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Enzyme Nomenclature
Information on EC 1.2.7.6 - glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
for references in articles please use BRENDA:EC1.2.7.6
Word Map on EC 1.2.7.6
- 1.2.7.6
-
hyperthermophilic
- furiosus
- archaeon
-
embden-meyerhof
- tungsten
- formaldehyde
-
glycolytic
-
adp-dependent
-
tungsten-containing
- 6-phosphofructokinase
-
nonphosphorylating
- 3-phosphoglycerate
-
adp-forming
- glucokinase
- aerophilum
- degradation
- pterin
- thermococcus
-
extant
-
phosphoglucose
-
methanococcus
- eucarya
-
continental
-
pyrobaculum
-
tungstoenzymes
- molybdenum
-
volcanic
-
gluconeogenic
- maripaludis
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Specify your search results
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
1.2.7.6
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RECOMMENDED NAME
GeneOntology No.
glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
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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
electron transfer, mechanism and reduction potential
-
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
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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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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 + 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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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q8U3K2
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+
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
Fe2+
-
1 [4Fe-4S]2+ cluster per enzyme molecule; 5-6 iron g-atoms per mol of enzyme
Fe2+
-
5-6 iron g-atoms per mol of enzyme; enzyme contains iron-sulfur cluster
Fe2+
-
1 [4Fe-4S]2+ cluster per enzyme molecule; determination of the redox potential
Tungsten
-
0.85 tungsten g-atoms per mol of enzyme, part of a tungsten-molybdopterin cofactor
Tungsten
-
1 tungsten center per molecule of enzyme; determination of the redox potential
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INHIBITORS
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)
17
113fold purified, at 50°C, with a yield of 0.2%; pH 7.8, 50°C
25
120
Mo-GAPOR purified from Escherichia coli strain Rosetta-gami 2(DE3)
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
specific activity is 10fold higher in starch-grown cells than in lactate-grown cells
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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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SUBUNITS
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
2 h, 70% residual activity; 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 Embden–Meyerhof pathway
degradation
the major physiological role of GAPOR in Methanococcus maripaludis most likely involves only nonoptimal growth conditions
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.7.6)
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