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Information on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and Organism(s) Homo sapiens
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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.
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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: Homo sapiens
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
-
-
-
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CP 17/CP 18
-
-
-
-
D-glyceraldehyde-3-phosphate dehydrogenase
dehydrogenase, glyceraldehyde phosphate
-
-
-
-
dihydrogenase, glyceraldehyde phosphate
-
-
-
-
G3PD
GAPD
GAPDH
GAPDH1
-
-
-
-
GAPDH2
-
-
-
-
GAPDS
glyceraldehyde 3-phosphate dehydrogenase
glyceraldehyde phosphate dehydrogenase (NAD)
-
-
-
-
glyceraldehyde-3-P-dehydrogenase
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-
-
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glyceraldehyde-3-phosphate dehydrogenase
glyceraldehyde-3-phosphate dehydrogenase (NAD)
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-
-
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GPD
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-
-
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Gra3PDH
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-
-
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GraP-DH
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-
-
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Larval antigen OVB95
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-
-
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Major larval surface antigen
-
-
-
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NAD+-G-3-P dehydrogenase
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-
-
-
NAD-dependent glyceraldehyde phosphate dehydrogenase
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-
-
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NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
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-
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NAD-G3PDH
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-
-
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NADH-glyceraldehyde phosphate dehydrogenase
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-
-
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P-37
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-
-
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phosphoglyceraldehyde dehydrogenase
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-
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Plasmin receptor
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-
-
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Plasminogen-binding protein
-
-
-
-
sperm-specific glyceraldehyde-3-phosphate dehydrogenase
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TLAb
-
-
-
-
triose phosphate dehydrogenase
-
-
-
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G3PD
-
-
-
-
GAPDH
-
-
-
-
GAPDH
-
-
GAPDH
-
glyceraldehyde-3-phosphate dehydrogenase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+
ordered ter bi mechanism characterized by the sequential addition of NAD+, glyceraldehyde 3-phosphate and phosphate to the enzyme and the sequential release of 3-phospho-D-glyceroyl phosphate and NADH from the enzyme
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
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
acetaldehyde + phosphate + NAD+
acetyl phosphate + NADH
-
enzyme form E6.6 shows 27% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E6.8 shows 9% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 6% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.4% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
butyraldehyde + phosphate + NAD+
butyryl phosphate + NADH
-
enzyme form E6.6 shows 10% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E6.8 shows 15% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 12% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.9% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
DL-glyceraldehyde + phosphate + NAD+
D-glyceroyl phosphate + NADH
-
enzyme form E6.6 shows no activity, enzyme form E6.8 shows 2.5% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 30% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 3.0% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
erythrose 4-phosphate + phosphate + NAD+
? + NADH
-
enzyme form E6.6 shows no activity, enzyme form E6.8 shows 1.2% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 25% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 1.5% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
glucose + phosphate + NAD+
? + NADH
-
enzyme form E6.6 shows no activity, enzyme form E6.8 shows 0.6% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 6.0% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.8% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
propionaldehyde + phosphate + NAD+
propionyl phosphate + NADH
-
enzyme form E6.6 shows 33% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E6.8 shows 12% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 10% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.8% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
valeraldehyde + phosphate + NAD+
pentanoyl phosphate + NADH
-
enzyme form E6.6 shows no activity, enzyme form E6.8 shows 19% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 18% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.9% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
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
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
glycolytic enzyme
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
absolute specificity for NAD+
-
-
?
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+
-
-
-
-
r
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+
-
-
-
?
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+
-
-
-
?
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+
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
r
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+
-
-
-
r
additional information
?
-
-
enzyme is regulated by ATP and by D-glyceraldehyde 3-phosphate
-
-
?
additional information
?
-
-
classical glycolytic protein involved exclusively in cytosolic energy production
-
-
?
additional information
?
-
-
hypoxia upregulates the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase in endothelial cells through a 5'-hypoxic regulatory element. Cell-specific patterns of HIF-1alpha and HIF-2alpha expression lead to cell-specific gene upregulation during hypoxia
-
-
?
additional information
?
-
GAPDH interacts with DNA damages, such as uracil
-
-
?
additional information
?
-
the enzyme interacts directly with the D-serine synthetic enzyme serine racemase, SRR. Glyceraldehyde-3-phosphate (G3P) augments the SRR-GAPDH interaction in a dose-dependent manner, whereas NAD+ and its reduced form, NADH, inhibit the interaction
-
-
?
additional information
?
-
-
GAPDH directly binds to cyclic adenosine diphosphoribose (cADPR), molecule docking and molecular dynamic simulations, overview. Arg234 and His179 in GAPDH might be the potential binding sites for cADPR
-
-
?
additional information
?
-
interaction analysis of the purified enzyme with oligodeoxyribonucleotides, poly(dA-dU) and poly(dA-dT) substrate synthesis, overview. GAPDH, like DNA glycosylases/AP lyases, is able to cleave DNA and to remain bound with the 5'-terminal product of beta-elimination via the Schiff base-dependent bonding. But unlike DNA glycosylases/AP lyases, GAPDH forms considerably more stable complexes with the product of beta-elimination that potentially can make it inefficient as an AP lyase. Lack of the UDG activity in classical GAPDH. Disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA
-
-
?
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
-
glycolytic enzyme
-
-
?
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+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
r
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+
-
-
-
?
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+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
r
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+
-
-
-
r
additional information
?
-
-
enzyme is regulated by ATP and by D-glyceraldehyde 3-phosphate
-
-
?
additional information
?
-
-
classical glycolytic protein involved exclusively in cytosolic energy production
-
-
?
additional information
?
-
-
hypoxia upregulates the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase in endothelial cells through a 5'-hypoxic regulatory element. Cell-specific patterns of HIF-1alpha and HIF-2alpha expression lead to cell-specific gene upregulation during hypoxia
-
-
?
additional information
?
-
GAPDH interacts with DNA damages, such as uracil
-
-
?
additional information
?
-
the enzyme interacts directly with the D-serine synthetic enzyme serine racemase, SRR. Glyceraldehyde-3-phosphate (G3P) augments the SRR-GAPDH interaction in a dose-dependent manner, whereas NAD+ and its reduced form, NADH, inhibit the interaction
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
-
287900, 287910, 287913, 287925, 287932, 287945, 287967, 684120, 684972, 685025, 685292, 686080, 688250, 688661, 712640, 725592, 741870, 742751
NAD+
monomer interactions with all three neighbor subunits are essential for maintaining the cooperativity of NAD+ binding exhibited by GAPD, NAD+ binding analysis, kinetics, overview
NAD+
NAD+ binding analysis with truncated and mutant enzymes, kinetics, overview. The enzyme exhibits positive cooperativity with the saturation being reached at the NAD+/protein concentration ratio of about 20. The E96Q and E244Q substitutions do not alter the NAD+-binding behavior of dN-GAPDS significantly. The mutant proteins exhibit a well-pronounced positive cooperativity in coenzyme binding, while mutant dN-GAPDS D311N binds NAD+ noncooperatively
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn
-
enzyme form E8.5 contains 0.64 gatoms of zinc per mol of enzyme, enzyme form E9.0 contain 2.76 gatom of zinc per mol of enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetylleucine chloromethyl ketone
-
binds to GAPDH to modulate the conformation of the enzyme, the modified enzyme is susceptible to chymotrypsin-like protease activity, cleavage at TRp195-Arg196; irreversible inhibition, enzyme modified by acetylleucine chloromethyl ketone is deduced to be digested at the peptide bond Trp196-Arg196
CGP-3466
-
deprenyl-related compound that inhibits the pro-apoptotic activity of GAPDH
demethylasterriquinone B1
-
binding of demethylasterriquinone B1 toGAPDH could disrupt phosphatase acting upon phosphatidylinositol lipids and thereby potentiate insulin signaling via the phosphatidylinositol-3-kinase pathway
diepoxybutane
-
incubation of GAPDH with bis-electrophiles results in inhibition of its catalytic activity, but only at high concentrations of diepoxybutane
ferriprotoporphyrin IX
-
enzyme is partially inactivated through oxidation of critical thiols
FK506-binding protein 36
-
i.e. FKBP36. The interaction between FKBP36 and GAPDH directly inhibits the catalytic activity of GAPDH. FKBP36 expression causes a significant reduction of the GAPDH level and activity in COS-7 cells. GAPDH is depleted by FKBP36 expression, particularly in the cytosolic fraction
-
guanidine hydrochloride
unfolding of both wild type and mutant dN-GAPDS proteins is described by a single [GdnHCl]50 value. For the truncated mutant dN-GAPDS, it constitutes 1.83 M. Different mutations of dN-GAPDS alter this parameter to various extents. The most pronounced effect is observed in the case of mutants P111A, P157A, and D311N. The mutation P111A increases the value of [GdnHCl]50 by 0.43 M, the mutations P157A and D311N decrease the GdnHCl50 value by 0.36 and 0.48 M, respectively. In other mutants, the [GdnHCl]50 value is less affected or does not change, overview; unfolding of muscle isoenzyme GAPD is a two step process
Koningic acid
-
inhibits arsenate reductase activity and activity with D-glyceraldehyde 3-phosphate, phosphate and NAD+
N-acetylcysteine
-
5 mM N-acetylcysteine significantly reduces G3PD activation induced by both H2O2 and ferric protoporphyrin IX
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
-
T0501_7749
2-[2-amino-3-(4-methylphenyl)sulfonylpyrrolo[3,2-b]quinoxalin-1-yl]-1-(4-nitrophenyl)ethanol, a small-molecule, highly selective isozyme GAPDHS inhibitor, molecular docking simulations in GAPDHS and GAPDH isozymes, binding structure, overview; 2-[2-amino-3-(4-methylphenyl)sulfonylpyrrolo[3,2-b]quinoxalin-1-yl]-1-(4-nitrophenyl)ethanol, identification of a small-molecule GAPDHS inhibitor with micromolar potency and high selectivity that exerts the expected inhibitory effects on sperm glycolysis and motility. The compound causes significant reductions in the percentage of motile human sperm. Molecular docking simulations in GAPDHS and GAPDH isozymes, binding structure, overview
T0506_9350
1-cyclohexyl-3-[4-[(4-methoxyphenyl)sulfamoyl]-2-nitroanilino]urea, a partial selective isozyme GAPDH inhibitor, binding structure, overview; 1-cyclohexyl-3-[4-[(4-methoxyphenyl)sulfamoyl]-2-nitroanilino]urea, a partial selective isozyme GAPDH inhibitor, binding structure, overview. T0506_9350 inhibition of human and mouse tGAPDHS is competitive with both D-glyceraldehyde 3-phosphate and NAD+
tris(2-carboxyethyl)phosphine
a reducing agent to break the disulfide bonds, inhibits formation of the GAPDH-AP DNA-borohydride-independent adduct
tubulin
-
GAPDH catalytic activity is inhibited upon formation of a complex with tubulin
-
ATP
-
inhibition is less pronounced for enzyme from sarcoma tissue as compared to normal muscle tissue
D-glyceraldehyde 3-phosphate
2-mercaptoethanol protects against the inhibition
NADH
2-mercaptoethanol protects against the inhibition, but the inhibitory effect of NADH is not influenced by heavy metal ions or EDTA
additional information
-
stauroporine does not inhibit stimulation of G3PD activity
-
additional information
-
not inhibited by DMSO, dibromomethane and 1,2-dibromoethane
-
additional information
-
anti-GAPDH immunoglobulin G in the cerebrospinal fluid of patients with multiple sclerosis inhibits GAPDH glycolytic activity (38% or 58% inhibition after incubation of GAPDH with 0.002 or 0.004 mg, respectively)
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
doxorubicin
-
treatment results in increased nuclear localization of expressed wild-type GAPDH, where it protects telomeres against rapid degradation, concomitant with increased resistance to the growth-inhibitory effects of the drug
Ferric protoporphyrin IX
-
145% increase of activity at 0.04 mM ferric protoporphyrin IX after 30 min exposure to stauroporin
gemcitabine
-
treatment results in increased nuclear localization of expressed wild-type GAPDH, where it protects telomeres against rapid degradation, concomitant with increased resistance to the growth-inhibitory effects of the drug
H2O2
-
subapoptotic doses lead to strong hyperactivation, related to mild oxidative stress. U937 cells hyperactivate glyceraldehyde 3-phosphate dehydrogenase with the same timing observed for glyceraldehyde 3-phosphate dehydrogenase alterations from apoptogenic doses of H2O2
additional information
GAPDH functions as a coactivator with high selectivity for androgen receptor and enhances androgen receptor transactivation independent of its glycolytic activity
-
additional information
-
human TATA-binding protein-associated factor II 68-TEC fusion protein-dependent transcription is enhanced by GAPDH
-
additional information
20% increase of GADPH expression 3 h post concentric exercise
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00046
D-glyceraldehyde 3-phosphate
N-terminally truncated mutant, pH 8.5, 25°C
0.097
D-glyceraldehyde 3-phosphate
recombinant dN-GAPDS enzyme, pH 8.9, 20°C
0.149
D-glyceraldehyde 3-phosphate
-
pH 7.3, enzyme isolated of healthy patients
0.159
D-glyceraldehyde 3-phosphate
-
pH 8.0, enzyme isolated of healthy patients
0.24
D-glyceraldehyde 3-phosphate
recombinant dN-GAPDS enzyme mutant D311N, pH 8.9, 20°C
0.25
D-glyceraldehyde 3-phosphate
glyceraldehyde-3-phosphate dehydrogenase, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
0.27
D-glyceraldehyde 3-phosphate
recombinant wild-type enzyme, pH 8.9, 20°C
0.46
D-glyceraldehyde 3-phosphate
recombinant, highly soluble form of sperm-specific glyceraldehyde-3-phosphate dehydrogenase truncated at the N-terminus, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
0.77
D-glyceraldehyde 3-phosphate
in 50 mM glycine, 50 mM potassium phosphate, 5 mM EDTA, pH 9.0
3.7
D-glyceraldehyde 3-phosphate
-
immobilized enzyme reactor, at pH 8.6 and 25°C
3.7
D-glyceraldehyde 3-phosphate
-
enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
0.022
NAD+
in 50 mM glycine, 50 mM potassium phosphate, 5 mM EDTA, pH 9.0
0.75
NAD+
-
enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
35
NAD+
recombinant, highly soluble form of sperm-specific glyceraldehyde-3-phosphate dehydrogenase truncated at the N-terminus, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
100
NAD+
glyceraldehyde-3-phosphate dehydrogenase, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
additional information
additional information
the sperm-specific isoenzyme of glyceraldehyde-3-phosphate dehydrogenase exhibits strong positive cooperativity in coenzyme binding, kinetics, overview
-
additional information
additional information
the sperm-specific isoenzyme of glyceraldehyde-3-phosphate dehydrogenase exhibits strong positive cooperativity in coenzyme binding, kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
199
D-glyceraldehyde 3-phosphate
glyceraldehyde-3-phosphate dehydrogenase, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
234
D-glyceraldehyde 3-phosphate
recombinant, highly soluble form of sperm-specific glyceraldehyde-3-phosphate dehydrogenase truncated at the N-terminus, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0602
T0506_9350
versus NAD+, pH and temperature not specified in the publication
0.0633
T0506_9350
versus D-glyceraldehyde 3-phosphate, pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
T0501_7749
Homo sapiens
pH and temperature not specified in the publication
0.0385
T0501_7749
Homo sapiens
pH and temperature not specified in the publication
0.0958
T0506_9350
Homo sapiens
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
46
purified recombinant truncated enzyme mutant dN-GAPDS P213A, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
47
50
purified recombinant truncated enzyme mutant dN-GAPDS P157A, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
60
64
92
95
45
purified recombinant truncated enzyme mutant dN-GAPDS, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
45
purified recombinant truncated enzyme mutant dN-GAPDS, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
47
purified recombinant truncated enzyme mutant dN-GAPDS P111A, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
47
purified recombinant truncated enzyme mutant dN-GAPDS P164A, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
47
purified recombinant truncated enzyme mutant dN-GAPDS P326A, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
60
purified recombinant truncated enzyme mutant dN-GAPDS E244Q, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
60
purified recombinant truncated enzyme mutant dN-GAPDS E244Q, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
64
purified recombinant truncated enzyme mutant dN-GAPDS E96Q, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
64
purified recombinant truncated enzyme mutant dN-GAPDS E96Q, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
64
purified recombinant truncated enzyme mutant dN-GAPDS P197A, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
92
purified recombinant truncated enzyme mutant dN-GAPDS D311N, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
92
purified recombinant truncated enzyme mutant dN-GAPDS D311N, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
95
purified recombinant wild-type enzyme, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
95
purified recombinant wild-type enzyme, pH 8.9, 20°C, oxidation of D-glyceraldehyde 3-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
enzyme form E6.8, two pH optima: pH 7.0 and pH 8.5, with activity between pH 7.5 and pH 8.0 being rather low
8 - 8.3
8.5
8.9
8.5
-
enzyme form E6.8, two pH optima: pH 7.0 and pH 8.5, with activity between pH 7.5 and pH 8.0 being rather low
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.8
-
above, sharp decline in activity for enzyme of patients with chronic myeloid leukemia, no similar sharp decline for enzyme of healthy subjects
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
25
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
-
in both fetal and senior cells, considerable GAPDH is present in intracellular domains characterized by significantly reduced catalysis. Human cells contain significant intracellular levels of enzymatically inactive GAPDH which is age-independent
a multimeric high-molecular-weight glyceraldehyde-3-phosphate dehydrogenase, the isozyme is secreted. Low levels of non-serum-specific isozyme GAPDH. The serum-specific high-molecular weight isozyme is also secreted from cancer cells
GAPDHS displays significantly higher expression in uveal melanoma (UM) than in normal controls
additional information
-
expressing Bcl-2, overproduction of the Bcl-2 protein does not change the non-native GAPDH localization in the growing HeLa-Bcl-2 cells
immunodetection of GAPDH and its adducts with apurinic/apyrimidinic DNA in cell extracts
-
staining of HeLa cells with mAbs 6C5 reveals the predominant accumulation of the non-native forms of GAPDH, i.e. dimers, monomers, the denatured forms of GAPDH, in the nucleus during normal growth
GAPDS exists in sperms bound to the fibrous sheath of the flagellum
ejaculated sperm cells, localization of the GAPDHS protein in the sperm head, immunologic analysis, in the principal piece and acrosomal part of the sperm cells, overview
sperm-specific glyceraldehyde 3-phosphate dehydrogenase, restricted enzyme expression during spermatogenesis
additional information
astrocytes express SRR in the subiculum of human hippocampal formation
additional information
sperm-specific enzyme GAPDHS is highly expressed in melanoma cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
specific interaction of actin with non-native GAPDH, i.e. dimers, monomers, the denatured forms of GAPDH
extracellular GAPDH in human serum is a multimeric, high-molecular-weight, yet glycolytically active enzyme. The enzyme is secreted
-
GAPDS is an insoluble protein that is attached to the cytoskeleton of the sperm flagellum via the N-terminus
-
additional information
-
predominantly cytoplasmic localization of tetrameric native form GAPDH within HeLa cells
protein complex containing GAPDH and androgen receptor in the cytosol
-
GAPDH colocalizes with viral RNA-dependentRNA polymerase in cells infected with Japanese encephalitis virus. GAPDH remains relatively constant in the cytosol, while increasing at 12 to 24 hours postinfection and decreasing at 36 hours postinfection in the nuclear fraction of infected cells. There is no direct protein-protein interaction; instead, GAPDH binds to the 3' termini of plus- and minus-strand RNAs of Japanese encephalitis virus. GAPDH binds to the minus-strand more efficiently than to the plus-strand of Japanese encephalitis virus RNAs
protein complex containing GAPDH and androgen receptor in the nucleus
-
GAPDH colocalizes with viral RNA-dependentRNA polymerase in cells infected with Japanese encephalitis virus. GAPDH remains relatively constant in the cytosol, while increasing at 12 to 24 hours postinfection and decreasing at 36 hours postinfection in the nuclear fraction of infected cells. There is no direct protein-protein interaction; instead, GAPDH binds to the 3' termini of plus- and minus-strand RNAs of Japanese encephalitis virus. GAPDH binds to the minus-strand more efficiently than to the plus-strand of Japanese encephalitis virus RNAs
isozyme uracil-DNA glycosylase localizes in the nucleus as a monomer, UDG, or a dimer (RNA-binding form), but not in the native tetrameric form
additional information
-
the subcellular localization of enzyme form E6.6 is uncertain
-
additional information
-
immunohistochemic analysis of subcellular enzyme localization
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
both GAPDS and GAPD are homotetramers with the sequence identity of about 70%. They are encoded by different genes which have emerged after duplication of the original gene during the early evolution of chordates
evolution
both GAPDS and GAPD are homotetramers with the sequence identity of about 70%. They are encoded by different genes which have emerged after duplication of the original gene during the early evolution of chordates. The GAPDS gene is lost by most lineages, and specialized to a testis-specific protein in reptilians and mammals
evolution
cellular glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a phylogenetically conserved, ubiquitous enzyme
evolution
the sequence of the isozyme uracil-DNA glycosylase, UDG polypeptide (331 amino acids), differs from the sequence of classical GAPDH (335 amino acids) by the substitution of the residues 194-213 and the deletion of the residues 328-330. The amino acid sequence of the GAPDH isoform UDG because of its activity is hardly connected with alternative splicing of GAPDH pre-mRNA. The UDG region with the altered amino acids 194-213 is situated within the exon far from its boundaries. It appears to be a result of the single-nucleotide deletion in the GAPDH gene exon, causing the shift of the reading frame. Downstream to this region, there is theadditional deletion of 2 nucleotides in the UDG sequence, leading to restoration of the initial reading frame. The observed discrepancies in the sequences of these proteins are likely due to a sequencing error. Interestingly, the altered region belongs to the GAPDH glyceraldehyde-3-phosphate-binding site not participating in DNA binding
malfunction
-
GAPDH knockdown abolishes cADPR-induced Ca2+ release. GAPDH knockdown markedly inhibits NPE-cADPR- or PALcIDPRE-induced cytosolic Ca2+ increase in Jurkat cells, RyR3-expressing HEK-293 cells, or human coronary artery smooth muscle cells. Washing saponin-treated cells with PBS abolishes cADPR-induced colocalization of GAPDH with ryanodine receptors, RyRs
malfunction
GAPDHS inhibitor effects on sperm motility and metabolism, overview
malfunction
knockdown of GAPDHS in uveal melanoma (UM) cell lines hinders glycolysis by decreasing glucose uptake, lactate production, ATP generation, cell growth and proliferation. Conversely, overexpression of GAPDHS promotes glycolysis, cell growth and proliferation. Transcription factor SOX10 knockdown reduces the activation of GAPDHS, leading to an attenuated malignant phenotype, and SOX10 overexpression promotes the activation of GAPDHS, leading to an enhanced malignant phenotype. Mechanistically, SOX10 exerts its function by binding to the promoter of GAPDHS to regulate its expression. Importantly, SOX10 abrogation suppresses in vivo tumor growth and proliferation
metabolism
GAPDH not only catalyses the sixth step of glycolysis, but is also implicated in multiple nonmetabolic processes. Glycolytic flux controls D-serine synthesis through glyceraldehyde-3-phosphate dehydrogenase in astrocytes. Astrocytic energy metabolism controls D-serine production, thereby influencing glutamatergic neurotransmission in the hippocampus, overview. Involvement of glycolysis in modulating D-serine levels
metabolism
the enzyme is involved in glycolysis, the glycolytic conversion of glucose to pyruvic acid
physiological function
-
downregulation of GAPDH using siRNA reduces both macrophage colony stimulating factor CSF-1 mRNA and protein levels, through destabilizing CSF-1 mRNA. CSF-1 mRNA half-lives are decreased by 50% in the presence of GAPDH siRNA. GAPDH associates with a large AU-rich containing regionof CSF-1
physiological function
-
GAPDH is a translational suppressor of angiotensin II type 1 receptor expression and mediates the effect of H2O2 on angiotensin II type 1 receptor mRNA
physiological function
GAPDH physically associates with DNA repair enzyme APE1. This interaction allows GAPDH to convert the oxidized species of APE1 to the reduced form, thereby reactivating its endonuclease activity to cleave abasic sites
physiological function
apurinic/apyrimidinic (AP) sites are some of the most frequent DNA damages and the key intermediates of base excision repair. Certain proteins can interact with the deoxyribose of the AP site to form a Schiff base, which can be stabilized by NaBH4 treatment. The enzyme interacts with single-stranded AP DNA and AP DNA duplex with both 5' and 3' dangling ends. The protein forming this adduct is an isoform of glyceraldehyde-3-phosphate dehydrogenase called uracil-DNA glycosylase. GAPDH, at least partially, is covalently linked with the AP site by a mechanism other than the Schiff base formation. In spite of the ability to form a Schiff-base intermediate with the deoxyribose of the AP site, GAPDH does not display the AP lyase activity. In addition, along with the borohydride-dependent adducts with AP DNAs containing single-stranded regions, GAPDH was also shown to form the stable borohydride-independent crosslinks with these AP DNAs. GAPDH crosslinks preferentially to AP DNAs cleaves via the beta-elimination mechanism (spontaneously or by AP lyases) as compared to DNAs containing the intact AP site. The level of GAPDH-AP DNA adduct formation depends on oxidation of the protein SH-groups. Disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA
physiological function
cellular glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a phylogenetically conserved, ubiquitous enzyme that plays an indispensable role in energy metabolism. The extracellular GAPDH in human serum is a multimeric, high-molecular-weight, yet glycolytically active enzyme, the enzymatic function of serum GAPDH remained unaffected by the multimers
physiological function
-
GAPDH plays essential role in glycolysis and gluconeogenesis as a housekeeping enzyme. Cyclic adenosine diphosphoribose (cADPR), an endogenous nucleotide derived from NAD+, mobilizes Ca2+ release from endoplasmic reticulum via ryanodine receptors (RyRs). cADPR interacts directly with enzyme GAPDH and induces the transient interaction between GAPDH and RyRs in vivo, without cADPR the interaction is weak. GAPDH is required for cADPR-mediated Ca2+ mobilization from endoplasmic reticulum via RyRs. cADPR-mediated Ca2+ signaling pathway is involved in a wide variety of cellular processes,1 e.g. abscisic acid signaling, calorie restriction in gut stem cell, circadian clock in plants, and long-term synaptic depression in hippocampus
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
physiological function
glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, GAPDHS, is a sperm-specific glycolytic enzyme involved in energy production during spermatogenesis and sperm motility
physiological function
glycolytic flux controls D-serine synthesis through glyceraldehyde-3-phosphate dehydrogenase in astrocytes. D-Serine production in astrocytes is modulated by the interaction between the D-serine synthetic enzyme serine racemase (SRR) and a glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPDH). In primary cultured astrocytes, glycolysis activity is negatively correlated with D-serine level. SRR interacts directly with GAPDH, and activation of glycolysis augments this interaction. GAPDH suppresses SRR activity by direct binding to GAPDH and through NADH, a product of GAPDH. NADH allosterically inhibits the activity of SRR by promoting the disassociation of ATP from SRR
physiological function
the C-terminal domain of human host cell glyceraldehyde 3-phosphate dehydrogenase plays an important role in suppression of tRNALys3 packaging into human immunodeficiency virus type-1 particles. Human immunodeficiency virus type-1 (HIV-1) requires the packaging of human tRNALys3 as a primer for effective viral reverse transcription. The binding of human GAPDH to Pr55gag is important for the suppression mechanism, and residues Asp256, Lys260, Lys263 and Glu267 of GAPDH are essential for the suppression of tRNALys3 packaging. The C-terminal domain of GAPDH (151-335) interacts with both the matrix region (MA, 1-132) and capsid N-terminal domain (CANTD, 133-282)
physiological function
the enzyme is involved in glycolysis, the pathway plays an important role in tumor cells
physiological function
-
the significance of D-glyceraldehyde-3-phosphate dehydrogenase is not restricted to its pivotal glycolytic function. GAPDH localized in the nucleus can be involved in numerous processes: regulation of the length of telomeres, DNA repair, gene expression, and regulation of cyclin functions. GAPDH may act as a specific scaffold for cytoskeleton-associated proteins independently of its catalytic activity
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme, whose main role is to provide energy for different cellular functions. Also the enzyme appears to be involved in numerous cell processes that have no relation to glycolysis
physiological function
sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDHS) switches glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate by coupling with the reduction of NAD+ to NADH. The sperm-specific glycolysis enzyme is regulated by transcription factor SOX10 to promote uveal melanoma (UM) tumorigenesis. GAPDHS, which is regulated by SOX10, controls glycolysis and contributes to UM tumorigenesis. GAPDHS is involved in regulating the Warburg effect in UM cells. GAPDHS serves as a functional target gene in SOX10-mediated tumor proliferation and glycolysis in UM
additional information
comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
-
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
-
possible existence of actin/active GAPDH dimer complexes similar to 3-phosphoglycerate kinase/active GAPDH dimer complexes
additional information
sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS, is stabilized by additional proline residues and an interdomain salt bridge. Residues P164, P326, and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at expense of the catalytic activity. Comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS, is stabilized by additional proline residues and an interdomain salt bridge. Residues P164, P326, and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at expense of the catalytic activity. Comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
the enzyme's catalytic domain interrupts interacting sites in the NAD+-binding domain of GAPDH
additional information
denatured GAPDH, in contrast to the native enzyme, interacts with the bacterial chaperonin GroEL and beta-amyloid peptide 1-42
additional information
-
denatured GAPDH, in contrast to the native enzyme, interacts with the bacterial chaperonin GroEL and beta-amyloid peptide 1-42
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). G3P_HUMAN
335
0
36053
Swiss-Prot
Mitochondrion (Reliability: 3)
G3PT_HUMAN
408
0
44501
Swiss-Prot
other Location (Reliability: 4)
Q2TSD0_HUMAN
335
0
36049
TrEMBL
Mitochondrion (Reliability: 3)
Q16768_HUMAN
44
0
4894
TrEMBL
other Location (Reliability: 1)
V9HVZ4_HUMAN
335
0
36053
TrEMBL
Mitochondrion (Reliability: 3)
A0A0K0K1K1_HUMAN
408
0
44501
TrEMBL
other Location (Reliability: 4)
Q5ZEY4_HUMAN
83
0
8891
TrEMBL
other Location (Reliability: 2)
Q5ZEY3_HUMAN
86
0
9201
TrEMBL
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
142000
150000
36000
38000
40000
58000
150000
N-terminally truncated enzyme after trypsin-treatment, Blue Native PAGE
40000
4 * 40000, N-terminally truncated enzyme after trypsin treatment, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
monomer
tetramer
additional information
?
x * 35470, apo-form of GADPH isozyme uracil-DNA glycosylase, mass spectrometry
?
x * 75000, about, recombinant enzyme, SDS-PAGE, x * 45000-50000, native enzyme, SDS-PAGE
homotetramer
4 * 40000, N-terminally truncated enzyme after trypsin treatment, SDS-PAGE
monomer
1 * 45000, SDS-PAGE, isozyme uracil-DNA glycosylase, enzyme as adduct with AP DNA
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
additional information
-
recombinant GAPDH binds directly with high affinity to a single-stranded oligonucleotide comprising three telomeric DNA repeats. Nucleotides T1, G5, and G6 of the TTAGGG repeat are essential for binding.The stoichiometry of the interaction is 2:1 DNA:GAPDH, and GAPDH appears to form a high-molecular-weight complex when bound to the oligonucleotide
additional information
-
recombinant glyceraldehyde 3-phosphate dehydrogenase binds to hepatitis B virus regulatory element RNA in vitro and inhibits hepatitis B virus regulatory element function. Overexpression of glyceraldehyde 3-phosphate dehydrogenase depresses the expression of hepatitis B virus antigen
additional information
GAPDH is composed of two folding domains, an NAD+-binding domain (residues 2-150) and a catalytic domain (residues 155-312)
additional information
high-molecular-weight multimers of serum GAPDH, multiple protein bands (about 25, and 50-75 kDa) along with some proteins with weak signals in albumin-depleted serum samples, SDS-PAGE and mass spectrometry. The enzymatic function of serum GAPDH remained unaffected by the multimers
additional information
the residues P164 (beta-turn), P326 (first position of alpha-helix), and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at the expense of the catalytic activity. The N-terminal domain is hidden inside the cytoskeleton structures and does not interact with the catalytic part of the enzyme
additional information
the residues P164 (beta-turn), P326 (first position of alpha-helix), and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at the expense of the catalytic activity. The N-terminal domain is hidden inside the cytoskeleton structures and does not interact with the catalytic part of the enzyme
additional information
three GAPDS-specific salt bridges, E96-H394 and D311-H124 connect the NAD+-binding and the catalytic domains within a single subunit, while E244-R320 is formed between two different subunits
additional information
three GAPDS-specific salt bridges, E96-H394 and D311-H124 connect the NAD+-binding and the catalytic domains within a single subunit, while E244-R320 is formed between two different subunits
additional information
human GAPDH identified by peptide mass fingerprinting and mass spectrometric analysis
additional information
-
human GAPDH identified by peptide mass fingerprinting and mass spectrometric analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
-
4-hydroxy-2-nonenal-modified GAPDH is degraded by cathepsin G
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of a a highly soluble form of GAPDS truncated at the N-terminus, amino acids 69398. The structure in complex with NAD+ and phosphate maps the two anion-recognition sites within the catalytic pocket that correspond to the conserved Ps site and Pi site identified in other organisms. The structure in complex with NAD+ and glycerol shows serendipitous binding of glycerol at the Ps and Pi sites
in complex with NAD+ and phosphate, hanging drop vapor diffusion method, using 20% (w/v) poly(ethylene glycol) 3350, 0.2 M sodium/potassium phosphate and 10% (v/v) ethylene glycol or in complex with NAD+ and glycerol, hanging drop vapor diffusion method, 20% PEG 3350, 0.2 M Na2SO4, 10% (v/v) ethylene glycol and 0.1 M Bis-Tris propane (pH 6.5)
purified recombinant apo-enzyme tGAPDHS, hanging-drop vapor-diffusion method, 10 mg/ml in 10 mM HEPES, pH 7.5, 500 mM NaCl, 5% glycerol, 0.5 mM TCEP, and 0.01% of sodium azide, is mixed in a 1:1 volume ratio with reservoir solution containing 0.2 M Na2SO4, 0.1 M Bis-Tris propane, pH 6.5, and 20% PEG 3350, 20°C, 2 days, crystallization of purified recombinant holoenzyme tGAPDHS in complex with NAD+, hanging-drop vapor-diffusion method, 10 mg/ml in 10 mM HEPES, pH 7.5, 500 mM NaCl, 5% glycerol, 0.5 mM TCEP, and 0.01% of sodium azide, is mixed in a 1:1 volume ratio with reservoir solution 0.2M NaNO3, and 20% PEG3350, 20°C, 2 days, X-ray diffraction structure determination and analysis at a.86 A (apoenzyme) and 1.73 A (holoenzyme) resolutions, method screening
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C149A
-
mutant has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition
C152G
mutant retains the ability to interact with but is unable to reactivate DNA repair enzyme APE1
C156G
mutant retains the ability to interact with but is unable to reactivate DNA repair enzyme APE1
D256R/K260E
site-directed mutagenesis, the double mutation of GAPDH results in loss of detectable binding activity to wild-type capsid N-terminal domain
D256R/K260E/K263E/E267R
site-directed mutagenesis, multiple-substituted GAPDH mutant D256R/K260E/K263E/E267R retains the oligomeric formation with wild-type GAPDH in HIV-1 producing cells, but the incorporation level of the hetero-oligomer is decreased in viral particles. The viruses produced from cells expressing the D256R/K260E/K263E/E267R mutant restores tRNALys3 packaging efficiency because the mutant exerts a dominant negative effect by preventing wild-type GAPDH from binding to matrix region and capsid N-terminal domain and improves the reverse transcription
D256R/K260E/Q264A
site-directed mutagenesis, the mutant lacks the ability to bind to the wild-type capsid N-terminal domain
D256R/K260E/Q264A/E267R
site-directed mutagenesis, the mutant lacks the binding ability to the wild-type capsid N-terminal domain
D311N
D32A
-
mutant is unable to bind NAD+, is enzymatically inactive and has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition
D356R
site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region
E244Q
E267R
site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region
E96Q
H179A
-
site-directed mutagenesis, the KD value of cADPR to GAPDHHis179Ala mutant protein is markedly increased compared to wild-type GAPDH enzyme
K263E
site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region
P111A
site-directed mutagenesis, mutation at first position of alpha-helix
P157A
site-directed mutagenesis, mutation at first position of alpha-helix
P164A
site-directed mutagenesis, mutation at beta-turn, the mutant shows reduced thermostability and reduced resistance against guanidine hydrochloride. The Tm value of the heat-absorption curve decreases by 3.3°C compared to the wild-type protein
P326A
site-directed mutagenesis, mutation at first position of alpha-helix, the mutant shows reduced thermostability and reduced resistance against guanidine hydrochloride. The Tm value of the heat-absorption curve decreases by 6.0°C compared to the wild-type protein
additional information
D311N
site-directed mutagenesis, the mutation breaks the salt bridge between the catalytic and NAD+-binding domains, mutant dN-GAPDS D311N binds NAD+ noncooperatively
D311N
site-directed mutagenesis, the mutation breaks the salt bridge between the catalytic and NAD+-binding domains, the inactivation rate constant in the presence of GdnHCl increases 6fold, and the value of GdnHCl concentration corresponding to the protein half-denaturation decreases from 1.83 to 1.35 M. The mutation D311N enhances the enzymatic activity of the protein 2fold
E244Q
site-directed mutagenesis, mutation at the interdomain salt bridge
E244Q
site-directed mutagenesis, mutation at the interdomain salt bridge, the E244Q substitution does not alter the NAD+-binding significantly. The mutant protein exhibits a well-pronounced positive cooperativity in coenzyme binding
E96Q
site-directed mutagenesis, mutation at the interdomain salt bridge
E96Q
site-directed mutagenesis, mutation at the interdomain salt bridge, the E96Q substitution does not alter the NAD+-binding significantly. The mutant protein exhibits a well-pronounced positive cooperativity in coenzyme binding
additional information
-
mutant htt shows co-localization of GAPDH with N-terminus of huntingtin aggregates
additional information
expression of a highly soluble form of GAPDS truncated at the N-terminus, amino acids 69398. Mutant displays a 3fold increase in catalytic efficiency and shows homotetrameric structure
additional information
-
expression of a highly soluble form of GAPDS truncated at the N-terminus, amino acids 69398. Mutant displays a 3fold increase in catalytic efficiency and shows homotetrameric structure
additional information
construction of a plasmid encoding truncated GAPDS lacking 68 N-terminal amino acids (dN-GAPDS)
additional information
construction of a plasmid encoding truncated GAPDS lacking 68 N-terminal amino acids (dN-GAPDS)
additional information
construction of a plasmid encoding truncated GAPDS lacking 68 N-terminal amino acids (dN-GAPDS). The recombinant GAPDS without the N-terminal sequence (dN-GAPDS) is soluble in contrast to the wild-type
additional information
construction of a plasmid encoding truncated GAPDS lacking 68 N-terminal amino acids (dN-GAPDS). The recombinant GAPDS without the N-terminal sequence (dN-GAPDS) is soluble in contrast to the wild-type
additional information
construction of three deletion mutants of GAPDH that lack different lengths in their C-terminal regions (GAPDH1-106, GAPDH1-176, and GAPDH1-230). Among these three mutants, GAPDH1-106 shows an affinity with SRR, whereas GAPDH1-176 and GAPDH1-230 do not, suggesting that the catalytic domain interrupts interacting sites in the NAD+-binding domain of GAPDH
additional information
viral mutations R58E, Q59A or Q63A in the matrix region, and E76R or R82E in the capsid N-terminal domain abrogate the interaction with the C-terminal domain of enzyme GAPDH. SAccharomyces cerevisiae two-hydrib interaction analysis between enzyme GAPDH wild-type and mutants with HIV-1 wild-type and mutant matrix region and capsid N-terminal domain, overview
additional information
knockdown of GAPDHS in uveal melanoma (UM) cell lines hinders glycolysis by decreasing glucose uptake, lactate production, ATP generation, cell growth and proliferation. Conversely, overexpression of GAPDHS promotes glycolysis, cell growth and proliferation. Transcription factor SOX10 knockdown reduces the activation of GAPDHS, leading to an attenuated malignant phenotype, and SOX10 overexpression promotes the activation of GAPDHS, leading to an enhanced malignant phenotype
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
acetylleucine chloromethyl ketone binds to GAPDH to modulate the conformation of the enzyme, the modified enzyme is susceptible to chymotrypsin-like protease activity, cleavage at TRp195-Arg196
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
after 6 months of storage, the specific activity of hGAPDH decreases to 10-15% of the original value due to the reversible oxidation of the enzyme. Reactivation of the enzyme by dissolving in 10 mM potassium phosphate, pH 7.4, and 5 mM DTT, to 1 mg/ml concentration, 2-4 h of incubation at 20-25°C, the specific activity of hGAPDH increases 5-7-fold. Alternatively, the enzyme can be dialyzed against required buffer solution containing 5 mM DTT
at -20°C storage after dialysis following the first (NH4)2SO4 fractionation step during purification, normal muscle and leukocyte enzyme is stable. Enzyme from chronic myeloid leukemia patients and sarcoma tissue loses about 80% of activity.
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography on a Hi-Trap chelating column charged with nickel sulfate, the His tag is cleaved and the enzyme is purified by an additional gel filtration step
DEAE-Sepharose column chromatography, ammonium sulfate precipitation, phenyl-Sepharose 6 column chromatography, and Superose 6 gel filtration
-
extracellular serum isozyme by immunoaffinity purification combined with anion exchange chromatography by using DEAE affigel blue chromatography
from normal leukocytes of healthy subjects, leukocytes of chronic myeloid leukemia patients and from sarcoma tissue
-
GST-fusion proteins are expressed in Escherichia coli and subsequently purified by absorption to glutathione-Sepharose beads, GST is seperated by digestion with thrombin protease
-
native enzyme from HeLa cells by ammonium sulfate fractionation followed by the heparin affinity chromatography, anion exchange chromatgraphy, and gel filtration
Ni-NTA agarose resin chromatography and Hi-Load 16/60 Superdex gel filtration
recombinant GST-tagged tGAPDHS from gapA-deficient Escherichia coli strain DS112 by glutathione affinity chromatography, and on-column cleavage of the GST-tag by bovine thrombin before elution of the enzyme
recombinant truncated mutant dN-GAPDS by cation exchange chromatography from Escherichia coli strain BL21(DE3). Recombinant enzyme mutants P197A and P164A by ammonium sulfate fractionation and dialysis, followed by anion exchange chromatography, the flow-through is further purified by hydrophobic interaction chromatography
recombinant untagged enzyme partially from Escherichia coli strain Rosetta 2 (DE3) by ammonium sulfate fractionation and precipitation in cyrstals, followed by desalting gel filtration, to homogeneity, method evaluation
recombinant wild-type and truncated mutant dN-GAPDS by cation exchange chromatography from Escherichia coli strain BL21(DE3), mutant dNGAPDS D311N by ammonium sulfate fractionation, and dialysis, followed by anion exchange chromatography, the flow-through is further purified by hydrophobic interaction chromatography
recombinant wild-type enzyme from Escherichia coli strain BL21(DE3)
red blood cell cytosol is prepared by hypotonic shock or freeze-thawing cycles, membranes are prepared by hypotonic lysis
-
recombinant wild-type enzyme from Escherichia coli strain BL21(DE3)
recombinant wild-type enzyme from Escherichia coli strain BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination of isozyme uracil-DNA glycosylase, UDG
expression in Escherichia coli
gene gapA, quantitative real-time PCR enzyme expression analysis, GAPDHS overexpression in melanoma cells (OCM1 cells), phenotype with and without SOX10 knockout, overview
recombinant enzyme expression of GST-tagged tGAPDHS (amino acids 76-408) in gapA-deficient Escherichia coli strain DS112
recombinant expression of mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain HB101
recombinant expression of untagged enzyme in Escherichia coli strain Rosetta 2 (DE3)
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain HB101
recombinant expression of wild-type enzyme in Escherichia coli strain BL21 (DE3), subcloning in Escherichia coli strain HB101
recombinant expression of wild-type enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain HB101
subcloned into a pET14b vector for expression in Escherichia coli BL21DE3 cells
-
subcloned into the pET15b vector for expression in Escherichia coli cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
24 h after irradiation at 5 gray, nuclear GAPDH levels increase 2.6fold, whereas total GAPDH increases only 1.2fold. Knockdown of GAPDH by siRNA leads to sensitization to X-ray-induced cell death
-
GAPDH-small interfering RNA knockdown sensitizes the cells to methyl methane sulfonate and bleomycin, which generate lesions that are repaired by APE1, but cells show normal sensitivity to 254-nm UV. GAPDH knockdown cells exhibit an increased level of spontaneous abasic sites in the genomic DNA as a result of diminished APE1 endonuclease activity
SOX10 modulates GAPDHS expression by binding to the promoter. Transcription factor SOX10 knockdown reduces the activation of GAPDHS, leading to an attenuated malignant phenotype, and SOX10 overexpression promotes the activation of GAPDHS, leading to an enhanced malignant phenotype
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
after 6 months of storage, the specific activity of hGAPDH decreases to 10-15% of the original value due to the reversible oxidation of the enzyme. Reactivation of the enzyme by dissolving in 10 mM potassium phosphate, pH 7.4, and 5 mM DTT, to 1 mg/ml concentration, 2-4 h of incubation at 20-25°C, the specific activity of hGAPDH increases 5-7-fold. Alternatively, the enzyme can be dialyzed against required buffer solution containing 5 mM DTT
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
medicine
functions are of chemotherapeutic interest, structure is a necessity for structure-based drug design
medicine
-
pathogenesis of Porphyromonas gingivalis involves interaction with oral mucosal epithelial cells, mediated by binding glyceraldehyde-3-phosphate dehydrogenase
medicine
-
among 256 ovarian and fallopian tube cancer specimens, GAPDH is regulated, with almost 50% of specimens having no GAPDH staining.Low GAPDH staining is associated with a low macrophage colony stimulating factor CSF-1 score
medicine
-
glyceraldehyde 3-phosphate dehydrogenase from malignant sources shows altered properties compared with enzyme from healthy subjects
medicine
-
glyceraldehyde 3-phosphate dehydrogenase may be involved in the postranscriptional regulation of hepatitis B virus. Recombinant glyceraldehyde 3-phosphate dehydrogenase binds to hepatitis B virus regulatory element RNA in vitro and inhibits hepatitis B virus regulatory element function. Overexpression of glyceraldehyde 3-phosphate dehydrogenase depresses the expression of hepatitis B virus antigen
medicine
GAPDHS, which is regulated by SOX10, controls glycolysis and contributes to uveal melanoma tumorigenesis, is a therapeutic target in cancer therapy
additional information
selective inhibition of GAPDHS, one of the glycolytic isozymes with restricted expression during spermatogenesis, is a potential strategy for the development of a non-hormonal contraceptive that directly blocks sperm function. Detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme can facilitate the identification of selective GAPDHS inhibitors for contraceptive development
additional information
selective inhibition of GAPDHS, one of the glycolytic isozymes with restricted expression during spermatogenesis, is a potential strategy for the development of a non-hormonal contraceptive that directly blocks sperm function. Detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme can facilitate the identification of selective GAPDHS inhibitors for contraceptive development
additional information
-
selective inhibition of GAPDHS, one of the glycolytic isozymes with restricted expression during spermatogenesis, is a potential strategy for the development of a non-hormonal contraceptive that directly blocks sperm function. Detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme can facilitate the identification of selective GAPDHS inhibitors for contraceptive development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lambeir, A.M.; Loiseau, A.M.; Kuntz, D.A.; Vellieux, F.M.; Michels, P.A.M.; Opperdoes, F.R.
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic properties and comparison with homologous enzymes
Eur. J. Biochem.
198
429-435
1991
Geobacillus stearothermophilus, Oryctolagus cuniculus, Homo sapiens, Trypanosoma brucei
Rogalski, A.A.; Steck, T.L.; Waseem, A.
Association of glyceraldehyde-3-phosphate dehydrogenase with the plasma membrane of the intact human red blood cell
J. Biol. Chem.
264
6438-6446
1989
Homo sapiens
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
Heinz, F.; Freimueller, B.
Glyceraldehyde-3-phosphate dehydrogenase from human tissues
Methods Enzymol.
89
301-305
1982
Homo sapiens
Wang, C.S.; Alaupovic, P.
Glyceraldehyde-3-phosphate dehydrogenase from human erythrocyte membranes. Kinetic mechanism and competitive substrate inhibition by glyceraldehyde 3-phosphate
Arch. Biochem. Biophys.
205
136-145
1980
Homo sapiens
Eby, D.; Kirtley, M.E.
Isolation and characterization of glyceraldehyde-3-phosphate dehydrogenase from human erythrocyte membranes
Arch. Biochem. Biophys.
198
608-613
1979
Homo sapiens
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
-
Mazzola, J.L.; Sirover, M.A.
Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function
Biochim. Biophys. Acta
1622
50-56
2003
Homo sapiens
Graven, K.K.; Bellur, D.; Klahn, B.D.; Lowrey, S.L.; Amberger, E.
HIF-2alpha regulates glyceraldehyde-3-phosphate dehydrogenase expression in endothelial cells
Biochim. Biophys. Acta
1626
10-18
2003
Homo sapiens
Yamaguchi, M.; Tsuchiya, Y.; Hishinuma, K.; Chikuma, T.; Hojo, H.
Conformational change of glyceraldehyde-3-phosphate dehydrogenase induced by acetylleucine chloromethyl ketone is followed by unique enzymatic degradation
Biol. Pharm. Bull.
26
1648-1651
2003
Homo sapiens
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
Ismail, S.A.; Park, H.W.
Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase
Acta Crystallogr. Sect. D
D61
1508-1513
2005
Homo sapiens (P04406), Homo sapiens
Jenkins, J.L.; Tanner, J.J.
High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase
Acta Crystallogr. Sect. D
D62
290-301
2006
Homo sapiens
Mazzola, J.L.; Sirover, M.A.
Aging of human glyceraldehyde-3-phosphate dehydrogenase is dependent on its subcellular localization
Biochim. Biophys. Acta
1722
168-174
2005
Homo sapiens
Omodeo Sale, F.; Vanzulli, E.; Caielli, S.; Taramelli, D.
Regulation of human erythrocyte glyceraldehyde-3-phosphate dehydrogenase by ferriprotoporphyrin IX
FEBS Lett.
579
5095-5099
2005
Homo sapiens
Sojar, H.T.; Genco, R.J.
Identification of glyceraldehyde-3-phosphate dehydrogenase of epithelial cells as a second molecule that binds to Porphyromonas gingivalis fimbriae
FEMS Immunol. Med. Microbiol.
45
25-30
2005
Oryctolagus cuniculus, Homo sapiens
Carujo, S.; Estanyol, J.M.; Ejarque, A.; Agell, N.; Bachs, O.; Pujol, M.J.
Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity
Oncogene
25
4033-4042
2006
Homo sapiens
Wu, J.; Lin, F.; Qin, Z.
Sequestration of glyceraldehyde-3-phosphate dehydrogenase to aggregates formed by mutant huntingtin
Acta Biochim. Biophys. Sin. (Shanghai)
39
885-890
2007
Homo sapiens
Kim, S.; Lee, J.; Kim, J.
Regulation of oncogenic transcription factor hTAF(II)68-TEC activity by human glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
Biochem. J.
404
197-206
2007
Homo sapiens
Omodeo-Sale, F.; Cortelezzi, L.; Riva, E.; Vanzulli, E.; Taramelli, D.
Modulation of glyceraldehyde 3 phosphate dehydrogenase activity and tyr-phosphorylation of Band 3 in human erythrocytes treated with ferriprotoporphyrin IX
Biochem. Pharmacol.
74
1383-1389
2007
Homo sapiens
Kuravsky, M.L.; Muronetz, V.I.
Somatic and sperm-specific isoenzymes of glyceraldehyde-3-phosphate dehydrogenase: comparative analysis of primary structures and functional features
Biochemistry
72
744-749
2007
Bos taurus, Canis lupus familiaris, Homo sapiens, Mus musculus, Oryctolagus cuniculus
Shchutskaya, Y.Y.; Elkina, Y.L.; Kuravsky, M.L.; Bragina, E.E.; Schmalhausen, E.V.
Investigation of glyceraldehyde-3-phosphate dehydrogenase from human sperms
Biochemistry
73
185-191
2008
Homo sapiens (O14556), Homo sapiens (P04406), Homo sapiens
Loecken, E.M.; Guengerich, F.P.
Reactions of glyceraldehyde 3-phosphate dehydrogenase sulfhydryl groups with bis-electrophiles produce DNA-protein cross-links but not mutations
Chem. Res. Toxicol.
21
453-458
2008
Homo sapiens
Tsuchiya, Y.; Okuno, Y.; Hishinuma, K.; Ezaki, A.; Okada, G.; Yamaguchi, M.; Chikuma, T.; Hojo, H.
4-Hydroxy-2-nonenal-modified glyceraldehyde-3-phosphate dehydrogenase is degraded by cathepsin G
Free Radic. Biol. Med.
43
1604-1615
2007
Homo sapiens
Harada, N.; Yasunaga, R.; Higashimura, Y.; Yamaji, R.; Fujimoto, K.; Moss, J.; Inui, H.; Nakano, Y.
Glyceraldehyde-3-phosphate dehydrogenase enhances transcriptional activity of androgen receptor in prostate cancer cells
J. Biol. Chem.
282
22651-22661
2007
Homo sapiens (P04406)
Nakajima, H.; Amano, W.; Fujita, A.; Fukuhara, A.; Azuma, Y.T.; Hata, F.; Inui, T.; Takeuchi, T.
The active site cysteine of the proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase is essential in oxidative stress-induced aggregation and cell death
J. Biol. Chem.
282
26562-26574
2007
Oryctolagus cuniculus, Homo sapiens (P04406)
Kim, H.; Deng, L.; Xiong, X.; Hunter, W.D.; Long, M.C.; Pirrung, M.C.
Glyceraldehyde 3-phosphate dehydrogenase is a cellular target of the insulin mimic demethylasterriquinone B1
J. Med. Chem.
50
3423-3426
2007
Homo sapiens
Seo, J.; Jeong, J.; Kim, Y.M.; Hwang, N.; Paek, E.; Lee, K.J.
Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase
J. Proteome Res.
7
587-602
2008
Homo sapiens
Mountassif, D.; Baibai, T.; Fourrat, L.; Moutaouakkil, A.; Iddar, A.; El Kebbaj, M.S.; Soukri, A.
Immunoaffinity purification and characterization of glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes
Acta Biochim. Biophys. Sin. (Shanghai)
41
399-406
2009
Homo sapiens
Cerella, C.; DAlessio, M.; Cristofanon, S.; De Nicola, M.; Radogna, F.; Dicato, M.; Diederich, M.; Ghibelli, L.
Subapoptogenic oxidative stress strongly increases the activity of the glycolytic key enzyme glyceraldehyde 3-phosphate dehydrogenase
Ann. N. Y. Acad. Sci.
1171
583-590
2009
Homo sapiens
Li, Y.; Huang, T.; Zhang, X.; Wan, T.; Hu, J.; Huang, A.; Tang, H.
Role of glyceraldehyde-3-phosphate dehydrogenase binding to hepatitis B virus posttranscriptional regulatory element in regulating expression of HBV surface antigen
Arch. Virol.
154
519-524
2009
Homo sapiens
Patra, S.; Ghosh, S.; Bera, S.; Roy, A.; Ray, S.; Ray, M.
Molecular characterization of tumor associated glyceraldehyde-3-phosphate dehydrogenase
Biochemistry (Moscow)
74
717-727
2009
Homo sapiens
Lu, J.; Suzuki, T.; Lu, S.; Suzuki, N.
Involvement of glyceraldehyde-3-phosphate dehydrogenase in the X-Ray resistance of HeLa cells
Biosci. Biotechnol. Biochem.
72
2432-2435
2008
Homo sapiens
Vissing, K.; Overgaard, K.; Nedergaard, A.; Fredsted, A.; Schjerling, P.
Effects of concentric and repeated eccentric exercise on muscle damage and calpain-calpastatin gene expression in human skeletal muscle
Eur. J. Appl. Physiol.
103
323-332
2008
Homo sapiens (P04406)
Azam, S.; Jouvet, N.; Jilani, A.; Vongsamphanh, R.; Yang, X.; Yang, S.; Ramotar, D.
Human glyceraldehyde-3-phosphate dehydrogenase plays a direct role in reactivating oxidized forms of the DNA repair enzyme APE1
J. Biol. Chem.
283
30632-30641
2008
Homo sapiens (P04406)
Jarczowski, F.; Jahreis, G.; Erdmann, F.; Schierhorn, A.; Fischer, G.; Edlich, F.
FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate dehydrogenase inhibitor
J. Biol. Chem.
284
766-773
2009
Oryctolagus cuniculus, Homo sapiens
Yang, S.; Liu, M.; Tien, C.; Chou, S.; Chang, R.
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interaction with 3 ends of Japanese encephalitis virus RNA and colocalization with the viral NS5 protein
J. Biomed. Sci.
16
40
2009
Homo sapiens, Mesocricetus auratus
Demarse, N.A.; Ponnusamy, S.; Spicer, E.K.; Apohan, E.; Baatz, J.E.; Ogretmen, B.; Davies, C.
Direct binding of glyceraldehyde 3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation
J. Mol. Biol.
394
789-803
2009
Homo sapiens
Zhou, Y.; Yi, X.; Stoffer, J.B.; Bonafe, N.; Gilmore-Hebert, M.; McAlpine, J.; Chambers, S.K.
The multifunctional protein glyceraldehyde-3-phosphate dehydrogenase is both regulated and controls colony-stimulating factor-1 messenger RNA stability in ovarian cancer
Mol. Cancer Res.
6
1375-1384
2008
Homo sapiens
Backlund, M.; Paukku, K.; Daviet, L.; De Boer, R.A.; Valo, E.; Hautaniemi, S.; Kalkkinen, N.; Ehsan, A.; Kontula, K.K.; Lehtonen, J.Y.
Posttranscriptional regulation of angiotensin II type 1 receptor expression by glyceraldehyde 3-phosphate dehydrogenase
Nucleic Acids Res.
37
2346-2358
2009
Homo sapiens
Koelln, J.; Zhang, Y.; Thai, G.; Demetriou, M.; Hermanowicz, N.; Duquette, P.; Van Den Noort, S.; Qin, Y.
Inhibition of glyceraldehyde-3-phosphate dehydrogenase activity by antibodies present in the cerebrospinal fluid of patients with multiple sclerosis
J. Immunol.
185
1968-1975
2010
Homo sapiens
Chaikuad, A.; Shafqat, N.; Al-Mokhtar, R.; Cameron, G.; Clarke, A.R.; Brady, R.L.; Oppermann, U.; Frayne, J.; Yue, W.W.
Structure and kinetic characterization of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS
Biochem. J.
435
401-409
2011
Homo sapiens (O14556), Homo sapiens
Guido, R.; Cardoso, C.; De Moraes, M.; Andricopulo, A.; Cass, Q.; Oliva, G.
Structural insights into the molecular basis responsible for the effects of immobilization on the kinetic parameters of glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi and human
J. Braz. Chem. Soc.
21
1845-1853
2010
Homo sapiens, Trypanosoma cruzi, Trypanosoma cruzi (P22513)
-
Kishimoto, N.; Onitsuka-Kishimoto, A.; Iga, N.; Takamune, N.; Shoji, S.; Misumi, S.
The C-terminal domain of glyceraldehyde 3-phosphate dehydrogenase plays an important role in suppression of tRNALys3 packaging into human immunodeficiency virus type-1 particles
Biochem. Biophys. Rep.
8
325-332
2016
Homo sapiens (P04406)
-
Arutyunova, E.I.; Domnina, L.V.; Chudinova, A.A.; Makshakova, O.N.; Arutyunov, D.Y.; Muronetz, V.I.
Localization of non-native D-glyceraldehyde-3-phosphate dehydrogenase in growing and apoptotic HeLa cells
Biochemistry (Moscow)
78
91-95
2013
Homo sapiens
Kuravsky, M.; Barinova, K.; Marakhovskaya, A.; Eldarov, M.; Semenyuk, P.; Muronetz, V.; Schmalhausen, E.
Sperm-specific glyceraldehyde-3-phosphate dehydrogenase is stabilized by additional proline residues and an interdomain salt bridge
Biochim. Biophys. Acta
1844
1820-1826
2014
Homo sapiens (O14556), Homo sapiens (P04406)
Kuravsky, M.L.; Barinova, K.V.; Asryants, R.A.; Schmalhausen, E.V.; Muronetz, V.I.
Structural basis for the NAD binding cooperativity and catalytic characteristics of sperm-specific glyceraldehyde-3-phosphate dehydrogenase
Biochimie
115
28-34
2015
Homo sapiens (O14556), Homo sapiens (P04406)
Maurer, J.; Bovo, F.; Gomes, E.; Loureiro, H.; Stevan, F.; Zawadzki-Baggio, S.; Nakano, M.
Kinetic data of D-glyceraldehyde-3-phosphate dehydrogenase from HeLa cells
Curr. Enzyme Inhib.
11
124-131
2015
Homo sapiens (P04406)
-
Zhang, K.; Sun, W.; Huang, L.; Zhu, K.; Pei, F.; Zhu, L.; Wang, Q.; Lu, Y.; Zhang, H.; Jin, H.; Zhang, L.H.; Zhang, L.; Yue, J.
Identifying glyceraldehyde 3-phosphate dehydrogenase as a cyclic adenosine diphosphoribose binding protein by photoaffinity protein-ligand labeling approach
J. Am. Chem. Soc.
139
156-170
2017
Homo sapiens
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)
Kunjithapatham, R.; Geschwind, J.F.; Devine, L.; Boronina, T.N.; OMeally, R.N.; Cole, R.N.; Torbenson, M.S.; Ganapathy-Kanniappan, S.
Occurrence of a multimeric high-molecular-weight glyceraldehyde-3-phosphate dehydrogenase in human serum
J. Proteome Res.
14
1645-1656
2015
Homo sapiens (P04406)
Danshina, P.; Qu, W.; Temple, B.; Rojas, R.; Miley, M.; Machius, M.; Betts, L.; OBrien, D.
Structural analyses to identify selective inhibitors of glyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific glycolytic enzyme
Mol. Hum. Reprod.
22
410-426
2016
Homo sapiens (O14556), Homo sapiens (P04406), Homo sapiens, Mus musculus (P16858), Mus musculus (Q64467), Mus musculus
Kosova, A.A.; Khodyreva, S.N.; Lavrik, O.I.
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interacts with apurinic/apyrimidinic sites in DNA
Mutat. Res.
779
46-57
2015
Homo sapiens (P04406), Oryctolagus cuniculus (P46406)
Suzuki, M.; Sasabe, J.; Miyoshi, Y.; Kuwasako, K.; Muto, Y.; Hamase, K.; Matsuoka, M.; Imanishi, N.; Aiso, S.
Glycolytic flux controls D-serine synthesis through glyceraldehyde-3-phosphate dehydrogenase in astrocytes
Proc. Natl. Acad. Sci. USA
112
E2217-E2224
2015
Homo sapiens (P04406)
Margaryan, H.; Dorosh, A.; Capkova, J.; Manaskova-Postlerova, P.; Philimonenko, A.; Hozak, P.; Peknicova, J.
Characterization and possible function of glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein GAPDHS in mammalian sperm
Reprod. Biol. Endocrinol.
13
15
2015
Homo sapiens (O14556), Homo sapiens, Mus musculus (Q64467), Mus musculus, Mus musculus BALB/c (Q64467)
Ding, X.; Wang, L.; Chen, M.; Wu, Y.; Ge, S.; Li, J.; Fan, X.; Lin, M.
Sperm-specific glycolysis enzyme glyceraldehyde-3-phosphate dehydrogenase regulated by transcription factor SOX10 to promote uveal melanoma tumorigenesis
Front. Cell Dev. Biol.
9
610683
2021
Homo sapiens (O14556)
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Release 2023.1 (January 2023)
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