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EC Tree
IUBMB Comments Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
The taxonomic range for the selected organisms is: Trypanosoma cruzi The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
gapdhs, d-glyceraldehyde-3-phosphate dehydrogenase, gapds, gadph, glyceraldehyde-3-phosphate dehydrogenases, plasmin receptor, gapc1, plasminogen-binding protein, gapcp, glyceraldehyde-3 phosphate dehydrogenase,
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3-phosphoglyceraldehyde dehydrogenase
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dehydrogenase, glyceraldehyde phosphate
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dihydrogenase, glyceraldehyde phosphate
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glyceraldehyde phosphate dehydrogenase (NAD)
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glyceraldehyde-3-P-dehydrogenase
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glyceraldehyde-3-phosphate dehydrogenase
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glyceraldehyde-3-phosphate dehydrogenase (NAD)
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Larval antigen OVB95
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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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NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
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NADH-glyceraldehyde phosphate dehydrogenase
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phosphoglyceraldehyde dehydrogenase
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Plasminogen-binding protein
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triose phosphate dehydrogenase
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GAPDH
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-, -, -, -, -, -, -, -, -, -, -, -, -
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D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating)
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
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?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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r
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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+
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D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
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NAD+
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(8E,11E)-C15:2-anacardic acid
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(8E,11E,14E)-C15:3-anacardic acid
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(E)-2-hydroxy-6-(pentadec-8-en-1-yl)benzoic acid
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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
guajaverin
molecular docking studies. Guajaverin is stabilized by five hydrogen bonds with the amino acids Ser165, Thr226, Arg249, Ser134, and Glu336
quercetin
molecular docking studies. Quercetin is stabilized by two hydrogen bonds with the amino acids Ala198 and Pro253
tiliroside
molecular docking studies. Tiliroside is stabilized by four hydrogen bonds with the amino acids Cys166, Ser134, and Ser110
(3-[(4-nitrophenoxy)carbonyl]but-3-en-1-yl)phosphonic acid
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2-(dodec-1-en-1-yl)-6-hydroxybenzoic acid
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inhibition is not reversed or prevented by addition of Triton X-100. Noncompetitive with respect to both substrate and cofactor
2-pentadecyl-6-hydroxybenzoic acid
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inhibition is not reversed or prevented by addition of Triton X-100. Noncompetitive with respect to both substrate and cofactor
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DMSO
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activity is increased about 2fold in the presence of 5% DMSO (v/v)
methanol
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activity is increased about 6fold in the presence of 5% methanol (v/v)
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0.42 - 0.5
D-glyceraldehyde 3-phosphate
0.0102 - 0.5
D-glyceraldehyde 3-phosphate
0.425 - 0.5
D-Glyceraldehyde-3-phosphate
0.42
D-glyceraldehyde 3-phosphate
free enzyme,25°C, pH 8.6
0.5
D-glyceraldehyde 3-phosphate
enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
0.26
NAD+
free enzyme,25°C, pH 8.6
0.67
NAD+
enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
0.0102
D-glyceraldehyde 3-phosphate
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in the presence of 5% (v/v) methanol, in TEA-HCl buffer (pH 7.5) at 25°C
0.0102
D-glyceraldehyde 3-phosphate
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in the presence of 5% (v/v) methanol
0.0108
D-glyceraldehyde 3-phosphate
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in the presence of 5% (v/v) DMSO, in TEA-HCl buffer (pH 7.5) at 25°C
0.0108
D-glyceraldehyde 3-phosphate
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in the presence of 5% (v/v) DMSO
0.0393
D-glyceraldehyde 3-phosphate
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in the absence of DMSO and methanol, in TEA-HCl buffer (pH 7.5) at 25°C
0.42
D-glyceraldehyde 3-phosphate
free enzyme, at pH 7.5 and 25°C
0.5
D-glyceraldehyde 3-phosphate
immobilized enzyme reactor, at pH 7.5 and 25°C
0.425
D-Glyceraldehyde-3-phosphate
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free enzyme
0.5
D-Glyceraldehyde-3-phosphate
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GAPDH immobilized on an octyl silica column
0.258
NAD+
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free enzyme
0.26
NAD+
free enzyme, at pH 7.5 and 25°C
0.67
NAD+
immobilized enzyme reactor, at pH 7.5 and 25°C
0.674
NAD+
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GAPDH immobilized on an octyl silica column
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71.4 - 442
D-glyceraldehyde 3-phosphate
71.4
D-glyceraldehyde 3-phosphate
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in the absence of DMSO and methanol, in TEA-HCl buffer (pH 7.5) at 25°C
118
D-glyceraldehyde 3-phosphate
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in the presence of 5% (v/v) DMSO, in TEA-HCl buffer (pH 7.5) at 25°C
442
D-glyceraldehyde 3-phosphate
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in the presence of 5% (v/v) methanol, in TEA-HCl buffer (pH 7.5) at 25°C
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0.004 - 0.005
2-(dodec-1-en-1-yl)-6-hydroxybenzoic acid
0.002 - 0.004
2-pentadecyl-6-hydroxybenzoic acid
0.004
2-(dodec-1-en-1-yl)-6-hydroxybenzoic acid
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pH 8.9, 25°C, substrate D-glyceraldehyde 3-phosphate
0.005
2-(dodec-1-en-1-yl)-6-hydroxybenzoic acid
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pH 8.9, 25°C, substrate NAD+
0.002
2-pentadecyl-6-hydroxybenzoic acid
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pH 8.9, 25°C, substrate D-glyceraldehyde 3-phosphate
0.004
2-pentadecyl-6-hydroxybenzoic acid
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pH 8.9, 25°C, substrate NAD+
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0.161
(8E)-C15:1-anacardic acid
Trypanosoma cruzi
pH 7.5, 25°C
0.069
(8E,11E)-C15:2-anacardic acid
Trypanosoma cruzi
pH 7.5, 25°C
0.038
(8E,11E,14E)-C15:3-anacardic acid
Trypanosoma cruzi
pH 7.5, 25°C
0.14
guajaverin
Trypanosoma cruzi
pH 7.5, 25°C
0.149
mangiferin
Trypanosoma cruzi
pH 7.5, 25°C
0.142
quercetin
Trypanosoma cruzi
pH 7.5, 25°C
0.046
tiliroside
Trypanosoma cruzi
pH 7.5, 25°C
0.055
2-(dodec-1-en-1-yl)-6-hydroxybenzoic acid
Trypanosoma cruzi
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pH 8.9, 25°C
0.028
2-pentadecyl-6-hydroxybenzoic acid
Trypanosoma cruzi
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pH 8.9, 25°C
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Uniprot
brenda
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G3PG_TRYCR
359
0
39061
Swiss-Prot
other Location (Reliability: 5 )
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molecular dynamics simulations based on PDB entry 1K3T. The first stage of the reaction (oxidoreduction) takes place in the Pi site (energetically more favourable), with the formation of oxyanion thiohemiacetal and thioacylenzyme intermediates without acid-base assistance of His194. Residue Arg249 has an important role in the ability of the enzyme to bind the glyceraldehyde 3-phosphatesubstrate, which interacts with NAD+ and other important residues, such as Cys166, Glu109, Thr167, Ser247 and Thr226, in the GAPDH active site
hanging drop vapour diffusion method, enzyme in complex with the covalently bound GAP analogue, 3-(p-nitrophenoxycarboxyl)-3-ethylene propyl dihydroxyphosphonate, at an improved resolution of 2.0-2.5 A
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-80°C, triethanolamine (100 mM, pH 7.5), containing 1.0 mM beta-mercaptoethanol, 1.0 mM EDTA, 30 mM sodium arsenate heptahydrate, 1.0 mM phenylmethylsulfonyl fluoride, 50 mM NAD+, 1.0 mM pepstatin, 1.0 mM leupeptin, 0.5 M KCl, and glycerol 10% (v/v), 8 months, 1% loss of activity
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25°C, free enzyme in Tris-HCl (50 mM, pH 8.6), containing 1.0 mM beta-mercaptoethanol, 30 mM sodium arsenate heptahydrate, and 1.0 mM EDTA, 99% of the enzymatic activity is retained after 24 h and 57% after 120 h
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4°C, free enzyme in buffer 8, 55% of the enzymatic activity is retained after dialysis and after 48 h the calculated activity has fallen to 7%
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4°C, free enzyme in Tris-HCl (50 mM, pH 8.6), containing 1.0 mM beta-mercaptoethanol, 30 mM sodium arsenate heptahydrate, and 1.0 mM EDTA, 55% of the enzymatic activity is retained after dialysis and after 48 h the calculated activity has fallen to 25%
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two genes for glyceraldehyde-3-phosphate dehydrogenase
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Kendall, G.; Ashall, F.; Miles, M.A.; Kelly, J.M.
Genes encoding glyceraldehyde-3-phosphate dehydrogenase in Trypanosoma cruzi
Biochem. Soc. Trans.
16
1067
1988
Trypanosoma cruzi
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brenda
Castilho, M.S.; Pavao, F.; Oliva, G.; Ladame, S.; Willson, M.; Perie, J.
Evidence for the two phosphate binding sites of an analogue of the thioacyl intermediate for the Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase-catalyzed reaction, from its crystal structure
Biochemistry
42
7143-7151
2003
Trypanosoma cruzi
brenda
Wiggers, H.J.; Cheleski, J.; Zottis, A.; Oliva, G.; Andricopulo, A.D.; Montanari, C.A.
Effects of organic solvents on the enzyme activity of Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase in calorimetric assays
Anal. Biochem.
370
107-114
2007
Trypanosoma cruzi
brenda
Cardoso, C.L.; de Moraes, M.C.; Guido, R.V.; Oliva, G.; Andricopulo, A.D.; Wainer, I.W.; Cass, Q.B.
The development of an immobilized enzyme reactor containing glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi: the effect of species specific differences on the immobilization
Analyst
133
93-99
2008
Trypanosoma cruzi
brenda
Pereira, J.M.; Severino, R.P.; Vieira, P.C.; Fernandes, J.B.; da Silva, M.F.; Zottis, A.; Andricopulo, A.D.; Oliva, G.; Correa, A.G.
Anacardic acid derivatives as inhibitors of glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi
Bioorg. Med. Chem.
16
8889-8895
2008
Trypanosoma cruzi
brenda
Freitas, R.F.; Prokopczyk, I.M.; Zottis, A.; Oliva, G.; Andricopulo, A.D.; Trevisan, M.T.; Vilegas, W.; Silva, M.G.; Montanari, C.A.
Discovery of novel Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase inhibitors
Bioorg. Med. Chem.
17
2476-2482
2009
Trypanosoma cruzi (P22513)
brenda
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)
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brenda
Reis, M.; Alves, C.N.; Lameira, J.; Tunon, I.; Marti, S.; Moliner, V.
The catalytic mechanism of glyceraldehyde 3-phosphate dehydrogenase from Trypanosoma cruzi elucidated via the QM/MM approach
Phys. Chem. Chem. Phys.
15
3772-3785
2013
Trypanosoma cruzi, Trypanosoma cruzi (P22513)
brenda