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Literature summary extracted from

  • Qvit, N.; Joshi, A.U.; Cunningham, A.D.; Ferreira, J.C.; Mochly-Rosen, D.
    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 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.12 sequence comparisons Homo sapiens
1.2.1.12 sequence comparisons Rattus norvegicus
1.2.1.12 sequence comparisons Mus musculus
1.2.1.12 sequence comparisons Danio rerio
1.2.1.12 sequence comparisons Gallus gallus
1.2.1.12 sequence comparisons Anolis carolinensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.1.12 cytosol
-
 Homo sapiens 5829
-
1.2.1.12 cytosol
-
 Rattus norvegicus 5829
-
1.2.1.12 cytosol
-
 Mus musculus 5829
-
1.2.1.12 cytosol
-
 Danio rerio 5829
-
1.2.1.12 cytosol
-
 Gallus gallus 5829
-
1.2.1.12 cytosol
-
 Anolis carolinensis 5829
-
1.2.1.12 mitochondrion
-
 Homo sapiens 5739
-
1.2.1.12 mitochondrion
-
 Rattus norvegicus 5739
-
1.2.1.12 mitochondrion
-
 Mus musculus 5739
-
1.2.1.12 mitochondrion
-
 Danio rerio 5739
-
1.2.1.12 mitochondrion
-
 Gallus gallus 5739
-
1.2.1.12 mitochondrion
-
 Anolis carolinensis 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+ Homo sapiens
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+ Rattus norvegicus
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+ Mus musculus
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+ Danio rerio
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+ Gallus gallus
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+ Anolis carolinensis
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+ Rattus norvegicus Wistar
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.12 Anolis carolinensis H9GBL1
-
-
1.2.1.12 Danio rerio Q6NYI5
-
-
1.2.1.12 Gallus gallus P00356
-
-
1.2.1.12 Homo sapiens P04406
-
-
1.2.1.12 Mus musculus P16858
-
-
1.2.1.12 Rattus norvegicus P04797
-
-
1.2.1.12 Rattus norvegicus Wistar P04797
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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

EC Number Source Tissue Comment Organism Textmining
1.2.1.12 heart
-
 Homo sapiens
-
1.2.1.12 heart
-
 Rattus norvegicus
-
1.2.1.12 heart
-
 Mus musculus
-
1.2.1.12 heart
-
 Danio rerio
-
1.2.1.12 heart
-
 Gallus gallus
-
1.2.1.12 heart
-
 Anolis carolinensis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Homo sapiens 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Rattus norvegicus 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Mus musculus 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Danio rerio 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Gallus gallus 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Anolis carolinensis 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Rattus norvegicus Wistar 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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

EC Number Synonyms Comment Organism
1.2.1.12 GAPDH
-
 Homo sapiens
1.2.1.12 GAPDH
-
 Rattus norvegicus
1.2.1.12 GAPDH
-
 Mus musculus
1.2.1.12 GAPDH
-
 Danio rerio
1.2.1.12 GAPDH
-
 Gallus gallus
1.2.1.12 GAPDH
-
 Anolis carolinensis
1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase
-
 Homo sapiens
1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase
-
 Rattus norvegicus
1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase
-
 Mus musculus
1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase
-
 Danio rerio
1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase
-
 Gallus gallus
1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase
-
 Anolis carolinensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.12 37
-
 assay at Homo sapiens
1.2.1.12 37
-
 assay at Rattus norvegicus
1.2.1.12 37
-
 assay at Mus musculus
1.2.1.12 37
-
 assay at Danio rerio
1.2.1.12 37
-
 assay at Gallus gallus
1.2.1.12 37
-
 assay at Anolis carolinensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.12 7.4
-
 assay at Homo sapiens
1.2.1.12 7.4
-
 assay at Rattus norvegicus
1.2.1.12 7.4
-
 assay at Mus musculus
1.2.1.12 7.4
-
 assay at Danio rerio
1.2.1.12 7.4
-
 assay at Gallus gallus
1.2.1.12 7.4
-
 assay at Anolis carolinensis

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.12 NAD+
-
 Homo sapiens
1.2.1.12 NAD+
-
 Rattus norvegicus
1.2.1.12 NAD+
-
 Mus musculus
1.2.1.12 NAD+
-
 Danio rerio
1.2.1.12 NAD+
-
 Gallus gallus
1.2.1.12 NAD+
-
 Anolis carolinensis

General Information

EC Number General Information Comment Organism
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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
1.2.1.12 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