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3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
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-
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
additional information
?
-
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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-
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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-
-
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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-
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r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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additional information
?
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enzymatic activity strictly depends on residue Cys149. Catalytic Cys149 is the only solvent-exposed cysteine of the protein and its thiol is relatively acidic, pKa =5.7
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?
additional information
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enzymatic activity strictly depends on residue Cys149. Catalytic Cys149 is the only solvent-exposed cysteine of the protein and its thiol is relatively acidic, pKa =5.7
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nitric oxide
isoform GAPC1 is irreversibly inhibited in a time- and concentration-dependent manner
oxidized glutathione
inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found glutathionylated; inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found glutathionylated
S-nitrosoglutathione
inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found nitrosylated; inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found nitrosylated; inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol
Tyr-Asp
a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions; a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions
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glutathione
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5 mM oxidized glutathione, GSSG, formation of mixed disulfide between glutathione and A4-GAPDH results in the inhibition of enzyme activity
glutathione
inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol
H2O2
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H2O2
inhibits enzyme activity by converting the thiolate of Cys149 into irreversibly oxidized forms, -SO2- and SO3- via a labile sulfenate intermediate SO?. Reduced glutathione prevents this irreversible process by reacting with Cys149 sulfenates to give rise to a mixed disulfide. Glutathionylated enzyme can be fully reactivated either by cytosolic glutaredoxin, via a glutathione-dependent monothiol mechanism, or, less efficiently, by cytosolic thioredoxins physiologically reduced by NADPH:thioredoxin reductase
H2O2
isoform GAPC1 is irreversibly inhibited in a time- and concentration-dependent manner
additional information
no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu); no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu)
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additional information
no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu); no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu)
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malfunction
knockout or overexpression of GAPC isozymes causes significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Two double knockout seeds show over 3% of dry weight decrease in oil content compared with that of the wild-type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild-type and the fatty acid composition is altered. The transgenic lines exhibit decreased fertility. Seed-specific overexpression lines show over 3% increase in seed oil without compromised seed yield or fecundity, phenotypes, overview
malfunction
transcriptomic and metabolomic analyses indicate that the lack of GAPCp activity affects nitrogen and carbon metabolism as well as mineral nutrition and that glycerate and glutamine are the main metabolites responding to GAPCp activity, phenotypic analysis, detailed overview. Mutants gapcp1gapcp2 display a drastic reduction not only of root growth but also of the aerial part (AP) when grown both on plates and in greenhouse conditions. This phenotype is observed in double homozygous mutants only. Single mutants (gapcp1 or gapcp2) or mutant plants homozygous for one of the genes and heterozygous for the other are phenotypically indistinguishable from the wild-type plants. At the adult stage, GAPCp1 expression in the AP is able to complement the sterile phenotype of gapcp1gapcp2, resulting in plants with siliques and fertile seeds. The developmental pattern of gapcp1gapcp2 RBCS:GAPCp1 is also altered as compared with gapcp1gapcp2, probably as a consequence of the fertile phenotype, displaying shorter shoots than gapcp1gapcp2. A similar developmental pattern alteration is observed in the sterile gapcp1gapcp2 35S:GAPCp1 lines
malfunction
transcriptomic and metabolomic analyses indicate that the lack of GAPCp activity affects nitrogen and carbon metabolism as well as mineral nutrition and that glycerate and glutamine are the main metabolites responding to GAPCp activity, phenotypic analysis, detailed overview. Mutants gapcp1gapcp2 display a drastic reduction not only of root growth but also of the aerial part when grown both on plates and in greenhouse conditions. This phenotype is observed in double homozygous mutants only. Single mutants (gapcp1 or gapcp2) or mutant plants homozygous for one of the genes and heterozygous for the other are phenotypically indistinguishable from the wild-type plants
malfunction
Tyr-Asp inhibition of glyceraldehyde 3-phosphate dehydrogenase affects plant redox metabolism. Tyr-Asp inhibits the activity of a key glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPC), and redirects glucose toward pentose phosphate pathway (PPP) and NADPH production. Tyr-Asp supplementation improves the growth performance of both Arabidopsis and tobacco seedlings subjected to oxidative stress conditions. Neither the combination of Tyr and Asp nor the two other tested dipeptides, Ser-Leu and Gly-Pro, exhibit the bioactivity of Tyr-Asp. Tyr-Asp treatment, but neither the combination of amino acids nor the two other tested dipeptides improves plant performance under stress conditions. Tyr-Asp supplementation increases biomass of catechin-treated wild-type seedlings. The Tyr-Asp-associated stress tolerance is dependent on the inhibition of the GAPC1 and GAPC2 activities. Proteome characterization of the Tyr-Asp feeding experiment revealed changes in protein and redox metabolism consistent with the Tyr-Asp protein interactions beyond that with GAPC, Tyr-Asp affects redox and protein metabolism, phenotypes, overview
metabolism
GAPCp might be an important metabolic connector of glycolysis with other pathways, such as the phosphorylated pathway of serine biosynthesis, the ammonium assimilation pathway, or the metabolism of gamma-aminobutyrate, which in turn affect plant development
metabolism
plastidial isozyme GAPCp might be an important metabolic connector of glycolysis with other pathways, such as the phosphorylated pathway of serine biosynthesis, the ammonium assimilation pathway, or the metabolism of gamma-aminobutyrate, which in turn affect plant development
metabolism
the enzyme is involved in glycolysis catalyzing a key reaction
metabolism
in the cytosol, two different GAPDHs are involved in glycolysis, the phosphorylating NAD+-dependent GAPDH (GAPC1 and GAPC2; EC 1.2.1.12) and the non-phosphorylating, NADP+-dependent GAPDH (GAPN, EC 1.2.1.9). GAPN irreversibly oxidizes G3P to 3-phosphoglycerate (3PGA) and has no homology to GAPC. Besides their role in carbon assimilation and partitioning, phosphorylating GAPDHs (particularly, GAPC1 and GAPA1) have additional moonlighting functionalities
physiological function
double mutants lacking both plastidial isoforms gapcp1 and gapcp2 display a drastic phenotype of arrested root development, dwarfism, and sterility. In spite of their low gene expression level, GAPCp down-regulation leads to altered gene expression and to drastic changes in the sugar and amino acid balance of the plant. GAPCps are important for the synthesis of serine in roots. Serine supplementation to the growth medium rescues root developmental arrest and restores normal levels of carbohydrates and sugar biosynthetic activities in gapcp double mutants
physiological function
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gapc-1 null mutant line shows a delay in growth, morpholigical alterations in siliques, and low seed number. Embryo development is altered, showing abortions and empty embryonic sacs in basal and apical siliques, respectively. Mutant shows a decrease in ATP levels and reduced respiratory rate as well as a decrease in the expression and activity of aconitase and succinate dehydrogenase and reduced levels of pyruvate and several Krebs cycle intermediates, and increased reactive oxygen species levels
physiological function
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GAPDH controls generation of H2O2 by the proapoptotic family member Bax and heat shock, which in turn suppresses cell death in yeast and plant cells
physiological function
cadmium-induced stress in seedlings roots induces nitric oxide accumulation, cytosolic oxidation, activation of the GAPC1 promoter, GAPC1 protein accumulation in enzymatically inactive form, and strong relocalization of GAPC1 to the nucleus. All the effects are detected in the same zone of the root tip. In vitro, GAPC1 is inactivated by either nitric oxide donors or hydrogen peroxide, but no inhibition is directly provided by cadmium
physiological function
knockout or overexpression of isoforms GapC1 and GapC2 causes significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Double knockout seeds have about 3% of dry weight decrease in oil content compared with wild type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild type and the fatty acid composition is altered. These transgenic lines exhibit decreased fertility. Seed-specific overexpression lines have more than 3% increase in seed oil without compromised seed yield or fecundity
physiological function
plastidial isozymes GAPCps are critical for primary root growth and essential for microspore development. Plastidial isozyme GAPCp1 is not functionally important in photosynthetic cells but plays a fundamental role in roots and in heterotrophic cells of the aerial part. GAPCp1 expression in reproductive organs is necessary for Arabidopsis fertility. GAPCp activity may be required in root meristems and the root cap for normal primary root growth. GAPCp might be an important metabolic connector of glycolysis with other pathways, such as the phosphorylated pathway of serine biosynthesis, the ammonium assimilation pathway, or the metabolism of gamma-aminobutyrate, which in turn affect plant development. Isozymes GAPCp1 and GAPCp2 are redundant to one another
physiological function
the plastidial GAPCps are critical for primary root growth and essential for microspore development. Plastidial isozyme GAPCp might be an important metabolic connector of glycolysis with other pathways, such as the phosphorylated pathway of serine biosynthesis, the ammonium assimilation pathway, or the metabolism of gamma-aminobutyrate, which in turn affect plant development. Isozymes GAPCp1 and GAPCp2 are redundant to one another
physiological function
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plastidial glyceraldehyde-3-phosphate dehydrogenase GAPCp is not functionally significant in photosynthetic cells, but GAPCp activity expression in root tips is necessary for primary root growth, its expression in heterotrophic cells of aerial parts and roots is necessary for plant growth and development. GAPCp is an important metabolic connector of carbon and nitrogen metabolism through the phosphorylated pathway of serine biosynthesis, role of the pathway in the control of plant growth and development, overview. 3-Phospho-D-glyceroyl phosphate is converted into acetyl-coA in plastids, which is used for the biosynthesis of fatty acids
physiological function
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possible role of NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase in growth promotion of Arabidopsis seedlings by low levels of selenium. The pro-growth effect of selenium arises enhancing mitochondrial performance in a GSH-dependent manner, in which NAD-GAPDH may serve as a key regulator
physiological function
two cytosolic GAPC isozymes play important roles in cellular metabolism and seed oil accumulation. GAPC levels play important roles in the overall cellular production of reductants, energy, and carbohydrate metabolites, and GAPC levels are directly correlated with seed oil accumulation
additional information
proteogenic dipeptides act as evolutionarily conserved small-molecule regulators at the nexus of stress, protein degradation, and metabolism
additional information
proteogenic dipeptides act as evolutionarily conserved small-molecule regulators at the nexus of stress, protein degradation, and metabolism
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C155S
nuclear relocalization of GAPC1 under cadmium-induced oxidative stress is stimulated, rather than inhibited, by mutation of the catalytic cysteine C155
C159S
the mutant C159S of the isozyme GapC2 shows decreased specific activity
C149S
the mutant shows 92% activity compared to the wild type enzyme
C149S
about 1% of wild-type activity, residue Cys149 is both essential for catalysis and the only accessible cysteine
C153S
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mutant, having only one cysteine in the catalytic site, is oxidized and glutathionylated similarly to the wild-type enzyme
C153S
the mutant shows 0.7% activity compared to the wild type enzyme
C153S
residue Cys153 has apparently no role in catalysis, in spite of the proximity in space with catalytic Cys149
additional information
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GAPC-1 antisense line shows a delay in growth, morpholigical alterations in siliques, and low seed number. Embryo development is altered, showing abortions and empty embryonic sacs in basal and apical siliques, respectively. Mutant shows a decrease in the expression and activity of aconitase and succinate dehydrogenase and reduced levels of pyruvate and several Krebs cycle intermediates, and increased reactive oxygen species levels
additional information
construction of enzyme gapcp double mutants, gapcp1gapcp2, under the control of photosynthetic (Rubisco small subunit RBCS2B [RBCS]) or heterotrophic (phosphate transporter PHT1.2 [PHT]) cell-specific promoters
additional information
construction of enzyme gapcp double mutants, gapcp1gapcp2, under the control of photosynthetic (Rubisco small subunit RBCS2B [RBCS]) or heterotrophic (phosphate transporter PHT1.2 [PHT]) cell-specific promoters
additional information
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construction of glyceraldehyde-3-phosphate dehydrogenase double mutant gapcp1gapcp2. GAPCp expression in photosynthetic cells of gapcp1-gapcp2 does not complement the growth arrest of the aerial parts of the mutant plants, the lack of GAPCp activity in epidermal cells restricts leaf growth
additional information
knockout or overexpression of GAPC isozymes in Arabidopsis thaliana causing significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Construction of two double knockout seeds by T-DNA insertion showing over 3% of dry weight decrease in oil content compared with that of the wild-type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild-type and the fatty acid composition is altered. The transgenic lines exhibit decreased fertility. Seed-specific overexpression lines show over 3% increase in seed oil without compromised seed yield or fecundity, phenotypes, overview
additional information
knockout or overexpression of GAPC isozymes in Arabidopsis thaliana causing significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Construction of two double knockout seeds by T-DNA insertion showing over 3% of dry weight decrease in oil content compared with that of the wild-type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild-type and the fatty acid composition is altered. The transgenic lines exhibit decreased fertility. Seed-specific overexpression lines show over 3% increase in seed oil without compromised seed yield or fecundity, phenotypes, overview
additional information
-
knockout or overexpression of GAPC isozymes in Arabidopsis thaliana causing significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Construction of two double knockout seeds by T-DNA insertion showing over 3% of dry weight decrease in oil content compared with that of the wild-type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild-type and the fatty acid composition is altered. The transgenic lines exhibit decreased fertility. Seed-specific overexpression lines show over 3% increase in seed oil without compromised seed yield or fecundity, phenotypes, overview
additional information
generation of a gapc1/gapc2 double mutant that is entirely devoid of the cytosolic GAPC activity and insensitive to Tyr-Asp inhibition of GAPC activity
additional information
generation of a gapc1/gapc2 double mutant that is entirely devoid of the cytosolic GAPC activity and insensitive to Tyr-Asp inhibition of GAPC activity
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Marri, L.; Sparla, F.; Pupillo, P.; Trost, P.
Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana
J. Exp. Bot.
56
73-80
2005
Arabidopsis thaliana
brenda
Marri, L.; Trost, P.; Pupillo, P.; Sparla, F.
Reconstitution and properties of the recombinant glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase supramolecular complex of Arabidopsis
Plant Physiol.
139
1433-1443
2005
Arabidopsis thaliana
brenda
Zaffagnini, M.; Michelet, L.; Marchand, C.; Sparla, F.; Decottignies, P.; Le Marechal, P.; Miginiac-Maslow, M.; Noctor, G.; Trost, P.; Lemaire, S.D.
The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3-phosphate dehydrogenase is selectively regulated by glutathionylation
FEBS J.
274
212-226
2007
Arabidopsis thaliana, Spinacia oleracea
brenda
Trost, P.; Fermani, S.; Marri, L.; Zaffagnini, M.; Falini, G.; Scagliarini, S.; Pupillo, P.; Sparla, F.
Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3-phosphate dehydrogenase: autonomous vs. CP12-dependent mechanisms
Photosynth. Res.
89
263-275
2006
Arabidopsis thaliana, Spinacia oleracea
brenda
Holtgrefe, S.; Gohlke, J.; Starmann, J.; Druce, S.; Klocke, S.; Altmann, B.; Wojtera, J.; Lindermayr, C.; Scheibe, R.
Regulation of plant cytosolic glyceraldehyde 3-phosphate dehydrogenase isoforms by thiol modifications
Physiol. Plant.
133
211-228
2008
Arabidopsis thaliana (P25858), Arabidopsis thaliana (Q56WJ4), Arabidopsis thaliana, Oryctolagus cuniculus, Saccharomyces cerevisiae, Spinacia oleracea
brenda
Baek, D.; Jin, Y.; Jeong, J.; Lee, H.; Moon, H.; Lee, J.; Shin, D.; Kang, C.; Kim, D.; Nam, J.; Lee, S.; Yun, D.
Suppression of reactive oxygen species by glyceraldehyde-3-phosphate dehydrogenase
Phytochemistry
69
333-338
2008
Arabidopsis thaliana
brenda
Rius, S.P.; Casati, P.; Iglesias, A.A.; Gomez-Casati, D.F.
Characterization of Arabidopsis lines deficient in GAPC-1, a cytosolic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
Plant Physiol.
148
1655-1667
2008
Arabidopsis thaliana
brenda
Munoz-Bertomeu, J.; Cascales-Minana, B.; Mulet, J.M.; Baroja-Fernandez, E.; Pozueta-Romero, J.; Kuhn, J.M.; Segura, J.; Ros, R.
Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to altered root development and affects the sugar and amino acid balance in Arabidopsis
Plant Physiol.
151
541-558
2009
Arabidopsis thaliana (Q5E924), Arabidopsis thaliana (Q9SAJ6)
brenda
Bedhomme, M.; Adamo, M.; Marchand, C.H.; Couturier, J.; Rouhier, N.; Lemaire, S.D.; Zaffagnini, M.; Trost, P.
Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro
Biochem. J.
445
337-347
2012
Arabidopsis thaliana, Arabidopsis thaliana (P25858)
brenda
Vescovi, M.; Zaffagnini, M.; Festa, M.; Trost, P.; Lo Schiavo, F.; Costa, A.
Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots
Plant Physiol.
162
333-346
2013
Arabidopsis thaliana, Arabidopsis thaliana (P25858)
brenda
Guo, L.; Ma, F.; Wei, F.; Fanella, B.; Allen, D.; Wang, X.
Cytosolic phosphorylating glyceraldehyde-3-phosphate dehydrogenases affect Arabidopsis cellular metabolism and promote seed oil accumulation
Plant Cell
26
3023-3035
2014
Arabidopsis thaliana (P25858), Arabidopsis thaliana (Q9FX54), Arabidopsis thaliana
brenda
Takeda, T.; Fukui, Y.
Possible role of NAD-dependent glyceraldehyde-3-phosphate dehydrogenase in growth promotion of Arabidopsis seedlings by low levels of selenium
Biosci. Biotechnol. Biochem.
79
1579-1586
2015
Arabidopsis thaliana
brenda
Guo, L.; Ma, F.; Wei, F.; Fanella, B.; Allen, D.K.; Wang, X.
Cytosolic phosphorylating glyceraldehyde-3-phosphate dehydrogenases affect Arabidopsis cellular metabolism and promote seed oil accumulation
Plant Cell
26
3023-3035
2014
Arabidopsis thaliana (P25858), Arabidopsis thaliana (Q9FX54), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (P25858), Arabidopsis thaliana Col-0 (Q9FX54)
brenda
Anoman, A.D.; Munoz-Bertomeu, J.; Rosa-Tellez, S.; Flores-Tornero, M.; Serrano, R.; Bueso, E.; Fernie, A.R.; Segura, J.; Ros, R.
Plastidial glycolytic glyceraldehyde-3-phosphate dehydrogenase is an important determinant in the carbon and nitrogen metabolism of heterotrophic cells in Arabidopsis
Plant Physiol.
169
1619-1637
2015
Arabidopsis thaliana (Q5E924), Arabidopsis thaliana (Q9SAJ6)
brenda
Anoman, A.D.; Flores-Tornero, M.; Rosa-Tellez, S.; Munoz-Bertomeu, J.; Segura, J.; Ros, R.
The specific role of plastidial glycolysis in photosynthetic and heterotrophic cells under scrutiny through the study of glyceraldehyde-3-phosphate dehydrogenase
Plant Signal. Behav.
11
e1128614
2016
Arabidopsis thaliana
brenda
Moreno, J.C.; Rojas, B.E.; Vicente, R.; Gorka, M.; Matz, T.; Chodasiewicz, M.; Peralta-Ariza, J.S.; Zhang, Y.; Alseekh, S.; Childs, D.; Luzarowski, M.; Nikoloski, Z.; Zarivach, R.; Walther, D.; Hartman, M.D.; Figueroa, C.M.; Iglesias, A.A.; Fernie, A.R.; Skirycz, A.
Tyr-Asp inhibition of glyceraldehyde 3-phosphate dehydrogenase affects plant redox metabolism
EMBO J.
40
e106800
2021
Nicotiana tabacum (A0A0K2GN10), Nicotiana tabacum (A0A0K2GP10), Arabidopsis thaliana (P25858), Arabidopsis thaliana (Q9FX54)
brenda