1.2.1.12: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
This is an abbreviated version!
For detailed information about glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), go to the full flat file.
Word Map on EC 1.2.1.12
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1.2.1.12
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tetramer
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chloroplast
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gapcs
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streptococcal
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stearothermophilus
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glomerulonephritis
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nadp-dependent
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genorm
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normfinder
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medicine
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3-phosphoglycerate
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phosphofructokinase
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flagellum
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poststreptococcal
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1,3-bisphosphoglycerate
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bestkeeper
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lobster
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glycosomal
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2.7.1.11
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glyceraldehyde-phosphate
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nephritogenic
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4.1.2.13
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plr
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2.7.2.3
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endocapillary
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drug development
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agriculture
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biofuel production
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analysis
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synthesis
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biotechnology
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pharmacology
- 1.2.1.12
- tetramer
- chloroplast
-
gapcs
- streptococcal
- stearothermophilus
- glomerulonephritis
-
nadp-dependent
-
genorm
-
normfinder
- medicine
- 3-phosphoglycerate
-
phosphofructokinase
- flagellum
-
poststreptococcal
- 1,3-bisphosphoglycerate
-
bestkeeper
- lobster
- glycosomal
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2.7.1.11
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glyceraldehyde-phosphate
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nephritogenic
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4.1.2.13
- plr
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2.7.2.3
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endocapillary
- drug development
- agriculture
- biofuel production
- analysis
- synthesis
- biotechnology
- pharmacology
Reaction
Synonyms
3-phosphoglyceraldehyde dehydrogenase, A4-GAPDH, A4-glyceraldehyde-3-phosphate dehydrogenase, AB-GAPDH, AnBn-GAPDH, AsGAPDH, At3g04120, BARS-38, CbbG, CgGAP, Clo1313_2095, complement-C3-binding protein, CP 17/CP 18, Ctherm_Gapdh, cytosolic NAD-dependent glyceraldehyde 3-P dehydrogenase, cytosolic phosphorylating glyceraldehyde-3-phosphate dehydrogenase, D-glyceraldehyde-3-phosphate dehydrogenase, D-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating), dehydrogenase, glyceraldehyde phosphate, dihydrogenase, glyceraldehyde phosphate, EcGAPDH, EcGAPDH1, FgGAPDH, FhGAPDH, G3PD, G3PDH, Ga3P dehydrogenase, Ga3PDHase, GADPH, GAP, GAP1, gap2, GapA, GapB, GAPC, GapC-1, GapC1, GapC2, GAPCp, GAPCp1, GAPCp2, GAPD, GAPDH, GAPDH type 1, GAPDH1, GAPDH2, GAPDH3, GAPDHS, GAPDS, GAPN, GBS GAPDH, glyceraldehyde 3-phosphate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase-S, glyceraldehyde phosphate dehydrogenase (NAD), glyceraldehyde-3 phosphate dehydrogenase, glyceraldehyde-3-P-dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase (NAD), glyceraldehyde-3-phosphate dehydrogenase 1, glyceraldehyde-3-phosphate dehydrogenase, type I, glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein GAPDHS, glyceraldehyde-3-phosphate dehydrogenases, GPD, GPD2, Gra3PDH, GraP-DH, H.c-C3BP, hGAPDH, HsGAPDH, kmGAPDH1p, Larval antigen OVB95, Major larval surface antigen, Mtb-GAPDH, NAD+-dependent GAPDH, NAD+-dependent glyceraldehyde 3-phosphate dehydrogenase, NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD+-G-3-P dehydrogenase, NAD+-GAPDH, NAD-dependent Ga3PDHase, NAD-dependent glyceraldehyde 3-phosphate dehydrogenase, NAD-dependent glyceraldehyde phosphate dehydrogenase, NAD-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent phosphorylating glyceraldehyde-3-phosphate dehydrogenase, NAD-G3PDH, NAD-GAPDH, NADH-glyceraldehyde phosphate dehydrogenase, P-37, p-GAPDH, PfGAPDH, phosphoglyceraldehyde dehydrogenase, phosphorylating NAD+-dependent GAPDH, Plasmin receptor, Plasminogen-binding protein, plastidial glyceraldehyde-3-phosphate dehydrogenase, pmGAPDH, PyGapdh, rmGAPDH, Rv1436, somatic GAPD, somatic glyceraldehyde 3-phosphate dehydrogenase, sperm-specific GAPDS, sperm-specific glyceraldehyde 3-phosphate dehydrogenase, sperm-specific glyceraldehyde-3-phosphate dehydrogenase, TaeNAD-GAPDH, TagapC, TDH1, TDH2, TDH3, TLAb, triose phosphate dehydrogenase, UDG, uracil-DNA glycosylase, vGPD
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1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)Advanced search results
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results (Posttranslational Modification
Posttranslational Modification on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
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POSTTRANSLATIONAL MODIFICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acylation
alkylation
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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
phosphoprotein
proteolytic modification
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the precursor has a MW of 40000 Da, the processed polypeptide has a MW of 36000 Da
ribosylation
additional information
acylation
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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
acylation
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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
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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
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
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
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
phosphoprotein
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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
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
phosphoprotein
multiple phosphorylations changing the pI of the enzyme, overview
phosphoprotein
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multiple phosphorylations changing the pI of the enzyme, overview
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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
phosphoprotein
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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
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phosphoprotein
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
phosphoprotein
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
ribosylation
mono-ADP-ribosylation does not affect GADPH activity
additional information
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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+
additional information
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no signal peptide is found in the deduced protein
additional information
no signal peptide is found in the deduced protein
additional information
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4-hydroxy-2-nonenal-modified GAPDH is degraded by cathepsin G
additional information
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posttranslational modification of the enzyme with NADH is stimulated by thiols, possibly through superoxide, and is independent of NO
additional information
Plasmodium yoelii, Gapdh undergoes multiple posttranslational modifications
additional information
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Plasmodium yoelii, Gapdh undergoes multiple posttranslational modifications
additional information
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Plasmodium yoelii, Gapdh undergoes multiple posttranslational modifications
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additional information
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
additional information
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posttranslational modification of the enzyme by nitrogen oxide
additional information
Tetrahymena pyriformis E / ATCC 30005
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posttranslational modification of the enzyme by nitrogen oxide
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