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Literature summary for 1.2.1.12 extracted from
- Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) protein-protein interaction inhibitor reveals a non-catalytic role for GAPDH oligomerization in cell death (2016), J. Biol. Chem., 291, 13608-13621 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| sequence comparisons | Homo sapiens |
| sequence comparisons | Rattus norvegicus |
| sequence comparisons | Mus musculus |
| sequence comparisons | Danio rerio |
| sequence comparisons | Gallus gallus |
| sequence comparisons | Anolis carolinensis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH | Anolis carolinensis | |
| additional information | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH | Danio rerio | |
| additional information | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH | Gallus gallus | |
| additional information | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH | Homo sapiens | |
| additional information | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH | Mus musculus | |
| additional information | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH | Rattus norvegicus | |
| pseudo-GAPDH | psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction | Anolis carolinensis | |
| pseudo-GAPDH | psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction | Danio rerio | |
| pseudo-GAPDH | psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction | Gallus gallus | |
| pseudo-GAPDH | psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction | Homo sapiens | |
| pseudo-GAPDH | psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction | Mus musculus | |
| pseudo-GAPDH | psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction | Rattus norvegicus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Homo sapiens | 5829 | - |
| cytosol | - |
Rattus norvegicus | 5829 | - |
| cytosol | - |
Mus musculus | 5829 | - |
| cytosol | - |
Danio rerio | 5829 | - |
| cytosol | - |
Gallus gallus | 5829 | - |
| cytosol | - |
Anolis carolinensis | 5829 | - |
| mitochondrion | - |
Homo sapiens | 5739 | - |
| mitochondrion | - |
Rattus norvegicus | 5739 | - |
| mitochondrion | - |
Mus musculus | 5739 | - |
| mitochondrion | - |
Danio rerio | 5739 | - |
| mitochondrion | - |
Gallus gallus | 5739 | - |
| mitochondrion | - |
Anolis carolinensis | 5739 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Homo sapiens | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |  |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Rattus norvegicus | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Mus musculus | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Danio rerio | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Gallus gallus | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Anolis carolinensis | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Rattus norvegicus Wistar | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Anolis carolinensis | H9GBL1 | - |
- |
| Danio rerio | Q6NYI5 | - |
- |
| Gallus gallus | P00356 | - |
- |
| Homo sapiens | P04406 | - |
- |
| Mus musculus | P16858 | - |
- |
| Rattus norvegicus | P04797 | - |
- |
| Rattus norvegicus Wistar | P04797 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | phosphorylation of GAPDH by delta protein kinase C (deltaPKC). When deltaPKC is inactive, its GAPDH-docking site may be occupied by a pseudo-GAPDH (psiGAPDH) site, a GAPDH-like sequence that mimics the deltaPKC-binding site on GAPDH, overview | Homo sapiens |
| phosphoprotein | phosphorylation of GAPDH by delta protein kinase C (deltaPKC). When deltaPKC is inactive, its GAPDH-docking site may be occupied by a pseudo-GAPDH (psiGAPDH) site, a GAPDH-like sequence that mimics the deltaPKC-binding site on GAPDH, overview | Rattus norvegicus |
| phosphoprotein | phosphorylation of GAPDH by delta protein kinase C (deltaPKC). When deltaPKC is inactive, its GAPDH-docking site may be occupied by a pseudo-GAPDH (psiGAPDH) site, a GAPDH-like sequence that mimics the deltaPKC-binding site on GAPDH, overview | Mus musculus |
| phosphoprotein | phosphorylation of GAPDH by delta protein kinase C (deltaPKC). When deltaPKC is inactive, its GAPDH-docking site may be occupied by a pseudo-GAPDH (psiGAPDH) site, a GAPDH-like sequence that mimics the deltaPKC-binding site on GAPDH, overview | Danio rerio |
| phosphoprotein | phosphorylation of GAPDH by delta protein kinase C (deltaPKC). When deltaPKC is inactive, its GAPDH-docking site may be occupied by a pseudo-GAPDH (psiGAPDH) site, a GAPDH-like sequence that mimics the deltaPKC-binding site on GAPDH, overview | Gallus gallus |
| phosphoprotein | phosphorylation of GAPDH by delta protein kinase C (deltaPKC). When deltaPKC is inactive, its GAPDH-docking site may be occupied by a pseudo-GAPDH (psiGAPDH) site, a GAPDH-like sequence that mimics the deltaPKC-binding site on GAPDH, overview | Anolis carolinensis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| heart | - |
Homo sapiens | - |
| heart | - |
Rattus norvegicus | - |
| heart | - |
Mus musculus | - |
| heart | - |
Danio rerio | - |
| heart | - |
Gallus gallus | - |
| heart | - |
Anolis carolinensis | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Homo sapiens | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Rattus norvegicus | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Mus musculus | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Danio rerio | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Gallus gallus | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Anolis carolinensis | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Rattus norvegicus Wistar | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo | Homo sapiens |
| tetramer | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo | Rattus norvegicus |
| tetramer | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo | Mus musculus |
| tetramer | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo | Danio rerio |
| tetramer | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo | Gallus gallus |
| tetramer | either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo | Anolis carolinensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GAPDH | - |
Homo sapiens |
| GAPDH | - |
Rattus norvegicus |
| GAPDH | - |
Mus musculus |
| GAPDH | - |
Danio rerio |
| GAPDH | - |
Gallus gallus |
| GAPDH | - |
Anolis carolinensis |
| glyceraldehyde-3-phosphate dehydrogenase | - |
Homo sapiens |
| glyceraldehyde-3-phosphate dehydrogenase | - |
Rattus norvegicus |
| glyceraldehyde-3-phosphate dehydrogenase | - |
Mus musculus |
| glyceraldehyde-3-phosphate dehydrogenase | - |
Danio rerio |
| glyceraldehyde-3-phosphate dehydrogenase | - |
Gallus gallus |
| glyceraldehyde-3-phosphate dehydrogenase | - |
Anolis carolinensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
| 37 | - |
assay at | Rattus norvegicus |
| 37 | - |
assay at | Mus musculus |
| 37 | - |
assay at | Danio rerio |
| 37 | - |
assay at | Gallus gallus |
| 37 | - |
assay at | Anolis carolinensis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Homo sapiens |
| 7.4 | - |
assay at | Rattus norvegicus |
| 7.4 | - |
assay at | Mus musculus |
| 7.4 | - |
assay at | Danio rerio |
| 7.4 | - |
assay at | Gallus gallus |
| 7.4 | - |
assay at | Anolis carolinensis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Homo sapiens | |
| NAD+ | - |
Rattus norvegicus | |
| NAD+ | - |
Mus musculus | |
| NAD+ | - |
Danio rerio | |
| NAD+ | - |
Gallus gallus | |
| NAD+ | - |
Anolis carolinensis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Homo sapiens |
| 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 | Rattus norvegicus |
| 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 | Mus musculus |
| 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 | Danio rerio |
| 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 | Gallus gallus |
| 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 | Anolis carolinensis |
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