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Information on EC 1.2.1.107 - glyceraldehyde-3-phosphate dehydrogenase (arsenate-transferring)
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1.2.1.107 glyceraldehyde-3-phosphate dehydrogenase (arsenate-transferring)IUBMB Comments
The enzyme, discovered in bacteria, is very similar to EC 1.2.1.12, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). However, the gene encoding it is located in arsenic resistance islands in the chromosome, next to a gene (arsJ) that encodes a transporter that removes the product, 1-arsono-3-phosphoglycerate, from the cell. Together the two proteins form an arsenic detoxification system.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
fa-gpdh, [beta-(2-furyl)acryloyl]glyceraldehyde-3-phosphate dehydrogenase, acylglyceraldehyde-3-phosphate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-glyceraldehyde-3-phosphate dehydrogenase
G3PD
GAPDH
glyceraldehyde-3-P dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde 3-phosphate + arsenate + NAD+ = 1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (arsenate-transferring)
The enzyme, discovered in bacteria, is very similar to EC 1.2.1.12, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating). However, the gene encoding it is located in arsenic resistance islands in the chromosome, next to a gene (arsJ) that encodes a transporter that removes the product, 1-arsono-3-phosphoglycerate, from the cell. Together the two proteins form an arsenic detoxification system.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
DL-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
additional information
?
-
-
the enzyme is absolutely specific for NAD+. NADP+ does not substitute for NAD+
-
-
-
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
ir
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
ir
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
ir
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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 + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
ir
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
ir
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arsono-3-phospho-D-glycerate + NADH + H+
-
-
-
-
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
the enzyme is absolutely specific for NAD+. NADP+ does not substitute for NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-alpha-cholorhydrin
-
100 or 200 mg/kg (S)-alpha-cholorhydrin inhibits arsenate reduction by the liver, but not by the whole body
arsenate
-
the enzyme is allosterically inhibited at concentrations above 10 mM
L-Glyceraldehyde 3-phosphate
-
the enzyme is allosterically inhibited at concentrations above 1 mM
D-glyceraldehyde 3-phosphate
-
the enzyme is allosterically inhibited at concentrations above 1 mM
Ghost band 3 polypeptide
-
the inhibition is competitive with respect to NAD+ and arsenate, but non-competitive with glyceraldehyde 3-phosphate
-
Ghost band 3 polypeptide
-
the inhibition is competitive with respect to NAD+ and arsenate, but non-competitive with glyceraldehyde 3-phosphate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
the enzyme activity is increased about 10fold in the presence of 0.045 M (NH4)2SO4
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
100
D-glyceraldehyde 3-phosphate
-
mutant enzyme H176N, at pH 8.5 and 27°C
100
D-glyceraldehyde 3-phosphate
-
wild type enzyme, at pH 8.5 and 27°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is preferentially associated with the plasma membrane of erythrocytes
brenda
-
the enzyme is preferentially associated with the plasma membrane of erythrocytes
brenda
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
145000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using either 12.9% (w/w) PEG 2000, 50 mM acetate buffer (pH 5.2) and 6.4% (w/v) PEG 200 or2.5% (w/v) PEG 1000, 50 mM acetate buffer (pH 4.8) and 25.7% (w/v) PEG 2000 MME
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H176N
-
the mutant shows a Km value 5times smaller than for the wild type enzyme while the Km value for arsenate is about 5times larger. The mutant has a significantly reduced thermal stability at 65°C. The half-life for thermal denaturation for the mutant holoenzyme is increased nearly 100fold over the corresponding value for the apoenzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is dissociated into subunits by ATP and can be reversibly dissociated by urea
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, acetone precipitation, NAD-Sepharose column chromatography, and Sephadex G-100 gel filtration, and DEAE-Sephadex gel filtration
-
ammonium sulfate precipitation, DEAE-Sephadex.column chromatography, and SE-Sephadex gel filtration
-
phenyl-Sepharose column chromatography and DEAE-cellulose column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli AW3110 cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Machado, A.; Silva, M.; Iulek, J.
Expression, purification, enzymatic characterization and crystallization of glyceraldehyde-3-phosphate dehydrogenase from Naegleria gruberi, the first one from phylum Percolozoa
Protein Expr. Purif.
127
125-130
2016
Naegleria gruberi
brenda
Malhotra, O.; Bernhard, S.
Role of nicotinamide adenine dinucleotide as an effector in formation and reactions of acylglyceraldehyde-3-phosphate dehydrogenase
Biochemistry
20
5529-5538
1981
Acipenser sp.
brenda
Malhotra, O.; Bernhard, S.
Noncovalent modulation by ATP of the acyl transfer from acyl-glyceraldehyde-3-phosphate dehydrogenase to phosphate
Biochemistry
28
124-128
1989
Acipenser sp.
brenda
Liu, L.; Huskey, W.
Progress in establishing the rate-limiting features and kinetic mechanism of the glyceraldehyde-3-phosphate dehydrogenase reaction
Biochemistry
31
6898-6903
1992
Oryctolagus cuniculus
brenda
Tomschy, A.; Glockshuber, R.; Jaenicke, R.
Functional expression of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima in Escherichia coli Authenticity and kinetic properties of the recombinant enzyme
Eur. J. Biochem.
214
43-50
1993
Thermotoga maritima, Thermotoga maritima MSB 8
brenda
Veress, L.; Mullin, D.; Bovarsky, D.; Dimaunahan, C.; Byers, L.
The role of His-176 in the chemical mechanism and thermal stability of glyceraldehyde-3-phosphate dehydrogenase
FASEB J.
10
A1385
1996
Geobacillus stearothermophilus
-
brenda
Tsai, I.; Murthy, S.; Steck, T.
Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase
J. Biol. Chem.
257
1438-1442
1982
Oryctolagus cuniculus, Homo sapiens
brenda
Rogalski, A.; Steck, T.; 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, Rattus norvegicus
brenda
Wu, S.; Wang, L.; Gan, R.; Tong, T.; Bian, H.; Li, Z.; Du, S.; Deng, Z.; Chen, S.
Signature arsenic detoxification pathways in Halomonas sp. strain GFAJ-1
mBio
9
e00515-18
2018
Halomonas sp. GFAJ-1
brenda
Dagher, S.; Deal, W.J.
[54] Glyceraldehyde-3-phosphate dehydrogenase from pig liver
Methods Enzymol.
89
310-316
1982
Sus scrofa
brenda
Speranza, M.; Ferri, G.
[55] Glyceraldehyde-3-phosphate dehydrogenase (glycolytic form) from spinach leaves
Methods Enzymol.
89
316-319
1982
Spinacia oleracea
-
brenda
Duggleby, R.; Dennis, D.
[56] Glyceraldehyde-3-phosphate dehydrogenase from pea seeds
Methods Enzymol.
89
319-325
1982
Pisum sativum
-
brenda
Oshima, T.; Fujita, S.; Imahori, K.
[58] Glyceraldehyde-3-phosphate dehydrogenase from Thermus thermophilus
Methods Enzymol.
89
335-340
1982
Thermus thermophilus
-
brenda
Chen, J.; Yoshinaga, M.; Garbinski, L.; Rosen, B.
Synergistic interaction of glyceraldehydes-3-phosphate dehydrogenase and ArsJ, a novel organoarsenical efflux permease, confers arsenate resistance
Mol. Microbiol.
100
945-953
2016
Pseudomonas aeruginosa (A0A071L3D0)
brenda
Nemeti, B.; Csanaky, I.; Gregus, Z.
Effect of an inactivator of glyceraldehyde-3-phosphate dehydrogenase, a fortuitous arsenate reductase, on disposition of arsenate in rats
Toxicol. Sci.
90
49-60
2006
Rattus norvegicus
brenda
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