in stationary phase cells, overview. GDH1, but not GDH3, is responsible for the resistance against stress-induced apoptosis in logarithmic phase cells, Necessity of GDH3 for the resistance to stress-induced apoptosis and chronological aging is due to the stationary phase-specific expression of GDH3 and concurrent degradation of Gdh1 in which the Lys-426 residue plays an essential role
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physiological function
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besides the distinct kinetic properties, the two isozymes in Benjaminiella poitrasii, BpNADPGDH I and BpNADPGDH II, are regulated by cAMP-dependent- and calmodulin (CaM)-dependent protein kinases, respectively
-
physiological function
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besides the distinct kinetic properties, the two isozymes in Benjaminiella poitrasii, BpNADPGDH I and BpNADPGDH II, are regulated by cAMP-dependent- and calmodulin (CaM) dependent protein kinases, respectively
-
physiological function
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the rocG gene deletion mutant produces intracellular glutamic acid with a concentration of 90 ng/log (CFU), which is only 23.7% that of the wild-type. The poly-gamma.glutamic acid yield of the mutant is 5.37 g/l, a decrease of 45.3% compared to the wild type
-
physiological function
-
gene YALI0F17820g (GDH1) encodes a NADP?dependent GDH whereas YALI0E09603g (GDH2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. NADP-GDH1 enzyme activity is most highly expressed in stationary and nitrogen starved cells. NADP-Gdh1 is required for efficient nitrogen assimilation. GDH1 and GDH2 are not interchangeable
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physiological function
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glutamate dehydrogenases (GDHs) are fundamental to cellular nitrogen and energy balance. NADP-ylGdh1p is required for efficient nitrogen assimilation. Glutamate dehydrogenase (GDH) activity in gdh-null Saccharomyces cerevisiae mutant cells is restored by introduction of YALI0F17820g (ylGDH1) or YALI0E09603g (ylGDH2, EC 1.4.1.2) from Yarrowia lipolytica
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physiological function
-
the gdh3/gdh3 mutant is able to grow on either arginine or proline as a sole carbon and nitrogen source, but the strain is locked in the yeast morphology in proline-containing medium. In proline medium, the gdh3/gdh3 mutant strain fails to form filaments, whilst the wild-type develops hyphae. Different concentrations of ATP, NAD+, NADH, NAPD+, NADPH, as well as 62 other metabolites, and 19 isotopically labelled are found metabolites between the mutant and the wild-type strains
-
physiological function
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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
-
physiological function
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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 allosteric regulation of NADP-GDH activity is influenced by 2-oxoglutarate and NADP, and not by small molecules (e.g. GTP, AMP) or amino acids. Role of the GDH path in ROS-mediated apoptosis. Role of GDH1 and GDH2 (EC 1.4.1.2) in glutamate synthesis and its possible implication to oxidation stress defense through the glutathione system. GDH1 regulates chromatin through its catalytic activity. The expression of both GDH3 and GDH1 is required to achieve wild-type growth in respiration. The transcriptional regulation of GDH3 is controlled by carbon sources and not by nitrogen catabolite repression as in the case of GDH1. The regulation of GDH1 under glucose conditions is performed by nitrogen catabolite repressor (NCR)-sensitive activators, Leu3p and activators exclusive for respiratory growth such as the HAP complex that coordinates nuclear and mitochondrial gene expression. Under ethanol conditions, GDH1 derepression is mediated by the Gcn4 and Hap4 transcriptional activators and is amplified by Gln3
-
physiological function
-
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 allosteric regulation of NADP-GDH activity is influenced by 2-oxoglutarate and NADP, and not by small molecules (e.g. GTP, AMP) or amino acids. Role of the GDH path in ROS-mediated apoptosis. GDH2 (EC 1.4.1.2) genetically interacts with GDH3 and controls stress-induced apoptosis. The transcription of GDH3 occurs extensively during the stationary phase. The activity of Gdh3p presents a 20 to 140fold increment when cells are grown under aerobic conditions. Under these conditions the majority of the total NADP-GDH activity is attributed to Gdh3p monomers that can contribute up to 70% to the pool, especially when cells enter or remain in aerobic metabolism for several days. Under acetate/raffinose conditions with ammonia as the only nitrogen source, yeast cells lacking GDH3 gene has a significant impairment in glutamate synthesis. The increase of the NADP-dependent GDH activity observed in gdh1DELTA mutants is presumably due to Gdh3p that seems to play a prominent role in glutamate metabolism under aerobic conditions. Glutamate synthesis under aerobic conditions is insufficient and requires additionally the activity of Gdh1p. The expression of both GDH3 and GDH1 is required to achieve wild-type growth in respiration. The transcriptional regulation of GDH3 is controlled by carbon sources and not by nitrogen catabolite repression as in the case of GDH1. The glucose-repressed expression of GDH3 is attributed to the condensed chromatin organization of its promoter
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physiological function
-
gene YALI0F17820g (GDH1) encodes a NADP?dependent GDH whereas YALI0E09603g (GDH2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. NADP-GDH1 enzyme activity is most highly expressed in stationary and nitrogen starved cells. NADP-Gdh1 is required for efficient nitrogen assimilation. GDH1 and GDH2 are not interchangeable
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physiological function
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glutamate dehydrogenases (GDHs) are fundamental to cellular nitrogen and energy balance. NADP-ylGdh1p is required for efficient nitrogen assimilation. Glutamate dehydrogenase (GDH) activity in gdh-null Saccharomyces cerevisiae mutant cells is restored by introduction of YALI0F17820g (ylGDH1) or YALI0E09603g (ylGDH2, EC 1.4.1.2) from Yarrowia lipolytica
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additional information
modelling of NADP+ in domain II reveals the potential contribution of positively charged residues from a neighbouring alpha-helical hairpin to phosphate recognition, sequence-structure relationship, overview. A single sequence accommodates both coenzymes in the dual-specificity GDHs of animals
additional information
the parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes
additional information
the parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes
additional information
the three-dimensional structure of hexameric PfGDH2 is solved to 3.1 A resolution, overview. The parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes
additional information
the three-dimensional structure of hexameric PfGDH2 is solved to 3.1 A resolution, overview. The parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes
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
additional information
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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
additional information
P320 and C321 are both important for NADP+ binding
additional information
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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
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