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evolution
both GAPDS and GAPD are homotetramers with the sequence identity of about 70%. They are encoded by different genes which have emerged after duplication of the original gene during the early evolution of chordates
evolution
both GAPDS and GAPD are homotetramers with the sequence identity of about 70%. They are encoded by different genes which have emerged after duplication of the original gene during the early evolution of chordates. The GAPDS gene is lost by most lineages, and specialized to a testis-specific protein in reptilians and mammals
evolution
cellular glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a phylogenetically conserved, ubiquitous enzyme
evolution
convergent evolution in GapA/B and GapC1, plastid GapC1 and GapA represent two independent cases of functional divergence and adaptations to the Calvin cycle entailing a shift in subcellular targeting and a shift in binding preference from NAD+ to NADPH. Comparisons between GapA sequences and cytosolic GAPDH and GapC1 and cytosolic GAPDH sequences (Gap2, GapA, GapB, or GapC1) to identify possible functionally divergent sites, homology modeling, phylogenetic tree, detailed overview
evolution
the sequence of the isozyme uracil-DNA glycosylase, UDG polypeptide (331 amino acids), differs from the sequence of classical GAPDH (335 amino acids) by the substitution of the residues 194-213 and the deletion of the residues 328-330. The amino acid sequence of the GAPDH isoform UDG because of its activity is hardly connected with alternative splicing of GAPDH pre-mRNA. The UDG region with the altered amino acids 194-213 is situated within the exon far from its boundaries. It appears to be a result of the single-nucleotide deletion in the GAPDH gene exon, causing the shift of the reading frame. Downstream to this region, there is theadditional deletion of 2 nucleotides in the UDG sequence, leading to restoration of the initial reading frame. The observed discrepancies in the sequences of these proteins are likely due to a sequencing error. Interestingly, the altered region belongs to the GAPDH glyceraldehyde-3-phosphate-binding site not participating in DNA binding
evolution
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molecular phylogenetic tree using sequences from 26 GAPDH proteins from 12 species of Aspergillus and 8 species of Trichoderma genus
evolution
molecular phylogenetic tree using sequences from 26 GAPDH proteins from 12 species of Aspergillus and 8 species of Trichoderma genus
evolution
sequence comparisons
evolution
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molecular phylogenetic tree using sequences from 26 GAPDH proteins from 12 species of Aspergillus and 8 species of Trichoderma genus
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evolution
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sequence comparisons
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evolution
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sequence comparisons
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evolution
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sequence comparisons
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evolution
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sequence comparisons
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malfunction
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FAO hepatoma cells with mutations of all 4 lysine residues (4K-R-GAPDH) in critical regions of enzyme GAPDH to mimic their unmodified state show reduced GAPDH glycolytic activity and glycolytic flux and increased gluconeogenic GAPDH activity and glucose production. Hepatic expression of mutant 4K-R-GAPDH in mice increases GAPDH gluconeogenic activity and the contribution of gluconeogenesis to endogenous glucose production in the unfed state. Consistent with the increased reliance on the energy-consuming gluconeogenic pathway, plasma free fatty acids and ketones are elevated inmice expressing 4K-RGAPDH, suggesting enhanced lipolysis and hepatic fatty acid oxidation. GAPDH acetylation is reduced in obese and type 2 diabetic db/db mice
malfunction
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GAPDH knockdown abolishes cADPR-induced Ca2+ release. GAPDH knockdown markedly inhibits NPE-cADPR- or PALcIDPRE-induced cytosolic Ca2+ increase in Jurkat cells, RyR3-expressing HEK-293 cells, or human coronary artery smooth muscle cells. Washing saponin-treated cells with PBS abolishes cADPR-induced colocalization of GAPDH with ryanodine receptors, RyRs
malfunction
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GAPDH-deficient cells are more sensitive to bleomycin or methyl methanesulfonate. In cells challenged with these genotoxic agents, GAPDH deficiency results in reduced cell viability and filamentous growth
malfunction
GAPDHS inhibitor effects on sperm motility and metabolism, overview
malfunction
GAPDHS inhibitor effects on sperm motility and metabolism, overview
malfunction
inhibition of GAPDH leads to substantially reduced energy generation
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
substitution of Phe34 with smaller side chain (e.g. Gly or Leu), or polar residue (e.g. Thr) abolishes the NAD+ binding affinity, or reduce the protein's catalytic efficiency
malfunction
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TDH3 deletion or overexpression does not affect overall cellular NAD+ levels, but affects nuclear NAD+ levels in yeast
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
knockdown of GAPDHS in uveal melanoma (UM) cell lines hinders glycolysis by decreasing glucose uptake, lactate production, ATP generation, cell growth and proliferation. Conversely, overexpression of GAPDHS promotes glycolysis, cell growth and proliferation. Transcription factor SOX10 knockdown reduces the activation of GAPDHS, leading to an attenuated malignant phenotype, and SOX10 overexpression promotes the activation of GAPDHS, leading to an enhanced malignant phenotype. Mechanistically, SOX10 exerts its function by binding to the promoter of GAPDHS to regulate its expression. Importantly, SOX10 abrogation suppresses in vivo tumor growth and proliferation
malfunction
RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. Genetic manipulation of gapdh1 and gapdh2 affects the biomass and total fatty acid of Mortierella alpina through an altered NADPH/NADP ratio
malfunction
RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. MA-RGAPDH2 is found to strengthen the metabolic flux of dihydroxyacetone phosphate to glycerol-3-phosphate. Genetic manipulation of gapdh1 and gapdh2 affects the biomass and total fatty acid of Mortierella alpina through an altered NADPH/NADP ratio
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
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
malfunction
when the cell is exposed to high levels of H2O2, GAPDH is irreversibly inhibited presumably by the formation of sulphenic acid in the active site cysteine, becoming a switch that balances the equilibrium between the glycolytic cycle and the pentose phosphate metabolic pathway and promoting the formation of NADPH to combat ROS-produced cell stress
malfunction
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RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. Genetic manipulation of gapdh1 and gapdh2 affects the biomass and total fatty acid of Mortierella alpina through an altered NADPH/NADP ratio
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malfunction
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RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. MA-RGAPDH2 is found to strengthen the metabolic flux of dihydroxyacetone phosphate to glycerol-3-phosphate. Genetic manipulation of gapdh1 and gapdh2 affects the biomass and total fatty acid of Mortierella alpina through an altered NADPH/NADP ratio
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malfunction
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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
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malfunction
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FAO hepatoma cells with mutations of all 4 lysine residues (4K-R-GAPDH) in critical regions of enzyme GAPDH to mimic their unmodified state show reduced GAPDH glycolytic activity and glycolytic flux and increased gluconeogenic GAPDH activity and glucose production. Hepatic expression of mutant 4K-R-GAPDH in mice increases GAPDH gluconeogenic activity and the contribution of gluconeogenesis to endogenous glucose production in the unfed state. Consistent with the increased reliance on the energy-consuming gluconeogenic pathway, plasma free fatty acids and ketones are elevated inmice expressing 4K-RGAPDH, suggesting enhanced lipolysis and hepatic fatty acid oxidation. GAPDH acetylation is reduced in obese and type 2 diabetic db/db mice
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malfunction
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TDH3 deletion or overexpression does not affect overall cellular NAD+ levels, but affects nuclear NAD+ levels in yeast
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metabolism
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GAPDH is not involved in the control of the glycolytic flux. A strain overproducing GAPDH shows a high NADH-to-NAD+ ratio, but no significant differences in growth rate when grown on glucose or lactose
metabolism
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replacement of Escherichia coli GapA glyceraldehyde 3-phosphate dehydrogenase by Clostridium acetobutylicum GapC glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.9 results in significant reduction of flux through the pentose phosphate pathway. Recombinant strains display increased NADPH availability, and consistently higher productivity than parent strains
metabolism
the enzyme is involved in glycolysis
metabolism
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a key enzyme of glycolysis, catalyses the oxidative phosphorylation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate using NAD+ as the co-enzyme
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
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GAPDH is a component of a multiprotein complex that repairs DNA lesions through the base excision repair pathway
metabolism
GAPDH not only catalyses the sixth step of glycolysis, but is also implicated in multiple nonmetabolic processes. Glycolytic flux controls D-serine synthesis through glyceraldehyde-3-phosphate dehydrogenase in astrocytes. Astrocytic energy metabolism controls D-serine production, thereby influencing glutamatergic neurotransmission in the hippocampus, overview. Involvement of glycolysis in modulating D-serine levels
metabolism
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glyceraldehyde-3-phosphate dehydrogenase, GAPDH, is a key enzyme of glycolysis
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 EMP pathway can be controlled through the glyceraldehyde 3-phosphate node by NAD+-GAPDH activity, recombinant NADP+-GAPDH heterologous activity can also exert a similar response, which modulates the glucose uptake and also the acetic acid production rate
metabolism
the enzyme is involved in glycolysis catalyzing a key reaction
metabolism
the enzyme is involved in glycolysis, the glycolytic conversion of glucose to pyruvic acid
metabolism
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anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
metabolism
different roles of GAPDH1 and GAPDH2 in lipid biosynthesis in Mortierella alpina
metabolism
different roles of GAPDH1 and GAPDH2 in lipid biosynthesis in Mortierella alpina. The GAPDH2 might be a moonlighting protein
metabolism
enzyme GAPDHS is essential in glycolysis
metabolism
glyceraldehyde 3-phosphate dehydrogenase (FgGAPDH) is a key enzyme of the glycolytic pathway
metabolism
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the glycolytic pathway that catalyzes the conversion of D-glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate
metabolism
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is the sixth enzyme in the glycolytic pathway, in which it converts D-glyceraldehyde 3-phosphate (D-G3P) to 1,3-bisphosphoglycerate and consumes inorganic phosphate using NAD+ as a coenzyme
metabolism
glyceraldehyde-3-phosphate dehydrogenase is a critical metabolic enzyme in the stony coral Acropora millepora
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
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
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
metabolism
mechanism of NADH-channeling from D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to L-lactate dehydrogenase (LDH). Enzyme kinetics studies show that LDH activity with free NADH and GAPDH-NADH complex always take place in parallel. The channeling is observed only in assays that mimic cytosolic conditions where free NADH concentration is negligible and the GAPDH-NADH complex is dominant. Molecular dynamics and protein-protein interaction studies show that LDH and GAPDH can form a leaky channeling complex only at the limiting NADH concentrations. Surface calculations show that positive electric field between the NAD(H) binding sites on LDH and GAPDH tetramers can merge in the LDH-GAPDH complex. NAD(H)-channeling within the LDH-GAPDH complex can be an extension of NAD(H)-channeling within each tetramer. In the case of a transient LDH-(GAPDH-NADH) complex, the relative contribution from the channeled and the diffusive paths depends on the overlap between the off-rates for the LDH-(GAPDH-NADH) complex and the GAPDH-NADH complex. The GAPDH complex can be observed in cell extracts, and with purified proteins in conditions that mimic high protein concentrations in cytosol
metabolism
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the enzyme is important in the carbon metabolism in plant leaves, overview
metabolism
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is the sixth enzyme in the glycolytic pathway, in which it converts D-glyceraldehyde 3-phosphate (D-G3P) to 1,3-bisphosphoglycerate and consumes inorganic phosphate using NAD+ as a coenzyme
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metabolism
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different roles of GAPDH1 and GAPDH2 in lipid biosynthesis in Mortierella alpina
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metabolism
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different roles of GAPDH1 and GAPDH2 in lipid biosynthesis in Mortierella alpina. The GAPDH2 might be a moonlighting protein
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metabolism
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the enzyme is involved in glycolysis catalyzing a key reaction
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metabolism
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the enzyme is involved in glycolysis
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metabolism
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a key enzyme of glycolysis, catalyses the oxidative phosphorylation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate using NAD+ as the co-enzyme
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metabolism
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glyceraldehyde-3-phosphate dehydrogenase, GAPDH, is a key enzyme of glycolysis
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metabolism
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is the sixth enzyme in the glycolytic pathway, in which it converts D-glyceraldehyde 3-phosphate (D-G3P) to 1,3-bisphosphoglycerate and consumes inorganic phosphate using NAD+ as a coenzyme
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physiological function
a GAPDH-deficient mutant can still grow in medium with glucose or other sugars as the sole carbon source, and no phosphofructokinase activity is detectable.The mutant can not utilize pyruvate as sole carbon source, whereas the wild-type can. Inactivation of GAPDH results in impairment of bacterial growth and virulence in the host plant, and reduction of intracellular ATP and extracellularpolysaccharide
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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downregulation of GAPDH using siRNA reduces both macrophage colony stimulating factor CSF-1 mRNA and protein levels, through destabilizing CSF-1 mRNA. CSF-1 mRNA half-lives are decreased by 50% in the presence of GAPDH siRNA. GAPDH associates with a large AU-rich containing regionof CSF-1
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
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GAPDH is a translational suppressor of angiotensin II type 1 receptor expression and mediates the effect of H2O2 on angiotensin II type 1 receptor mRNA
physiological function
GAPDH physically associates with DNA repair enzyme APE1. This interaction allows GAPDH to convert the oxidized species of APE1 to the reduced form, thereby reactivating its endonuclease activity to cleave abasic sites
physiological function
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interaction of GAPDH with Porphyromonas gingivalis major fimbrae plays an important role in Porphyromonas gingivalis colonization. Amino acid residues 166 to 183 of Streptococcus oralis GAPDH exhibit the strongest binding activity toward rFimA, and the synthetic peptide corresponding to amino acid residues 166 to 183 of GAPDH, peptide DNFGVVEGLMTTIHAYTG inhibits Streptococcus oralis-Porphyromonas gingivalis biofilm formation in a dose-dependent manner. The peptide inhibits interbacterial biofilm formation by several oral streptococci and Porphyromonas gingivalis strains with different types of FimA
physiological function
reduction of transcription by 41% and 67% using RNAi leads to transformants with sluggish motility and less active than wild-type
physiological function
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the adhesion mechanism of the lactobacilli is in part due to GAPDH binding to human ABO-type blood group antigens expressed on human colonic mucin. After periodate oxidation of colonic mucin, adhesion of Lactobacillus plantarum LA 318 bacterial cells significantly decreases compared to normal human colonic mucin. High binding is observed to A and B group antigens, while binding to H group antigen is lower. No interaction is observed between GAPDH and various monosaccharides. GAPDH binding to the B-trisaccharide biotinyl polymer probe [Gala1-3 (Fuca1-2) Gal-] is significantly higher as compared to B-disaccharide, Lewis D-trisaccharide, 3-fucosyl-N-acetylglucosamine and a-N-acetylneuraminic acid biotinyl polymer-probes
physiological function
the GAPDH gene product is a heat shock protein which might be involved in the developmental phase of the Lentinus polychrous
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
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deletion mutants of isoforms TDH1, TDH2, TDH3 show decreased enzymic activity following the trend ?tdh3>?tdh2>?tdh1 in both YEPD or YEPE medium. TDH3 encodes the major GAPDH isoenzyme. The GAPDH total activity is significantly lower in all genotypes grown on ethanol in comparison with the activity on glucose. A downregulation of GAPDH activity does not contribute to improved performance of engineered Saccharomyces cerevisiae on pentose substrates
physiological function
enzyme shows high affinity for Porphyromonas gingivalis proteins tonB-dependent receptor protein RagA4, 4-hydroxybutyryl-coenzyme A dehydratase AbfD, GAPDH, NAD-dependent glutamate dehydrogenase GDH, and malate dehydrogenase MDH. tonB-Dependent receptor protein RagA4, 4-hydroxybutyryl-coenzyme A dehydratase AbfD and NAD-dependent glutamate dehydrogenase GDH enhance coaggregation, whereas GAPDH and malate dehydrogenase inhibite coaggregation
physiological function
Q81X74, YP_027084
human plasminogen predominantly interacts with the GapA isoform at physiological concentrations and the interaction is lysine dependent
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
when endogenous phosphorylating NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Corynebacterium glutamicum is replaced by nonphosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (GapN) from Clostridium acetobutylicum, this NADPH-generating glycolytic pathway does not allow for the growth of Corynebacterium glutamicum with glucose as the sole carbon source. Heterologous expression of udhA encoding soluble transhydrogenase from Escherichia coli partly restores growth
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
apurinic/apyrimidinic (AP) sites are some of the most frequent DNA damages and the key intermediates of base excision repair. Certain proteins can interact with the deoxyribose of the AP site to form a Schiff base, which can be stabilized by NaBH4 treatment. The enzyme interacts with single-stranded AP DNA and AP DNA duplex with both 5' and 3' dangling ends. The protein forming this adduct is an isoform of glyceraldehyde-3-phosphate dehydrogenase called uracil-DNA glycosylase. GAPDH, at least partially, is covalently linked with the AP site by a mechanism other than the Schiff base formation. In spite of the ability to form a Schiff-base intermediate with the deoxyribose of the AP site, GAPDH does not display the AP lyase activity. In addition, along with the borohydride-dependent adducts with AP DNAs containing single-stranded regions, GAPDH was also shown to form the stable borohydride-independent crosslinks with these AP DNAs. GAPDH crosslinks preferentially to AP DNAs cleaves via the beta-elimination mechanism (spontaneously or by AP lyases) as compared to DNAs containing the intact AP site. The level of GAPDH-AP DNA adduct formation depends on oxidation of the protein SH-groups. Disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA
physiological function
apurinic/apyrimidinic (AP) sites are some of the most frequent DNA damages and the key intermediates of base excision repair. Certain proteins can interact with the deoxyribose of the AP site to form a Schiff base, which can be stabilized by NaBH4 treatment. The enzyme interacts with single-stranded AP DNA and AP DNA duplex with both 5' and 3' dangling ends. The protein forming this adduct is an isoform of glyceraldehyde-3-phosphate dehydrogenase called uracil-DNA glycosylase. GAPDH, at least partially, is covalently linked with the AP site by a mechanism other than the Schiff base formation. In spite of the ability to form a Schiff-base intermediate with the deoxyribose of the AP site, GAPDH does not display the AP lyase activity. In addition, along with the borohydride-dependent adducts with AP DNAs containing single-stranded regions, GAPDH was also shown to form the stable borohydride-independent crosslinks with these AP DNAs. GAPDH crosslinks preferentially to AP DNAs cleaves via the beta-elimination mechanism (spontaneously or by AP lyases) as compared to DNAs containing the intact AP site. The level of GAPDHAP DNA adduct formation depends on oxidation of the protein SH-groups. Disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA
physiological function
cellular glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a phylogenetically conserved, ubiquitous enzyme that plays an indispensable role in energy metabolism. The extracellular GAPDH in human serum is a multimeric, high-molecular-weight, yet glycolytically active enzyme, the enzymatic function of serum GAPDH remained unaffected by the multimers
physiological function
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diverse functions of GAPDH, including roles in membrane trafficking, apoptosis, and autophagy in addition to GAPDH's canonical role within the glycolytic and gluconeogenic pathways. In this capacity it converts D-glyceraldehyde-3-phosphate and NAD+ to 1,3-bisphosphoglycerate and NADH in the glycolytic pathway, or the reverse reaction in the gluconeogenic pathway. GAPDH plays a central role in carbohydrate metabolismin ground squirrels, which typically shift to non-carbohydrate fuels during winter hibernation, stable suppression of GAPDH (possibly by some reversible posttranslational modification) during ground squirrel torpor, which likely contributes to the overall reduction in carbohydrate metabolism when these animals switch to lipid fuels during dormancy. GAPDH regulation by reversible phosphorylation
physiological function
enzyme Gapdh is likely to have multiple nonglycolytic functions in the parasite in additon to its function in glycolysis. During intra-erythrocytic phage of its life cycle in humans, the parasite solely relies on glycolysis for its energy needs
physiological function
enzyme Gapdh is likely to have multiple nonglycolytic functions in the parasite in additon to its function in glycolysis. During intra-erythrocytic phage of its life cycle in humans, the parasite solely relies on glycolysis for its energy needs. PfGapdh appearing on the parasite cell surface can bind to extracellular proteins for moonlighting functions due to its specific interactions with with Pfeno, plasminogen, alpha-tubulin and lysozyme
physiological function
enzyme GAPDH plays a key role in glycolysis and gluconeogenesis by catalyzing the reversible oxidative phosphorylation of D-glyceraldehyde 3-phosphate to the energy-rich intermediate glyceraldehyde 1,3-bisphosphate
physiological function
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GAPDH is required for the efficient repair of DNA lesions in Escherichia coli. Interaction occur between GAPDH and enzymes of the base excision repair pathway, namely the AP-endonuclease Endo IV and uracil DNA glycosylase. GAPDH is a component of a protein complex dedicated to the maintenance of genomic DNA integrity. Interaction of GAPDH with the single-stranded DNA binding protein may recruit GAPDH to the repair sites and implicates GAPDH in DNA repair pathways activated by profuse DNA damage, such as homologous recombination or the SOS response.
physiological function
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GAPDH plays essential role in glycolysis and gluconeogenesis as a housekeeping enzyme. Cyclic adenosine diphosphoribose (cADPR), an endogenous nucleotide derived from NAD+, mobilizes Ca2+ release from endoplasmic reticulum via ryanodine receptors (RyRs). cADPR interacts directly with enzyme GAPDH and induces the transient interaction between GAPDH and RyRs in vivo, without cADPR the interaction is weak. GAPDH is required for cADPR-mediated Ca2+ mobilization from endoplasmic reticulum via RyRs. cADPR-mediated Ca2+ signaling pathway is involved in a wide variety of cellular processes,1 e.g. abscisic acid signaling, calorie restriction in gut stem cell, circadian clock in plants, and long-term synaptic depression in hippocampus
physiological function
glyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyses one of the two steps in glycolysis which generate the reduced coenzyme NADH. This reaction precedes the two ATP generating steps
physiological function
glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes an inevitable step in the central metabolism of most industrially important sugars such as glucose, fructose and sucrose. During the glycolysis of 1 mol glucose and 2 mol of NADH are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme of the glycolytic pathway, reversibly catalyzing the sixth step of glycolysis and concurrently reducing the coenzyme NAD+ to NADH
physiological function
glyceraldehyde-3-phosphate dehydrogenase is an essential enzyme in the glycolytic pathway. GAPDH also displays a range of other functions unrelated to its glycolytic function. GAPDH is a 3'-AU-rich element-binding protein, it can selectively bind to AU-rich +element, RNA recognition mechanism, overview. NAD1 inhibition for GAPDH3 RNA binding capability indicates that GAPDH3 likely binds to the AU-rich or polyadenosine RNA substrates through its NAD+-binding domain in vitro
physiological function
glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, GAPDHS, is a sperm-specific glycolytic enzyme involved in energy production during spermatogenesis and sperm motility
physiological function
glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, GAPDHS, is a sperm-specific glycolytic enzyme involved in energy production during spermatogenesis and sperm motility
physiological function
glycolytic flux controls D-serine synthesis through glyceraldehyde-3-phosphate dehydrogenase in astrocytes. D-Serine production in astrocytes is modulated by the interaction between the D-serine synthetic enzyme serine racemase (SRR) and a glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPDH). In primary cultured astrocytes, glycolysis activity is negatively correlated with D-serine level. SRR interacts directly with GAPDH, and activation of glycolysis augments this interaction. GAPDH suppresses SRR activity by direct binding to GAPDH and through NADH, a product of GAPDH. NADH allosterically inhibits the activity of SRR by promoting the disassociation of ATP from SRR
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
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reversible post-translational modification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), particularly acetylation, contributes to the reciprocal regulation of glycolysis/gluconeogenesis. Lysine post-translational modification of glyceraldehyde-3-phosphate dehydrogenase regulates hepatic and systemic metabolism
physiological function
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Tdh3, an NAD+-binding protein, influences nuclear NAD+ levels. Tdh3 links nuclear Sir2 with NAD+ from the cytoplasm
physiological function
the C-terminal domain of human host cell glyceraldehyde 3-phosphate dehydrogenase plays an important role in suppression of tRNALys3 packaging into human immunodeficiency virus type-1 particles. Human immunodeficiency virus type-1 (HIV-1) requires the packaging of human tRNALys3 as a primer for effective viral reverse transcription. The binding of human GAPDH to Pr55gag is important for the suppression mechanism, and residues Asp256, Lys260, Lys263 and Glu267 of GAPDH are essential for the suppression of tRNALys3 packaging. The C-terminal domain of GAPDH (151-335) interacts with both the matrix region (MA, 1-132) and capsid N-terminal domain (CANTD, 133-282)
physiological function
the enzyme inhibits complement function as measured by haemolytic assay and membrane attack complex (MAC) formation, C3-binding property of Haemonchus contortus GAPDH is an additional function of the enzyme, and it represents another entity of complement-binding protein. Key role of the protein in immune modulation
physiological function
the enzyme is involved in glycolysis, the pathway plays an important role in tumor cells
physiological function
the enzyme of the human pathogen binds hemoglobin and heme, it is a heme-binding protein and might be playing a dynamic role in the success of the invasive and infective processes of this pathogen
physiological function
the enzyme plays a central role in glycolysis, and nonglycolytic processes such as nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis
physiological function
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the significance of D-glyceraldehyde-3-phosphate dehydrogenase is not restricted to its pivotal glycolytic function. GAPDH localized in the nucleus can be involved in numerous processes: regulation of the length of telomeres, DNA repair, gene expression, and regulation of cyclin functions. GAPDH may act as a specific scaffold for cytoskeleton-associated proteins independently of its catalytic activity
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
physiological function
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a 13C signal (i.e. systematic 13C/12C variation) at tree-ring glucose C-4 signal seems to be introduced by glyceraldehyde-3-phosphate dehydrogenases in the cytosol of leaves, which means commitment of glyceraldehyde 3-phosphate to 3-phosphoglycerate versus fructose 1,6-bisphosphate metabolism, and the contribution of non-phosphorylating versus phosphorylating glyceraldehyde-3-phosphate dehydrogenase to catalysing the glyceraldehyde 3-phosphate to 3-phosphoglycerate forward reaction of glycolysis. Modelling of the cytosolic oxidation-reduction (COR) cycle, a carbon-neutral mechanism supplying NADPH at the expense of ATP and NADH, which may help to maintain leaf-cytosolic redox balances. Carbon isotope fractionation by glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is modelled. A positive correlation between air vapour pressure deficit and 13C discrimination at glucose C-4 is observed
physiological function
apart from its glycolytic function, GAPDH displays a battery of moonlighting activities. Primary location of the tetrameric GAPDH is in the cytoplasm, where it conducts its canonical role in glycolysis
physiological function
cytosolic glyceraldehyde-3-phosphate dehydrogenase (NAD-GAPDH) is involved in a critical energetic step of glycolysis and also has many important functions besides its enzymatic activity. NAD-GAPDH enzyme catalyzes the phosphorylating-coupled oxidation of glyceraldehyde 3-phosphate. Its catalytic role in glycolysis is based on a highly reactive catalytic cysteine that is often target of oxidative modifications that blocks its enzymatic activity and in turns trigger other moonlighting non-glycolytic roles. NAD-GAPDH is phosphorylated in vivo, the enzyme depicts different activity, abundance and phosphorylation profiles during development of seeds that mainly accumulate lipids (castor oil seed). In castor oil seed, the activity slightly increased and total protein levels do not significantly change in the first half of seed development but both abruptly decreases in the second part of development, when triacylglycerol synthesis and storage begin
physiological function
cytosolic glyceraldehyde-3-phosphate dehydrogenase (NAD-GAPDH) is involved in a critical energetic step of glycolysis and also has many important functions besides its enzymatic activity. NAD-GAPDH enzyme catalyzes the phosphorylating-coupled oxidation of glyceraldehyde 3-phosphate. Its catalytic role in glycolysis is based on a highly reactive catalytic cysteine that is often target of oxidative modifications that blocks its enzymatic activity and in turns trigger other moonlighting non-glycolytic roles. NAD-GAPDH is phosphorylated in vivo, the enzyme depicts different activity, abundance and phosphorylation profiles during development of seeds that mainly accumulate starch (wheat). NAD-GAPDH activity gradually increases along wheat seed development, but protein levels and phosphorylation status exhibit only slight changes
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyses the conversion of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate using NAD+ as a cofactor. It is a moonlighting enzyme playing multiple roles in the regulation of mRNA stability, intracellular membrane trafficking, iron uptake and transport, DNA replication and repair, and nuclear RNA transport
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme, whose main role is to provide energy for different cellular functions. Also the enzyme appears to be involved in numerous cell processes that have no relation to glycolysis
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the glycolytic pathway that catalyzes the conversion of D-glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional enzyme that plays critical roles in bacterial pathogenesis in some pathogenic bacteria
physiological function
in Fasciola gigantica, the glyceraldehyde 3-phosphate dehydrogenase (FgGAPDH) is a key enzyme of the glycolytic pathway and catalyzes the reversible oxidative phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate, with the simultaneous reduction of NAD+ to NADH. The enzyme has various roles in the parasite
physiological function
isozyme GAPDH1 contributes to NADPH supply and lipid accumulation in Mortierella alpina, and has a distinct role from isozyme GAPDH2. Transcriptional analysis of genes gapdh1 and gapdh2 shows that they have opposing roles during lipid accumulation. GAPDH1 possesses a stronger catalyzing ability than GAPDH2
physiological function
Mycobacterium tuberculosis relocates several housekeeping proteins to the cell surface for capture and internalization of host iron carrier protein transferrin. One of the identified receptors is the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Mycobacterium tuberculosis glyceraldehyde-3-phosphate dehydrogenase (GAPDH) functions as a receptor for human lactoferrin. Human lactoferrin is sequestered at the bacterial surface by GAPDH. The enzyme is a virulence factor in the bacterium. Iron is chelated by the siderophore and transported via specific iron regulated transporters
physiological function
sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDHS) switches glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate by coupling with the reduction of NAD+ to NADH. The sperm-specific glycolysis enzyme is regulated by transcription factor SOX10 to promote uveal melanoma (UM) tumorigenesis. GAPDHS, which is regulated by SOX10, controls glycolysis and contributes to UM tumorigenesis. GAPDHS is involved in regulating the Warburg effect in UM cells. GAPDHS serves as a functional target gene in SOX10-mediated tumor proliferation and glycolysis in UM
physiological function
the protein CbbG is a glyceraldehyde-3-phosphate (Ga3P) dehydrogenase (Ga3PDHase) catalyzing the reversible oxidation of Ga3P to 1,3-bis-phospho-glycerate (1,3bisPGA), using specifically NAD+/NADH as cofactor. CbbG seems to be the only Ga3PDHase present in Nitrosomonas europaea, which is involved in reducing triose phosphate during autotrophic carbon fixation. Otherwise, in cells grown under conditions deprived of ammonia and oxygen, the enzyme can catalyze the glycolytic step of Ga3P oxidation producing NADH
physiological function
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the adhesion mechanism of the lactobacilli is in part due to GAPDH binding to human ABO-type blood group antigens expressed on human colonic mucin. After periodate oxidation of colonic mucin, adhesion of Lactobacillus plantarum LA 318 bacterial cells significantly decreases compared to normal human colonic mucin. High binding is observed to A and B group antigens, while binding to H group antigen is lower. No interaction is observed between GAPDH and various monosaccharides. GAPDH binding to the B-trisaccharide biotinyl polymer probe [Gala1-3 (Fuca1-2) Gal-] is significantly higher as compared to B-disaccharide, Lewis D-trisaccharide, 3-fucosyl-N-acetylglucosamine and a-N-acetylneuraminic acid biotinyl polymer-probes
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physiological function
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the protein CbbG is a glyceraldehyde-3-phosphate (Ga3P) dehydrogenase (Ga3PDHase) catalyzing the reversible oxidation of Ga3P to 1,3-bis-phospho-glycerate (1,3bisPGA), using specifically NAD+/NADH as cofactor. CbbG seems to be the only Ga3PDHase present in Nitrosomonas europaea, which is involved in reducing triose phosphate during autotrophic carbon fixation. Otherwise, in cells grown under conditions deprived of ammonia and oxygen, the enzyme can catalyze the glycolytic step of Ga3P oxidation producing NADH
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physiological function
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional enzyme that plays critical roles in bacterial pathogenesis in some pathogenic bacteria
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physiological function
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isozyme GAPDH1 contributes to NADPH supply and lipid accumulation in Mortierella alpina, and has a distinct role from isozyme GAPDH2. Transcriptional analysis of genes gapdh1 and gapdh2 shows that they have opposing roles during lipid accumulation. GAPDH1 possesses a stronger catalyzing ability than GAPDH2
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physiological function
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the protein CbbG is a glyceraldehyde-3-phosphate (Ga3P) dehydrogenase (Ga3PDHase) catalyzing the reversible oxidation of Ga3P to 1,3-bis-phospho-glycerate (1,3bisPGA), using specifically NAD+/NADH as cofactor. CbbG seems to be the only Ga3PDHase present in Nitrosomonas europaea, which is involved in reducing triose phosphate during autotrophic carbon fixation. Otherwise, in cells grown under conditions deprived of ammonia and oxygen, the enzyme can catalyze the glycolytic step of Ga3P oxidation producing NADH
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physiological function
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glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes an inevitable step in the central metabolism of most industrially important sugars such as glucose, fructose and sucrose. During the glycolysis of 1 mol glucose and 2 mol of NADH are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate
-
physiological function
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glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, GAPDHS, is a sperm-specific glycolytic enzyme involved in energy production during spermatogenesis and sperm motility
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physiological function
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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
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physiological function
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Mycobacterium tuberculosis relocates several housekeeping proteins to the cell surface for capture and internalization of host iron carrier protein transferrin. One of the identified receptors is the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Mycobacterium tuberculosis glyceraldehyde-3-phosphate dehydrogenase (GAPDH) functions as a receptor for human lactoferrin. Human lactoferrin is sequestered at the bacterial surface by GAPDH. The enzyme is a virulence factor in the bacterium. Iron is chelated by the siderophore and transported via specific iron regulated transporters
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physiological function
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reversible post-translational modification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), particularly acetylation, contributes to the reciprocal regulation of glycolysis/gluconeogenesis. Lysine post-translational modification of glyceraldehyde-3-phosphate dehydrogenase regulates hepatic and systemic metabolism
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physiological function
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the GAPDH gene product is a heat shock protein which might be involved in the developmental phase of the Lentinus polychrous
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physiological function
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Mycobacterium tuberculosis relocates several housekeeping proteins to the cell surface for capture and internalization of host iron carrier protein transferrin. One of the identified receptors is the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Mycobacterium tuberculosis glyceraldehyde-3-phosphate dehydrogenase (GAPDH) functions as a receptor for human lactoferrin. Human lactoferrin is sequestered at the bacterial surface by GAPDH. The enzyme is a virulence factor in the bacterium. Iron is chelated by the siderophore and transported via specific iron regulated transporters
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physiological function
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
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physiological function
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Tdh3, an NAD+-binding protein, influences nuclear NAD+ levels. Tdh3 links nuclear Sir2 with NAD+ from the cytoplasm
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physiological function
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the protein CbbG is a glyceraldehyde-3-phosphate (Ga3P) dehydrogenase (Ga3PDHase) catalyzing the reversible oxidation of Ga3P to 1,3-bis-phospho-glycerate (1,3bisPGA), using specifically NAD+/NADH as cofactor. CbbG seems to be the only Ga3PDHase present in Nitrosomonas europaea, which is involved in reducing triose phosphate during autotrophic carbon fixation. Otherwise, in cells grown under conditions deprived of ammonia and oxygen, the enzyme can catalyze the glycolytic step of Ga3P oxidation producing NADH
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physiological function
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional enzyme that plays critical roles in bacterial pathogenesis in some pathogenic bacteria
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physiological function
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the protein CbbG is a glyceraldehyde-3-phosphate (Ga3P) dehydrogenase (Ga3PDHase) catalyzing the reversible oxidation of Ga3P to 1,3-bis-phospho-glycerate (1,3bisPGA), using specifically NAD+/NADH as cofactor. CbbG seems to be the only Ga3PDHase present in Nitrosomonas europaea, which is involved in reducing triose phosphate during autotrophic carbon fixation. Otherwise, in cells grown under conditions deprived of ammonia and oxygen, the enzyme can catalyze the glycolytic step of Ga3P oxidation producing NADH
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physiological function
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glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes an inevitable step in the central metabolism of most industrially important sugars such as glucose, fructose and sucrose. During the glycolysis of 1 mol glucose and 2 mol of NADH are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate
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physiological function
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enzyme Gapdh is likely to have multiple nonglycolytic functions in the parasite in additon to its function in glycolysis. During intra-erythrocytic phage of its life cycle in humans, the parasite solely relies on glycolysis for its energy needs. PfGapdh appearing on the parasite cell surface can bind to extracellular proteins for moonlighting functions due to its specific interactions with with Pfeno, plasminogen, alpha-tubulin and lysozyme
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additional information
comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
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detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
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detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
importance of Phe34 in NAD+ binding, Phe34 is stabilized in the presence of NAD+ but displays greater mobility in its absence. The oxidative state of the active site Cys149 residue is regulated by NAD+ binding, because this residue is found oxidized in the absence of dinucleotide. The distance between Cys149 and His176 decreases upon NAD binding and Cys149 remains in a reduced state when NAD+ is bound, cofactor binding and active site structures, catalytic mechanism, overview
additional information
kinetic and chemical mechanism of Mtb-GAPDH, overview. C158 is the active site nucleophile reacting with the aldehyde group of D-glyceraldehyde 3-phosphate to generate the thiohemiacetal and H185 is additionally required to either stabilize thiolate anion formation or act as a catalytic acid/base group
additional information
molecular docking simulation
additional information
molecular modeling of FhGAPDH monomer, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers
additional information
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molecular modeling of FhGAPDH monomer, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers
additional information
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possible existence of actin/active GAPDH dimer complexes similar to 3-phosphoglycerate kinase/active GAPDH dimer complexes
additional information
sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS, is stabilized by additional proline residues and an interdomain salt bridge. Residues P164, P326, and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at expense of the catalytic activity. Comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS, is stabilized by additional proline residues and an interdomain salt bridge. Residues P164, P326, and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at expense of the catalytic activity. Comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
the enzyme's catalytic domain interrupts interacting sites in the NAD+-binding domain of GAPDH
additional information
the phosphate group of the substrate is bound to the phosphate site in all four subunits, adenosyl binding pocket structure, comparison of group B Streptococcus ternary complex of enzyme with substrate and cofactor with human structure, comparative structure-function analysis of GBS GAPDH and hGAPDH, conformational changes upon ligand binding, overview. The active site residue Cys152 is positioned between the nicotinamide moiety of NAD+ and the side chain of active site residue His179
additional information
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comparison of Gapdh protein from Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, homology modeling, overview. The Gapdh from Thermoanaerobacterium saccharolyticum is less sensitive to ethanol and the NAD+/NADH ratio. Recombinant Gapdh from Thermoanaerobacterium saccharolyticum expressed in Clostridium thermocellum cells can improve the growth rate and ethanol resistance
additional information
denatured GAPDH, in contrast to the native enzyme, interacts with the bacterial chaperonin GroEL and beta-amyloid peptide 1-42
additional information
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denatured GAPDH, in contrast to the native enzyme, interacts with the bacterial chaperonin GroEL and beta-amyloid peptide 1-42
additional information
docking analysis of cofactor NAD+ and substrate glyceraldehyde 3-phosphate, identification and structure analysis of the binding sites, overview. Enzyme structure homology modeling using the structure of NAD+ bound BmGAPDH from Brugia malayi (PDB ID 4K9D) as template
additional information
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docking analysis of cofactor NAD+ and substrate glyceraldehyde 3-phosphate, identification and structure analysis of the binding sites, overview. Enzyme structure homology modeling using the structure of NAD+ bound BmGAPDH from Brugia malayi (PDB ID 4K9D) as template
additional information
docking and molecular dynamics simulations of the interaction between rabbit muscle GAPDH and rabbit muscle or porcine heart LDH, structure analysis and calculation of the rm(ph)LDH-rmGAPDH complex, overview. Multiscale MD calculations and molecular docking studies showed that rmLDH and rmGAPDH can form a dynamic complex facing each other with their NAD(H) binding sites. The complex breaks apart when the two enzymes are saturated with NAD(H) molecules. The complex breaks apart when the two enzymes are saturated with NAD(H) molecules. When rmLDH and rmGAPDH form a complex, the positive cavities on the surface of each enzyme merge to form a central positive cavity under the protein surface. The cavity connects four NAD(H) binding sites with an average separation of 2.9 nm between the adjacent sites. Thus, NADH channeling within the rmLDH-rmGAPDH complex can be an extension of NADH channeling between the two adjacent monomers in rmLDH and rmGAPDH tetramers. Analysis of interaction between phLDH and byGAPDH by analytical ultracentrifugation, on velocity experiments for detection of interaction between phLDH and byGAPDH. It is a transient protein-protein interactions and NADH channeling in cells
additional information
each GAPDH monomer contains a molecule of glyceraldehyde-3 phosphate in a non-previously identified site. The catalytic Cys149 is covalently attached to an about 300 Da molecule, possibly glutathione. This modification alters the conformation of an adjacent alpha-helix in the catalytic domain, right opposite to the NAD+ binding site. The conformation of the alpha-helix is stabilized after soaking the crystals with NAD+. Enzyme structure analysis, structure modeling, detailed overview
additional information
phosphate ion-binding sites structure analysis. Superimposition of GBS GAPDH and a ternary complex of GBS GAPDH (PDB ID 5jya), structure comparisons of ligand-binding state and of ternary complex enzyme and apoenzyme, implications for the catalytic mechanism, overview
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
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
additional information
structure homology modeling of GAPDH using the tetrameric GAPDH structure from Bacillus stearothermophilus (PDB ID 1GD1) as template. The glycine-valine-asparagine tripeptide sequence (at positions 140, 141, and 142 respectively) is highly conserved in several GAPDH homologues
additional information
the GAPDH enzyme from the reef-building stony coral Acropora millepora is a rather typical eukaryotic GAPDH, comprising an N-terminal NAD+-binding Rossman fold and a catalytic domain that provides important active site residues
additional information
the S-loop of GAPDH is required for interaction of the enzyme with its cofactor and with other proteins. NAD+-bound GAPDH S-loop fixation occurs by the formation of a complex with the coenzyme NAD+. The structure of trehalose-bound ecGAPDH is compared with the structures of both NAD+-free and NAD+-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4° rotation compared with the NAD+-free ecGAPDH structure and a 3.1° rotation compared with the NAD+-bound ecGAPDH structure
additional information
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the S-loop of GAPDH is required for interaction of the enzyme with its cofactor and with other proteins. NAD+-bound GAPDH S-loop fixation occurs by the formation of a complex with the coenzyme NAD+. The structure of trehalose-bound ecGAPDH is compared with the structures of both NAD+-free and NAD+-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4° rotation compared with the NAD+-free ecGAPDH structure and a 3.1° rotation compared with the NAD+-bound ecGAPDH structure
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three-dimensional structure analysis of EcGAPDH1 compared with the structures of HuGAPDH and MrsaGAPDH shows that the main difference is the loop conformation, especially the S-loop
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three-dimensional structure analysis of EcGAPDH1 compared with the structures of HuGAPDH and MrsaGAPDH shows that the main difference is the loop conformation, especially the S-loop
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phosphate ion-binding sites structure analysis. Superimposition of GBS GAPDH and a ternary complex of GBS GAPDH (PDB ID 5jya), structure comparisons of ligand-binding state and of ternary complex enzyme and apoenzyme, implications for the catalytic mechanism, overview
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kinetic and chemical mechanism of Mtb-GAPDH, overview. C158 is the active site nucleophile reacting with the aldehyde group of D-glyceraldehyde 3-phosphate to generate the thiohemiacetal and H185 is additionally required to either stabilize thiolate anion formation or act as a catalytic acid/base group
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structure homology modeling of GAPDH using the tetrameric GAPDH structure from Bacillus stearothermophilus (PDB ID 1GD1) as template. The glycine-valine-asparagine tripeptide sequence (at positions 140, 141, and 142 respectively) is highly conserved in several GAPDH homologues
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additional information
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structure homology modeling of GAPDH using the tetrameric GAPDH structure from Bacillus stearothermophilus (PDB ID 1GD1) as template. The glycine-valine-asparagine tripeptide sequence (at positions 140, 141, and 142 respectively) is highly conserved in several GAPDH homologues
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additional information
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phosphate ion-binding sites structure analysis. Superimposition of GBS GAPDH and a ternary complex of GBS GAPDH (PDB ID 5jya), structure comparisons of ligand-binding state and of ternary complex enzyme and apoenzyme, implications for the catalytic mechanism, overview
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