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Information on EC 1.2.7.6 - glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
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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
-
hyperthermophilic
- furiosus
- archaeon
-
embden-meyerhof
- tungsten
- formaldehyde
-
tungsten-containing
-
adp-dependent
- 3-phosphoglycerate
-
adp-forming
-
gluconeogenic
- glucokinase
-
nonphosphorylating
- 6-phosphofructokinase
- aerophilum
-
methanococcus
- pterin
- maripaludis
- thermococcus
-
tungstoenzymes
-
phosphoglucose
-
volcanic
-
pyrobaculum
- degradation
-
continental
- eucarya
-
ferredoxin-dependent
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
Synonyms
aldehyde ferredoxin oxidoreductase, dehydrogenase, glyceraldehyde phosphate (ferredoxin), G3P:ferredoxin oxidoreductase, GAP:FdOR, GAPOR, glyceraldehyde 3-phosphate ferredoxin oxidoreductase, glyceraldehyde 3-phosphate oxidoreductase, glyceraldehyde phosphate dehydrogenase (ferredoxin), glyceraldehyde-3-phosphate Fd oxidoreductase, glyceraldehyde-3-phosphate ferredoxin oxidoreductase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldehyde ferredoxin oxidoreductase
dehydrogenase, glyceraldehyde phosphate (ferredoxin)
-
-
-
-
G3P:ferredoxin oxidoreductase
GAPOR
glyceraldehyde phosphate dehydrogenase (ferredoxin)
-
-
-
-
glyceraldehyde-3-phosphate Fd oxidoreductase
-
-
-
-
glyceraldehyde-3-phosphate ferredoxin oxidoreductase
glyceraldehyde-3-phosphate ferredoxin reductase
-
-
-
-
glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
PAE1029
GAPOR
-
-
-
-
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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
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
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
electron transfer, mechanism and reduction potential
-
D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
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.
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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 ferredoxin
3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
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 methyl viologen
3-phospho-D-glycerate + reduced methyl viologen + H+
-
-
-
?
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
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
-
-
-
-
?
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
-
-
-
?
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
-
-
-
?
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
only GAPOR catalyzes D-glyceraldehyde-3-phosphate oxidation, catalysis under autotrophic conditions
-
-
ir
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
is highly specific for glyceraldehyde-3-phosphate
-
-
?
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
-
artificial electron acceptor
-
?
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
-
artificial electron acceptor
-
?
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
artificial electron acceptor
-
?
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
-
-
-
?
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
-
-
-
-
ir
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
-
-
-
?
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
-
-
?
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
-
might have a glycolytic role and functions in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase
-
?
additional information
?
-
-
does not use glyceraldehyde, acetaldehyde or formaldehyde as substrates
-
-
?
additional information
?
-
does not use glyceraldehyde, acetaldehyde or formaldehyde as substrates
-
-
?
additional information
?
-
-
enzyme shows high specificity for glyceraldehyde-3-phosphate and does not use glyceraldehyde, acetaldehyde or formaldehyde
-
-
?
additional information
?
-
enzyme shows high specificity for glyceraldehyde-3-phosphate and does not use glyceraldehyde, acetaldehyde or formaldehyde
-
-
?
additional information
?
-
enzyme shows high specificity for glyceraldehyde-3-phosphate and does not use glyceraldehyde, acetaldehyde or formaldehyde
-
-
?
additional information
?
-
-
no activity with NAD(P)+ as electron acceptor
-
-
?
additional information
?
-
-
no activity with NAD(P)+ as electron acceptor
-
-
?
additional information
?
-
-
no activity with formaldehyde, propionaldehyde, phenylacetaldehyde, butyraldehyde, crotonaldehyde, acetaldehyde, dihydroxyacetone phosphate, glyceraldehyde, benzaldehyde, glucose, glucose 6-phosphate, or glyoxylate
-
-
?
additional information
?
-
-
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 + 2 oxidized ferredoxin
3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
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
-
-
-
-
?
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
-
-
-
-
ir
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
enzyme is a site for glycolytic regulation
-
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
-
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
molybdopterin
content of Mo-GAPOR expressed in Escherichia coli strain BL21(DE3) is estimated to be 0.35 g-atoms per mol of protein
additional information
GAPOR obtained from cells grown in medium containing tungsten and molybdenum or in medium without added tungsten and molybdenum do not display any activity
-
additional information
-
GAPOR obtained from cells grown in medium containing tungsten and molybdenum or in medium without added tungsten and molybdenum do not display any activity
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Mo5+
molybdenum can in be incorporated, Mo(V) signal is observed in electron paramagnetic resonance
S2-
Mo-GAPOR expressed in Escherichia coli strain BL21(DE3) is estimated to contain 6.1 g-atoms of acid-labile sulfide per mol of protein
Tungsten
Tungsten
-
0.85 tungsten g-atoms per mol of enzyme, part of a tungsten-molybdopterin cofactor
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-Glyceraldehyde-3-phosphate
recombinant GAPOR is posttranscriptionally regulated as it exhibits pronounced and irreversible substrate inhibition. Inhibition is independent of benzyl viologen
O2
reversibly inactivates GAPOR purified from M9/Mo+ cultures. GAPOR activity of crude lysates is irreversibly inactivated
Dithionite
-
50% inhibition at 3 mM, pH 8.0; O2-scavenger; reversible by 70%
additional information
addition of 0.001 mM AMP, NADH, or NADPH has no effect on GAPOR activity
-
additional information
-
addition of 0.001 mM AMP, NADH, or NADPH has no effect on GAPOR activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
isopropyl-beta-D-thiogalactopyranoside
1 mM induces cultures at the exponential phase of growth
L-cysteine
reversibly activates GAPOR purified from M9/Mo+ cultures
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.28
D-glyceraldehyde 3-phosphate
-
cosubstrate: benzyl viologen, 50°C, pH not specified in the publication
0.028
D-Glyceraldehyde-3-phosphate
-
with ferredoxin as electron acceptor, pH 8.4, 70°C
0.043
D-Glyceraldehyde-3-phosphate
-
with benzyl viologen as electron acceptor, pH 8.4, 70°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.07
-
substrate: D-glyceraldehyde 3-phosphate (cosubstrate: benzyl viologen), 50°C, pH not specified in the publication, enzyme from starch-grown cells
1.8
maximum specific activity of protein for Mo-GAPOR expressed in Escherichia coli strain BL21(DE3)
120
Mo-GAPOR purified from Escherichia coli strain Rosetta-gami 2(DE3)
17
25
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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
50
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
specific activity is 10fold higher in starch-grown cells than in lactate-grown cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
metabolism
extracts of maltose/yeast extract/nitrate-grown cells contain all enzyme activities of a modified Embden-Meyerhof pathway, including ATP-dependent glucokinase, phosphoglucose isomerase, ATP-dependent 6-phosphofructokinase, fructose-1,6-phosphate aldolase, triose-phosphate isomerase, glyceraldehyde-3-phosphate ferredoxin oxidoreductase, phosphoglycerate mutase, enolase and pyruvate kinase
metabolism
-
extracts of maltose/yeast extract/nitrate-grown cells contain all enzyme activities of a modified Embden-Meyerhof pathway, including ATP-dependent glucokinase, phosphoglucose isomerase, ATP-dependent 6-phosphofructokinase, fructose-1,6-phosphate aldolase, triose-phosphate isomerase, glyceraldehyde-3-phosphate ferredoxin oxidoreductase, phosphoglycerate mutase, enolase and pyruvate kinase
-
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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). GAPOR_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
653
0
73948
Swiss-Prot
-
E8R8U8_DESM0
Desulfurococcus mucosus (strain ATCC 35584 / DSM 2162 / JCM 9187 / O7/1)
654
0
73957
TrEMBL
-
A4WHD7_PYRAR
Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)
616
0
69367
TrEMBL
-
A3DPV6_STAMF
Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)
658
0
75595
TrEMBL
-
G4RM55_THETK
Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)
625
0
70495
TrEMBL
-
A4FXX8_METM5
Methanococcus maripaludis (strain C5 / ATCC BAA-1333)
613
0
70911
TrEMBL
-
A1RTV9_PYRIL
Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)
619
0
69887
TrEMBL
-
A0A7R9N0X8_9EURY
629
0
70617
TrEMBL
-
D5U0S7_THEAM
Thermosphaera aggregans (strain DSM 11486 / M11TL)
651
0
73868
TrEMBL
-
A0A564Q2U5_9EURY
73
0
7903
TrEMBL
-
S0FU45_9DELT
629
0
71244
TrEMBL
-
H6QD48_PYROT
Pyrobaculum oguniense (strain DSM 13380 / JCM 10595 / TE7)
616
0
69475
TrEMBL
-
A3MTX3_PYRCJ
Pyrobaculum calidifontis (strain JCM 11548 / VA1)
629
0
70612
TrEMBL
-
A0A7R9R4X6_9EURY
629
0
70525
TrEMBL
-
Q8ZXY6_PYRAE
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
622
0
69912
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
70000
70000
PAE1029, represents the GAPOR encoding gene gapor, sequence analysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
100
retains 70% of its activity upon incubation for 2 h (half-life, 500 min)
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aerobic conditions: loss of about 50% activity in cell extract after 12 h at 23°C
-
644692
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
pET46-Ek/LIC-GAPOR vector expressed in Escherichia coli strains BL21(DE3) or Rosetta-gami 2(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
degradation
Pyrobaculum aerophilum contains a modified Embden-Meyerhof pathway, in which GAPOR replaces the GAPDH/phosphoglycerate kinase couple of the conventional EmbdenâMeyerhof pathway
degradation
the major physiological role of GAPOR in Methanococcus maripaludis most likely involves only nonoptimal growth conditions
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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
brenda
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
brenda
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
brenda
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
brenda
Reher, M.; Gebhard, S.; Schoenheit, P.
Glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) and nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN), key enzymes of the respective modified Embden-Meyerhof pathways in the hyperthermophilic crenarchaeota Pyrobaculum aerophi and Aeropyrum pernix
FEMS Microbiol. Lett.
273
196-205
2007
Pyrobaculum aerophilum, Pyrobaculum aerophilum (Q8ZXY6), no activity in Aeropyrum pernix, Pyrobaculum aerophilum DSM 7523 (Q8ZXY6)
brenda
Park, M.O.; Mizutani, T.; Jones, P.R.
Glyceraldehyde-3-phosphate ferredoxin oxidoreductase from Methanococcus maripaludis
J. Bacteriol.
189
7281-7289
2007
Methanococcus maripaludis (A4FXX8), Methanococcus maripaludis
brenda
Labes, A.; Schoenheit, P.
Sugar utilization in the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324: starch degradation to acetate and CO2 via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
Arch. Microbiol.
176
329-338
2001
Archaeoglobus fulgidus, Archaeoglobus fulgidus 7324
brenda
Solomons, J.T.; Johnsen, U.; Schönheit, P.; Davies, C.
3-Phosphoglycerate is an allosteric activator of pyruvate kinase from the hyperthermophilic archaeon Pyrobaculum aerophilum
Biochemistry
52
5865-5875
2013
Pyrobaculum aerophilum
brenda
Costa, K.C.; Lie, T.J.; Jacobs, M.A.; Leigh, J.A.
H2-independent growth of the hydrogenotrophic methanogen Methanococcus maripaludis
mBio
4
e00062-13
2013
Methanococcus maripaludis, Methanococcus maripaludis MM901
brenda
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)
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