Any feedback?
Information on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and Organism(s) Rattus norvegicus and UniProt Accession Q9ESV6
for references in articles please use BRENDA:EC1.2.1.12Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)IUBMB Comments
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
Specify your search results
Word Map
- 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
-
2.7.1.11
-
glyceraldehyde-phosphate
-
nephritogenic
-
4.1.2.13
- plr
-
2.7.2.3
-
endocapillary
- drug development
- agriculture
- biofuel production
- analysis
- synthesis
- biotechnology
- pharmacology
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
gapdhs, d-glyceraldehyde-3-phosphate dehydrogenase, gapds, gadph, glyceraldehyde-3-phosphate dehydrogenases, plasmin receptor, gapc1, plasminogen-binding protein, gapcp, glyceraldehyde-3 phosphate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-phosphoglyceraldehyde dehydrogenase
-
-
-
-
BARS-38
-
-
-
-
CP 17/CP 18
-
-
-
-
dehydrogenase, glyceraldehyde phosphate
-
-
-
-
dihydrogenase, glyceraldehyde phosphate
-
-
-
-
G3PD
-
-
-
-
GAPDH
GAPDH1
-
-
-
-
GAPDH2
-
-
-
-
glyceraldehyde phosphate dehydrogenase (NAD)
-
-
-
-
glyceraldehyde-3-P-dehydrogenase
-
-
-
-
glyceraldehyde-3-phosphate dehydrogenase
glyceraldehyde-3-phosphate dehydrogenase (NAD)
-
-
-
-
GPD
-
-
-
-
Gra3PDH
-
-
-
-
GraP-DH
-
-
-
-
Larval antigen OVB95
-
-
-
-
Major larval surface antigen
-
-
-
-
NAD+-G-3-P dehydrogenase
-
-
-
-
NAD-dependent glyceraldehyde phosphate dehydrogenase
-
-
-
-
NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
NAD-G3PDH
-
-
-
-
NADH-glyceraldehyde phosphate dehydrogenase
-
-
-
-
P-37
-
-
-
-
phosphoglyceraldehyde dehydrogenase
-
-
-
-
Plasmin receptor
-
-
-
-
Plasminogen-binding protein
-
-
-
-
TLAb
-
-
-
-
triose phosphate dehydrogenase
-
-
-
-
GAPDH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating)
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
CAS REGISTRY NUMBER
COMMENTARY
9001-50-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
additional information
?
-
-
plays a role in microtubule dynamics in the early secretory pathway
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
additional information
?
-
-
plays a role in microtubule dynamics in the early secretory pathway
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-chlorohydrin
the contraceptive activity of alpha-chlorohydrin and its apparent specificity for the sperm isoform in vivo are likely to be due to differences in metabolism to 3-chlorolactaldehyde in spermatozoa and somatic cells
fumarate
-
inactivation of GAPDH by fumarate in vitro correlates with formation of S-(2-succinyl)cysteine, in diabetic compared with control rats fumarate and S-(2-succinyl)cysteine concentration increase approximately 5fold, accompanied by an about 25% decrease in GAPDH specific activity
Koningic acid
-
inhibits arsenate reductase activity and activity with D-glyceraldehyde 3-phosphate, phosphate and NAD+
pseudo-GAPDH
psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction
-
S-(2-succinyl)cysteine
-
chemical modification by S-(2-succinyl)cysteine causes irreversible inactivation of glyceraldehyde-3-phosphate dehydrogenase in vitro. In diabetic rats, succination of GAPDH is increased in muscle, and the extent of succination correlates strongly with the decrease in specific activity of the enzyme
additional information
-
not inhibited by thiorphan and lipopolysaccharide
-
additional information
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cytoplasmic expression is elevated in apoptosis and proliferation
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
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). G3PT_RAT
432
0
46708
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
unusually low His content compared to other mammalian muscle acetaldehyde phosphate dehydrogenases
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure determination by formation of soluble recombinant rat sperm glyceraldehyde-3-phosphate dehydrogenase as a heterotetramer with the Escherichia coli glyceraldehyde-3-phosphate dehydrogenase in a ratio of 1:3. Refinement to 2.2 A for the holo enzyme, to 2.4 A for the complex with glyceraldehyde 3-phosphate. Glyceraldehyde 3-phosphate binds in the Ps pocket in the active site of the sperm enzyme subunit in the presence of NAD
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T227A
mutation at site of O-GlcNAcylation. Mutation induces the cytoplasmic accumulation of glyceraldehyde 3-phosphate dehydrogenase
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the rat cDNA library is cloned in the target vector pTRG, Escherichia coli is used as a reporter strain
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
in diabetic rats, modification of GAPDH by S-(2-succinyl)cysteine is increased in muscle, and the extent of succination correlates strongly with the decrease in specific activity of the enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ryzlak, M.T.; Pietruszko, R.
Heterogeneity of glyceraldehyde-3-phosphate dehydrogenase from human brain
Biochim. Biophys. Acta
954
309-324
1988
Homo sapiens, Rattus norvegicus
Tso, J.Y.; Sun, X.H.; Kao, T.h.; Reece, K.S.; Wu, R.
Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene
Nucleic Acids Res.
13
2485-2502
1985
Homo sapiens, Rattus norvegicus
Gafni, A.
Age-related effects on subunit interactions in rat muscle glyceraldehyde-3-phosphate dehydrogenase
Curr. Top. Cell. Regul.
24
273-285
1984
Rattus norvegicus
Nagradova, N.K.; Safronova, M.I.; Baratova, L.A.; Belianova, L.P.
Structural studies on glyceraldehyde-phosphate dehydrogenase from rat skeletal muscle
Biochim. Biophys. Acta
532
1-5
1978
Rattus norvegicus
Harris, J.I.; Waters, M.
Glyceraldehyde-3-phosphate dehydrogenase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
1-49
1976
Geobacillus stearothermophilus, Bacillus cereus, Bos taurus, Saccharomyces cerevisiae, Canis lupus familiaris, Gallus gallus, Oryctolagus cuniculus, Escherichia coli, Felis catus, Hippoglossus sp., Homo sapiens, Lobster, Meleagris gallopavo, Pisum sativum, Rattus norvegicus, Acipenser sp., Sus scrofa, Thermus aquaticus
-
Tisdale, E.J.
Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway
J. Biol. Chem.
277
3334-3341
2002
Rattus norvegicus
Gregus, Z.; Nemeti, B.
The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase works as an arsenate reductase in human red blood cells and rat liver cytosol
Toxicol. Sci.
5
859-869
2005
Homo sapiens, Rattus norvegicus
Dhar-Chowdhury, P.; Harrell, M.D.; Han, S.Y.; Jankowska, D.; Parachuru, L.; Morrissey, A.; Srivastava, S.; Liu, W.; Malester, B.; Yoshida, H.; Coetzee, W.A.
The glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase, triose-phosphate isomerase, and pyruvate kinase are components of the K(ATP) channel macromolecular complex and regulate its function
J. Biol. Chem.
280
38464-38470
2005
Rattus norvegicus
Welch, J.E.; Barbee, R.R.; Magyar, P.L.; Bunch, D.O.; OBrien, D.A.
Expression of the spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase (GAPDS) in rat testis
Mol. Reprod. Dev.
73
1052-1060
2006
Rattus norvegicus
Shalova, I.N.; Cechalova, K.; Rehakova, Z.; Dimitrova, P.; Ognibene, E.; Caprioli, A.; Schmalhausen, E.V.; Muronetz, V.I.; Saso, L.
Decrease of dehydrogenase activity of cerebral glyceraldehyde-3-phosphate dehydrogenase in different animal models of Alzheimers disease
Biochim. Biophys. Acta
1770
826-832
2007
Oryctolagus cuniculus, Mus musculus, Rattus norvegicus
Blatnik, M.; Frizzell, N.; Thorpe, S.R.; Baynes, J.W.
Inactivation of glyceraldehyde-3-phosphate dehydrogenase by fumarate in diabetes: formation of S-(2-succinyl)cysteine, a novel chemical modification of protein and possible biomarker of mitochondrial stress
Diabetes
57
41-49
2008
Oryctolagus cuniculus, Rattus norvegicus
Barbini, L.; Rodriguez, J.; Dominguez, F.; Vega, F.
Glyceraldehyde-3-phosphate dehydrogenase exerts different biologic activities in apoptotic and proliferating hepatocytes according to its subcellular localization
Mol. Cell. Biochem.
300
19-28
2007
Rattus norvegicus
Blatnik, M.; Thorpe, S.R.; Baynes, J.W.
Succination of proteins by fumarate: mechanism of inactivation of glyceraldehyde-3-phosphate dehydrogenase in diabetes
Ann. N. Y. Acad. Sci.
1126
272-275
2008
Rattus norvegicus
Park, J.; Han, D.; Kim, K.; Kang, Y.; Kim, Y.
O-GlcNAcylation disrupts glyceraldehyde-3-phosphate dehydrogenase homo-tetramer formation and mediates its nuclear translocation
Biochim. Biophys. Acta
1794
254-262
2009
Rattus norvegicus (P04797)
Frayne, J.; Taylor, A.; Cameron, G.; Hadfield, A.T.
Structure of insoluble rat sperm glyceraldehyde-3-phosphate dehydrogenase (GAPDH) via heterotetramer formation with Escherichia coli GAPDH reveals target for contraceptive design
J. Biol. Chem.
284
22703-22712
2009
Escherichia coli (P0A9B2), Escherichia coli, Rattus norvegicus (Q9ESV6)
Qvit, N.; Joshi, A.U.; Cunningham, A.D.; Ferreira, J.C.; Mochly-Rosen, D.
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) protein-protein interaction inhibitor reveals a non-catalytic role for GAPDH oligomerization in cell death
J. Biol. Chem.
291
13608-13621
2016
Anolis carolinensis (H9GBL1), Gallus gallus (P00356), Homo sapiens (P04406), Rattus norvegicus (P04797), Mus musculus (P16858), Danio rerio (Q6NYI5), Rattus norvegicus Wistar (P04797)
EXTERNAL LINKS (specific for EC-Number 1.2.1.12)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
