Activating Compound | Comment | Organism | Structure |
---|---|---|---|
actin | GAPDH catalytic activity is increased upon association with actin | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
tubulin | GAPDH catalytic activity is inhibited upon formation of a complex with tubulin | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
actin filament | specific interaction of actin with non-native GAPDH, i.e. dimers, monomers, the denatured forms of GAPDH | Homo sapiens | 5884 | - |
cytoplasm | predominantly cytoplasmic localization of tetrameric native form GAPDH within HeLa cells | Homo sapiens | 5737 | - |
additional information | immunohistochemic analysis of subcellular enzyme localization | Homo sapiens | - |
- |
nucleus | non-native GAPDH is unevenly distributed within the nuclei | Homo sapiens | 5634 | - |
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+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
HeLa cell | expressing Bcl-2, overproduction of the Bcl-2 protein does not change the non-native GAPDH localization in the growing HeLa-Bcl-2 cells | Homo sapiens | - |
HeLa cell | staining of HeLa cells with mAbs 6C5 reveals the predominant accumulation of the non-native forms of GAPDH, i.e. dimers, monomers, the denatured forms of GAPDH, in the nucleus during normal growth | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Homo sapiens | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
tetramer | - |
Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
D-glyceraldehyde-3-phosphate dehydrogenase | - |
Homo sapiens |
GAPDH | - |
Homo sapiens |
glyceraldehyde-3-phosphate dehydrogenase | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Homo sapiens | |
NADH | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | possible existence of actin/active GAPDH dimer complexes similar to 3-phosphoglycerate kinase/active GAPDH dimer complexes | Homo sapiens |
physiological function | 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 | Homo sapiens |