1.2.1.12: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
This is an abbreviated version!
For detailed information about glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), go to the full flat file.
Word Map on EC 1.2.1.12
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1.2.1.12
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tetramer
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chloroplast
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gapcs
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streptococcal
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stearothermophilus
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glomerulonephritis
-
nadp-dependent
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genorm
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normfinder
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medicine
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3-phosphoglycerate
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phosphofructokinase
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flagellum
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poststreptococcal
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1,3-bisphosphoglycerate
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bestkeeper
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lobster
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glycosomal
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2.7.1.11
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glyceraldehyde-phosphate
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nephritogenic
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4.1.2.13
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plr
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2.7.2.3
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endocapillary
-
drug development
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agriculture
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biofuel production
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analysis
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synthesis
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biotechnology
-
pharmacology
- 1.2.1.12
- tetramer
- chloroplast
-
gapcs
- streptococcal
- stearothermophilus
- glomerulonephritis
-
nadp-dependent
-
genorm
-
normfinder
- medicine
- 3-phosphoglycerate
-
phosphofructokinase
- flagellum
-
poststreptococcal
- 1,3-bisphosphoglycerate
-
bestkeeper
- lobster
- glycosomal
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2.7.1.11
-
glyceraldehyde-phosphate
-
nephritogenic
-
4.1.2.13
- plr
-
2.7.2.3
-
endocapillary
- drug development
- agriculture
- biofuel production
- analysis
- synthesis
- biotechnology
- pharmacology
Reaction
Synonyms
3-phosphoglyceraldehyde dehydrogenase, A4-GAPDH, A4-glyceraldehyde-3-phosphate dehydrogenase, AB-GAPDH, AnBn-GAPDH, AsGAPDH, At3g04120, BARS-38, CbbG, CgGAP, Clo1313_2095, complement-C3-binding protein, CP 17/CP 18, Ctherm_Gapdh, cytosolic NAD-dependent glyceraldehyde 3-P dehydrogenase, cytosolic phosphorylating glyceraldehyde-3-phosphate dehydrogenase, D-glyceraldehyde-3-phosphate dehydrogenase, D-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating), dehydrogenase, glyceraldehyde phosphate, dihydrogenase, glyceraldehyde phosphate, EcGAPDH, EcGAPDH1, FgGAPDH, FhGAPDH, G3PD, G3PDH, Ga3P dehydrogenase, Ga3PDHase, GADPH, GAP, GAP1, gap2, GapA, GapB, GAPC, GapC-1, GapC1, GapC2, GAPCp, GAPCp1, GAPCp2, GAPD, GAPDH, GAPDH type 1, GAPDH1, GAPDH2, GAPDH3, GAPDHS, GAPDS, GAPN, GBS GAPDH, glyceraldehyde 3-phosphate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase-S, glyceraldehyde phosphate dehydrogenase (NAD), glyceraldehyde-3 phosphate dehydrogenase, glyceraldehyde-3-P-dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase (NAD), glyceraldehyde-3-phosphate dehydrogenase 1, glyceraldehyde-3-phosphate dehydrogenase, type I, glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein GAPDHS, glyceraldehyde-3-phosphate dehydrogenases, GPD, GPD2, Gra3PDH, GraP-DH, H.c-C3BP, hGAPDH, HsGAPDH, kmGAPDH1p, Larval antigen OVB95, Major larval surface antigen, Mtb-GAPDH, NAD+-dependent GAPDH, NAD+-dependent glyceraldehyde 3-phosphate dehydrogenase, NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD+-G-3-P dehydrogenase, NAD+-GAPDH, NAD-dependent Ga3PDHase, NAD-dependent glyceraldehyde 3-phosphate dehydrogenase, NAD-dependent glyceraldehyde phosphate dehydrogenase, NAD-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent phosphorylating glyceraldehyde-3-phosphate dehydrogenase, NAD-G3PDH, NAD-GAPDH, NADH-glyceraldehyde phosphate dehydrogenase, P-37, p-GAPDH, PfGAPDH, phosphoglyceraldehyde dehydrogenase, phosphorylating NAD+-dependent GAPDH, Plasmin receptor, Plasminogen-binding protein, plastidial glyceraldehyde-3-phosphate dehydrogenase, pmGAPDH, PyGapdh, rmGAPDH, Rv1436, somatic GAPD, somatic glyceraldehyde 3-phosphate dehydrogenase, sperm-specific GAPDS, sperm-specific glyceraldehyde 3-phosphate dehydrogenase, sperm-specific glyceraldehyde-3-phosphate dehydrogenase, TaeNAD-GAPDH, TagapC, TDH1, TDH2, TDH3, TLAb, triose phosphate dehydrogenase, UDG, uracil-DNA glycosylase, vGPD
ECTree
1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)Advanced search results
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results (Inhibitors
Inhibitors on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide
-
treatment with (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide between 0.001 and 1 mM induces the oligomerization of GAPDH, dithiothreitol reduces (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide-induced aggregation in a concentration-dependent manner
2-(6-amino-2-methyl-9H-purin-9-yl)-5-(hydroxymethyl)tetrahydrofuran-3,4-diol
-
2-(dodec-1-en-1-yl)-6-hydroxybenzoic acid
-
inhibition is not reversed or prevented by addition of Triton X-100. Noncompetitive with respect to both substrate and cofactor
2-(hydroxymethyl)-5-[6-[(2-methylphenyl)amino]-9H-purin-9-yl]tetrahydrofuran-3,4-diol
-
2-(hydroxymethyl)-5-[6-[(3-methylbutyl)amino]-9H-purin-9-yl]tetrahydrofuran-3,4-diol
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2-(hydroxymethyl)-5-[6-[(3-methylphenyl)amino]-9H-purin-9-yl]tetrahydrofuran-3,4-diol
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2-pentadecyl-6-hydroxybenzoic acid
-
inhibition is not reversed or prevented by addition of Triton X-100. Noncompetitive with respect to both substrate and cofactor
2-[6-amino-8-(pyrimidin-2-ylsulfanyl)-9H-purin-9-yl]-5-(hydroxymethyl)tetrahydrofuran-3,4-diol
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2-[9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-yl]-2,3-dihydroisoquinoline
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3-(1,3-benzodioxol-5-yl)-6-[[(1E)-1H-indol-3-ylmethylene]amino]-2H-chromen-2-one
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3-(1,3-benzodioxol-5-yl)-6-[[(1E)-1H-pyrrol-2-ylmethylene]amino]-2H-chromen-2-one
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3-(1,3-benzodioxol-5-yl)-6-[[(1E)-2-furylmethylene]amino]-2H-chromen-2-one
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3-(1,3-benzodioxol-5-yl)-6-[[(1E)-pyridin-2-ylmethylene]amino]-2H-chromen-2-one
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3-(1,3-benzodioxol-5-yl)-6-[[(1E)-thien-2-ylmethylene]amino]-2H-chromen-2-one
-
3-(p-nitrophenoxycarboxyl)-3-ethylene propyl dihydroxyphosphinate
propyl dihydroxyphosphonate analogue of substrate glyceraldehyde 3-phosphate. The energy profiles correspond to the nucleophilic attack of Cys166 on the atom C1 of the carbonyl group of the inhibitor. The barrier for the inhibition reaction is lower than that observed for a natural substrate
3-morpholino-sydnonimine
-
the NO-generating compound inactivates by induction of a covalent binding of NAD+ to the enzyme. The superoxide anion released by 3-morpholino-sydnonimine potentiates the inactivation
9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-2-yl-9H-purin-6-amine
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9-(2-deoxy-2-[[(2,4-dihydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-2-yl-9H-purin-6-amine
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9-(2-deoxy-2-[[(2-hydroxy-3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(3,4-dihydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(3,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(3,5-dihydroxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(2-methylphenyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3-methylphenyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-phenyl-9H-purin-6-amine
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9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-[(3-methoxynaphthalen-1-yl)methyl]-9H-purin-6-amine
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9-(2-deoxy-2-[[(3-ethoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3-hydroxy-4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
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9-(2-deoxy-2-[[(3-hydroxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(3-hydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(3-hydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
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9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(2-methoxyphenyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-phenyl-9H-purin-6-amine
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9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-[(7-methylnaphthalen-1-yl)methyl]-9H-purin-6-amine
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9-(2-deoxy-2-[[(4-heptylphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(4-hydroxy-3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(4-hydroxy-3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
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9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(1-phenylethyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(2,5-dimethylphenyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3,4-dimethylphenyl)-9H-purin-6-amine
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9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amine
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9-(2-[[(4-chlorophenyl)carbonyl]amino]-2-deoxypentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amine
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9-(2-[[(4-chlorophenyl)carbonyl]amino]-2-deoxypentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
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9-(2-[[(4-chlorophenyl)carbonyl]amino]-2-deoxypentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
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9-[2-([[2,4-bis(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amine
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9-[2-([[3,4-bis(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amine
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9-[2-([[3-(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
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9-[2-([[3-(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amine
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9-[2-([[4-(acetyloxy)-3-methoxyphenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
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9-[2-deoxy-2-([[4-(dimethylamino)phenyl]carbonyl]amino)pentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amine
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9-[2-deoxy-2-[(phenylcarbonyl)amino]pentofuranosyl]-8-thiophen-2-yl-9H-purin-6-amine
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acetylleucine chloromethyl ketone
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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
ADP-ribose
coenzyme analogue with a non-cooperative behaviour of binding, is a potent competitive inhibitor
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
arsenate
linear substrate inhibition, competitive versus phosphate
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
Fe2+
-
in the absence of quercetin, GAPDH can be oxidized by ferrous ions due to the formation of reactive oxygen species according to the following series of reactions
guajaverin
molecular docking studies. Guajaverin is stabilized by five hydrogen bonds with the amino acids Ser165, Thr226, Arg249, Ser134, and Glu336
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
hydrogen peroxide
-
maximum inhibition is observed at concentrations of 0.2 mM
monoclonal antibody 8B7
-
antibody is specific for glyceraldehyde 3-phosphate dehydrogenase. In lysates of Sf21 cells, the antibody inhibits protein translation, possibly due to inhibition of the binding of glyceraldehyde 3-phosphate dehydrogenase to mRNA and tRNA
-
N-(3-acetylnaphthalen-1-yl)-9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
N-(3-acetylnaphthalen-1-yl)-9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
N-(4-acetylnaphthalen-1-yl)-9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
N-(4-acetylnaphthalen-1-yl)-9-[2-deoxy-2-([[4-(methylamino)phenyl]carbonyl]amino)pentofuranosyl]-9H-purin-6-amine
-
N-acetylcysteine
-
5 mM N-acetylcysteine significantly reduces G3PD activation induced by both H2O2 and ferric protoporphyrin IX
N-benzyl-9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
N-[2-(6-amino-8-bromo-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]benzamide
-
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]-1H-benzimidazole-5-carboxamide
-
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]-3,4,5-trihydroxybenzamide
-
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]benzamide
-
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]thiophene-2-carboxamide
-
Na+
-
120 mM almost complete inhibition. Cys, GSH and deproteinated crude extract protect against inhibition
nitric oxide
isoform GAPC1 is irreversibly inhibited in a time- and concentration-dependent manner
quercetin
molecular docking studies. Quercetin is stabilized by two hydrogen bonds with the amino acids Ala198 and Pro253
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
suramin
-
cyosolic enzyme: competitive with NAD+. Effect on Km-value and maximal veocity of glyoxysomal enzyme
tiliroside
molecular docking studies. Tiliroside is stabilized by four hydrogen bonds with the amino acids Cys166, Ser134, and Ser110
trehalose
might be an inhibitor, trehalose induces a conformational change in ecGAPDH in the current structure. The rotation of GAPDH also induced a conformational change in its active site. This suggests that the binding of trehalose to GAPDH induced a conformational change in its active site to prevent the binding of NAD+, although the NAD+- and trehalose-binding sites differ from one another
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
-
Agaricic acid
-
0.14 mM, 50% inhibition in absence of NAD+. 2 mM, 35% loss of activity in presence of 0.017 mM NAD+
Agaricic acid
-
glyoxysomal enzyme: 0.2 mM, 60% loss of activity. Cytosolic enzyme: 2 mM, less than 20% loss of activity
ATP
-
inhibition is less pronounced for enzyme from sarcoma tissue as compared to normal muscle tissue
ATP
-
at 0°C, loss of activity. Some of the lost activity is regained upon warming to room temperature
D-glyceraldehyde 3-phosphate
2-mercaptoethanol protects against the inhibition
ferriprotoporphyrin IX
-
enzyme is partially inactivated through oxidation of critical thiols
ferriprotoporphyrin IX
strongly inhibits PfGapdh, in contrast to the human GAPDH
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
-
FK506-binding protein 36
-
i.e. FKBP36, forms complexes with glyceraldehyde-3-phosphate dehydrogenase and Hsp90. Both proteins bind independently to different sites of the FKBP36 tetratricopeptide repeat domain. The interaction between FKBP36 and GAPDH directly inhibits the catalytic activity of GAPDH
-
fumarate
-
approximately 20% of GAPDH activity is lost by incubation with 0.5 mM fumarate for 24 h, and 100% activity is lost in incubations with 500 mM fumarate at 24 h, NADH in the presence or absence of D-glyceraldehyde 3-phosphate significantly accelerates the inactivation of GAPDH by fumarate
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
glutathione
-
5 mM oxidized glutathione, GSSG, formation of mixed disulfide between glutathione and A4-GAPDH results in the inhibition of enzyme activity
glutathione
inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol
glutathione
-
inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol
glutathione
-
inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol
glutathione
-
formation of mixed disulfide between glutathione and GAPDH results in the inhibition of enzyme activity
glutathione
-
inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol
H2O2
inhibits enzyme activity by converting the thiolate of Cys149 into irreversibly oxidized forms, -SO2- and SO3- via a labile sulfenate intermediate SO?. Reduced glutathione prevents this irreversible process by reacting with Cys149 sulfenates to give rise to a mixed disulfide. Glutathionylated enzyme can be fully reactivated either by cytosolic glutaredoxin, via a glutathione-dependent monothiol mechanism, or, less efficiently, by cytosolic thioredoxins physiologically reduced by NADPH:thioredoxin reductase
H2O2
isoform GAPC1 is irreversibly inhibited in a time- and concentration-dependent manner
H2O2
-
GAPDH is oxidized by H2O2 which is likely formed due to the spontaneous dismutation of the superoxide anion that is formed during the autooxidation of quercetin that can result in the oxidation of SH-groups of GAPDH
iodoacetamide
an irreversible, cysteine-specific alkylator, inactivation kinetics for inactivation of mutant C162A
Koningic acid
-
inhibits arsenate reductase activity and activity with D-glyceraldehyde 3-phosphate, phosphate and NAD+
Koningic acid
-
inhibits arsenate reductase activity and activity with D-glyceraldehyde 3-phosphate, phosphate and NAD+
Koningic acid
-
irreversible inhibition, GAPDH I : 50% inhibition by 1 mM, no effect at 0.1 mM. GAPDH II: 50% inhibition by 0.01 mM. Under conditions of koningic acid production the koningic-acid-resistant isoenzyme GAPDH I is produced. In peptone-rich medium where non koningic acid is produced the koningic-acid-sensitive isoenzyme GAPDH II is produced in addition to GAPDH 1
N-(phenoxyacetyl)-L-cysteine
-
inhibits by forming disulfide bonds with the Cys149 residue in the enzyme active site
N-(phenylacetyl)-glutathione
-
inhibits by forming disulfide bonds with the Cys149 residue in the enzyme active site
NAD+
NAD+ inhibition for GAPDH3 RNA binding capability, NAD+ inhibits the AUUUA binding. The inhibition effect is weaker for the 5-base substrate than for the 13-base substrate. RNA substrate binding needs to competitively displace the NAD+ molecules from the binding groove
NADH
2-mercaptoethanol protects against the inhibition, but the inhibitory effect of NADH is not influenced by heavy metal ions or EDTA
NADH
noncompetitive inhibition versus D-glyceraldehyde 3-phosphate, competitive inhibition versus both NAD+ and arsenate
oxidized glutathione
inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found glutathionylated; inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found glutathionylated
oxidized glutathione
-
inactivation, at least partially reversible upon addition of dithiothreitol
oxidized glutathione
-
inactivation, at least partially reversible upon addition of dithiothreitol
PCMB
-
1 mM, complete inhibition, partially reversed by dithiothreitol; 1 mM, inhibition is partially reversed by dithiothreitol
pentalenolactone
-
pentalenolactone-sensitive enzyme is strongly inhibited, pentalenolactone-insensitive enzyme is not inhibited
phosphate
linear substrate inhibition, competitive versus arsenate
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
-
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
-
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
-
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
-
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
-
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-nitrosoglutathione
inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found nitrosylated; inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found nitrosylated; inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol
S-nitrosoglutathione
-
inactivation, at least partially reversible upon addition of dithiothreitol; inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol
S-nitrosoglutathione
-
inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol
S-nitrosoglutathione
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inactivation, at least partially reversible upon addition of dithiothreitol; inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol
sodium nitroprusside
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the NO-generating compound inactivates by induction of a covalent binding of NAD+ to the enzyme
sodium nitroprusside
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inhibition in presence of NAD+ is due primarily to active-site nitrosylation, covalent binding of NAD+ through a NO-dependent thiol intermediate
sodium nitroprusside
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maximum inhibition is observed at concentrations of 0.2 mM
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
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, a small-molecule, highly selective isozymeGAPDHS inhibitor, the compound causes significant reductions in mouse sperm lactate production and in the percentage of motile mouse 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+
T0506_9350
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+
Trinitrobenzenesulfonic acid
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inactivation with pseudo-first-order kinetics. D-glyceraldehyde-3-phosphate, NAD+, NADH and 3-phospho-D-glyceroyl phosphate almost completely protect from inactivation
Tyr-Asp
a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions; a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions
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Tyr-Asp
a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions; a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions
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additional information
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wild-type Clostridium thermocellum is unable to initiate growth when inoculated into medium containing ethanol at concentrations of 20 g/l or higher. Strains adapted for improved tolerance by serial transfer over a period of several weeks have been shown to initiate growth in the presence of 50-55 g/l ethanol. A dramatic accumulation of NADH and NADPH is observed when ethanol is added to the culture. The Gapdh from Clostridium thermocellum (Ctherm_Gapdh) is very sensitive to the NADH/NAD+ ratio
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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
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additional information
no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu); no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu)
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additional information
no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu); no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu)
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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
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additional information
development of GAPDH inhibitors as anti-cancer and anti-parasitic agents
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additional information
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development of GAPDH inhibitors as anti-cancer and anti-parasitic agents
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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
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additional information
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the produced type I antibody induces a time-dependent decrease in the activity by 80-90% of the active holoenzyme and 25% of the apoenzyme
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additional information
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stauroporine does not inhibit stimulation of G3PD activity
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additional information
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not inhibited by DMSO, dibromomethane and 1,2-dibromoethane
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additional information
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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)
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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
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additional information
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stable suppression of GAPDH (possibly by some reversible posttranslational modification) during ground squirrel torpor, which likely contributes to the overall reduction in carbohydrate metabolism when these animals switch to lipid fuels during dormancy. Action of commercial alkaline phosphatase causes a 50% increase in euthermic GAPDH activity, activities of protein kinase C, AMP-dependent protein kinase, or calcium-calmodulin protein kinase lead to about 80% decreases in euthermic GAPDH activity
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additional information
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no inhibition by D-glucose 6-phosphate, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, pyruvate
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additional information
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the NADH/NAD+ ratio is shown to modulate the in vivo activity; the wild type GADPH is strongly inhibited in vitro by decreased pH values
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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
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additional information
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NADH, glucose-1-phosphate, AMP, ADP, ATP, and fructose-6-phosphate do not affect kinetic properties of GAPN and no change in cofactor preference from NAD+ to NADP+ in the presence of these metabolic intermediates is detected
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additional information
no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu); no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu)
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additional information
no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu); no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu)
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additional information
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not inhibited by thiorphan and lipopolysaccharide
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additional information
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not inhibited by ((R)-mandelyl)-(S)-cysteine
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additional information
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not inhibitory: N-((R)-mandelyl)-(S)-cysteine
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additional information
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not inhibited by thiorphan and lipopolysaccharide
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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
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additional information
the C-terminus of CP12 is inserted into the active-site region of glyceraldehyde-3-phosphate dehydrogenase, resulting in competitive inhibition of the enzyme
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additional information
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H2O2 does not significantly alter GAPDH-specific activity levels in cell free extracts
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