methylation on residues Lys213 and Asp242, site specific alterations in methylation sites suggests that the stable changes observed in kinetic and structural GAPDH properties may be due to posttranslational modification of this enzyme during torpor
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
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
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
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
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
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
posttranslational phosphorylation on tyrosine residues, global reduction in GAPDH tyrosine phosphorylation during torpor that the stable changes observed in kinetic and structural GAPDH properties may be due to posttranslational modification of this enzyme during torpor. GAPDH regulation by reversible phosphorylation, action of commercial alkaline phosphatase causes a 50% increase in euthermic GAPDH activity, activities of protein kinase C, AMP-dependent protein kinase, or calcium-calmodulin protein kinase lead to about 80% decreases in euthermic GAPDH activity
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
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
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
cytosolic glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in vivo during seed development. In vitro phosphorylation assays with different plant protein kinases (WPK4, SOS2, GSK3, MAPK, CKII, Tsl, and CDPK), overview
cytosolic glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in vivo during seed development. NAD-GAPDH is phosphorylated in vitro at Ser205 by a SNF1-related protein kinase 1 (SnRK1) from wheat heterotrophic (but not from photosynthetic) tissues. The S205D mutant enzyme (mimicking the phosphorylated form) exhibits a significant decrease in activity but similar affinity toward substrates. In vitro phosphorylation assays with different plant protein kinases (WPK4, SOS2, GSK3, MAPK, CKII, Tsl, and CDPK), overview. Phosphorylation assays with wheat seed extract show that S66A and S124A NAD-GAPDH mutants are phosphorylated in a similar way like the wild-type enzyme, but the S205A mutant is recalcitrant to phosphorylation in any of the conditions assayed
GAPDH of enterohemorrhagic and enteropathogenic Escherichia coli-strains is ADP-ribosylated either in the cytoplasm or in the extracellular medium. GAPDH catalyzes its own modification involving residue C149 at the active site, reaction requires NAD+
O-GlcNAcylation at residue T227 interrupts the hydrophobic interfaces formed between the enzyme monomers in its terameric state and allows for nucleic translocation of the cytoplasmic enzyme