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Information on EC 1.2.7.6 - glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) and Organism(s) Pyrococcus furiosus and UniProt Accession Q8U3K2
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1.2.7.6 glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)IUBMB Comments
Contains tungsten-molybdopterin and iron-sulfur clusters. This enzyme is thought to function in place of glyceralde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus . It is specific for glyceraldehyde-3-phosphate.
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Word Map
- 1.2.7.6
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hyperthermophilic
- furiosus
- archaeon
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embden-meyerhof
- tungsten
- formaldehyde
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tungsten-containing
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adp-dependent
- 3-phosphoglycerate
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gluconeogenic
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nonphosphorylating
- 6-phosphofructokinase
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adp-forming
- glucokinase
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ferredoxin-dependent
- pterin
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volcanic
- aerophilum
- maripaludis
- degradation
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methanococcus
- eucarya
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pyrobaculum
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tungstoenzymes
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continental
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phosphoglucose
- thermococcus
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Archaea, Bacteria
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
Synonyms
gapor, glyceraldehyde-3-phosphate ferredoxin oxidoreductase, glyceraldehyde-3-phosphate:ferredoxin oxidoreductase, gap:fdor, glyceraldehyde 3-phosphate ferredoxin oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, glyceraldehyde phosphate (ferredoxin)
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GAPOR
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glyceraldehyde phosphate dehydrogenase (ferredoxin)
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glyceraldehyde-3-phosphate Fd oxidoreductase
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glyceraldehyde-3-phosphate ferredoxin reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
this enzyme is thought to function in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhoff-type glycolytic pathway found in Pyrococcus furiosus. It is specific for glyceraldehyde-3-phosphate
D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
this enzyme is thought to function in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhoff-type glycolytic pathway found in Pyrococcus furiosus. It is specific for glyceraldehyde-3-phosphate
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D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
electron transfer, mechanism and reduction potential
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
Contains tungsten-molybdopterin and iron-sulfur clusters. This enzyme is thought to function in place of glyceralde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus [1]. It is specific for glyceraldehyde-3-phosphate.
CAS REGISTRY NUMBER
COMMENTARY
162995-20-2
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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 + H2O + 2 oxidized benzyl viologen
3-phospho-D-glycerate + 2 H+ + 2 reduced benzyl viologen
D-glyceraldehyde 3-phosphate is the only substrate oxidized by GAPOR, and the kinetics of the enzyme are unaffected by the presence of L-glyceraldehyde 3-phosphate
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-
?
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
artificial electron acceptor
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?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
D-glyceraldehyde-3-phosphate + H2O + oxidized methyl viologen
3-phospho-D-glycerate + reduced methyl viologen + H+
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-
-
?
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
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-
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
enzyme is a site for glycolytic regulation
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?
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
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artificial electron acceptor
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?
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
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artificial electron acceptor
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?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
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?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
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?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
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?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
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might have a glycolytic role and functions in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase
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?
additional information
?
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substrate glyceraldehyde-3-phosphate degrades at 60°C by non-enzymatic elimination of the phosphate group to methylglyoxal with a half-life of 6.5 min. Methylglyoxal is not a substrate or inhibitor of GAPOR
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additional information
?
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substrate glyceraldehyde-3-phosphate degrades at 60°C by non-enzymatic elimination of the phosphate group to methylglyoxal with a half-life of 6.5 min. Methylglyoxal is not a substrate or inhibitor of GAPOR
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additional information
?
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no activity with NAD(P)+ as electron acceptor
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?
additional information
?
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no activity with NAD(P)+ as electron acceptor
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?
additional information
?
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no activity with formaldehyde, propionaldehyde, phenylacetaldehyde, butyraldehyde, crotonaldehyde, acetaldehyde, dihydroxyacetone phosphate, glyceraldehyde, benzaldehyde, glucose, glucose 6-phosphate, or glyoxylate
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?
additional information
?
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no activity with formaldehyde, propionaldehyde, phenylacetaldehyde, butyraldehyde, crotonaldehyde, acetaldehyde, dihydroxyacetone phosphate, glyceraldehyde, benzaldehyde, glucose, glucose 6-phosphate, or glyoxylate
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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 + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
enzyme is a site for glycolytic regulation
-
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
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-
-
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
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might have a glycolytic role and functions in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mo5+
molybdenum can in be incorporated, Mo(V) signal is observed in electron paramagnetic resonance
Fe2+
Tungsten
Tungsten
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0.85 tungsten g-atoms per mol of enzyme, part of a tungsten-molybdopterin cofactor
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glyceraldehyde 3-phosphate
partial substrate inhibition, inhibition is alleviated completely by a 1M NaCl resulting in increased enzyme activity at high substrate concentrations
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
enzyme shows partial substrate inhibition, inhibition is alleviated completely by a 1M NaCl resulting in increased enzyme activity at high substrate concentrations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.028
D-Glyceraldehyde-3-phosphate
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with ferredoxin as electron acceptor, pH 8.4, 70°C
0.043
D-Glyceraldehyde-3-phosphate
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with benzyl viologen as electron acceptor, pH 8.4, 70°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
either of the two enzymes, ferredoxin-dependent glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) or NADP+-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN), involved in the modified Embden-Meyerhof glycolytic pathway can be deleted individually without impacting viability, albeit with differences in native fermentation product profiles. Pyrococcus furiosus is viable in the gluconeogenic direction (growth on pyruvate or peptides plus elemental sulfur) in a DAPOR/GAPN double deletion strain.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aerobic conditions: loss of about 50% activity in cell extract after 12 h at 23°C
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644692
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roy, R.; Menon, A.L.; Adams, M.W.W.
Aldehyde oxidoreductases from Pyrococcus furiosus
Methods Enzymol.
331
132-144
2001
Pyrococcus furiosus
Mukund, S.; Adams, M.W.
Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus
J. Biol. Chem.
270
8389-8392
1995
Pyrococcus furiosus
Hagedoorn, P.L.; Freije, J.R.; Hagen, W.R.
Pyrococcus furiosus glyceraldehyde 3-phosphate oxidoreductase has comparable W6+/5+ and W5+/4+ reduction potentials and unusual [4Fe-4S] EPR properties
FEBS Lett.
462
66-70
1999
Pyrococcus furiosus
van der Oost, J.; Schut, G.; Kengen, S.W.; Hagen, W.R.; Thomm, M.; de Vos, W.M.
The ferredoxin-dependent conversion of glyceraldehyde-3-phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation
J. Biol. Chem.
273
28149-28154
1998
Pyrococcus furiosus (Q8U3K2), Pyrococcus furiosus
Sevcenco, A.; Bevers, L.; Pinkse, M.; Krijger, G.; Wolterbeek, H.; Verhaert, P.; Hagen, W.; Hagedoorn, P.
Molybdenum incorporation in tungsten aldehyde oxidoreductase enzymes from Pyrococcus furiosus
J. Bacteriol.
192
4143-4152
2010
Pyrococcus furiosus (Q8U3K2)
Straub, C.T.; Schut, G.; Otten, J.K.; Keller, L.M.; Adams, M.W.W.; Kelly, R.M.
Modification of the glycolytic pathway in Pyrococcus furiosus and the implications for metabolic engineering
Extremophiles
24
511-518
2020
Pyrococcus furiosus (Q8U3K2), Pyrococcus furiosus
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