Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of FAO hepatoma cells with mutations of all 4 lysine residues K115, K160, K225, and K252 (4K-R-GAPDH) in critical regions of enzyme GAPDH to mimic their unmodified state reduces GAPDH glycolytic activity and glycolytic flux and increases gluconeogenic GAPDH activity and glucose production, phenotype overview | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
perinuclear region | the localization of enzyme mutant 4K-R-GAPDH remains primarily perinuclear in the basal state, similar to wild-type enzyme GAPDH in cells | Mus musculus | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Mus musculus | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Mus musculus C57BL6 | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Mus musculus C57BL6 | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
acylation | acetylation of lysine residues Lys115, -160, -225, and -252 as post-translational modification of glyceraldehyde-3-phosphate dehydrogenase. GAPDH acetylation is reduced in obese and type 2 diabetic db/db mice. Lys115, -225, and -252 are acetylated in a coordinated manner by the p300/cAMP response element-binding protein (CBP)-associated factor acetyltransferase, whereas Lys160 is acetylated by the p300/CBP acetyltransferase | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
hepatocyte | - |
Mus musculus | - |
hepatoma cell | - |
Mus musculus | - |
liver | - |
Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Mus musculus | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Mus musculus C57BL6 | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
GAPDH | - |
Mus musculus |
glyceraldehyde-3-phosphate dehydrogenase | - |
Mus musculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Mus musculus | |
NADH | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | 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 | Mus musculus |
physiological function | 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 | Mus musculus |