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Literature summary for 1.2.1.12 extracted from

  • Bond, S.T.; Howlett, K.F.; Kowalski, G.M.; Mason, S.; Connor, T.; Cooper, A.; Streltsov, V.; Bruce, C.R.; Walder, K.R.; McGee, S.L.
    Lysine post-translational modification of glyceraldehyde-3-phosphate dehydrogenase regulates hepatic and systemic metabolism (2017), FASEB J., 31, 2592-2602 .
    View publication on PubMed
Search for more literature for 1.2.1.12

Protein Variants

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

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/ Products (Substrates)

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
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 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Mus musculus C57BL6
-
-
-

Posttranslational Modification

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

Source Tissue Comment Organism Textmining
hepatocyte
-
 Mus musculus
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hepatoma cell
-
 Mus musculus
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liver
-
 Mus musculus
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
GAPDH
-
 Mus musculus
glyceraldehyde-3-phosphate dehydrogenase
-
 Mus musculus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Mus musculus
NADH
-
 Mus musculus

General Information

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