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EC Tree
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.
The expected taxonomic range for this enzyme is: Archaea, Bacteria
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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aldehyde ferredoxin oxidoreductase
dehydrogenase, glyceraldehyde phosphate (ferredoxin)
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G3P:ferredoxin oxidoreductase
glyceraldehyde 3-phosphate ferredoxin oxidoreductase
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glyceraldehyde 3-phosphate oxidoreductase
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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 oxidoreductase
glyceraldehyde-3-phosphate ferredoxin reductase
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glyceraldehyde-3-phosphate:Fd-OR
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glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
aldehyde ferredoxin oxidoreductase
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aldehyde ferredoxin oxidoreductase
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G3P:ferredoxin oxidoreductase
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G3P:ferredoxin oxidoreductase
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GAPOR
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glyceraldehyde-3-phosphate ferredoxin oxidoreductase
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glyceraldehyde-3-phosphate ferredoxin oxidoreductase
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glyceraldehyde-3-phosphate ferredoxin oxidoreductase
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glyceraldehyde-3-phosphate ferredoxin oxidoreductase
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glyceraldehyde-3-phosphate ferredoxin oxidoreductase
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glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
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glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
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glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
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PAE1029
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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
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
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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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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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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+
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?
additional information
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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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?
D-glyceraldehyde 3-phosphate + H2O + 2 oxidized ferredoxin
3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
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the enzyme is involved in the modified Embden-Meyerhof pathway
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?
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
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?
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
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?
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
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?
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
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ir
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
is highly specific for glyceraldehyde-3-phosphate
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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 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
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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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ir
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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?
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 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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does not use glyceraldehyde, acetaldehyde or formaldehyde as substrates
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additional information
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does not use glyceraldehyde, acetaldehyde or formaldehyde as substrates
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?
additional information
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enzyme shows high specificity for glyceraldehyde-3-phosphate and does not use glyceraldehyde, acetaldehyde or formaldehyde
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additional information
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enzyme shows high specificity for glyceraldehyde-3-phosphate and does not use glyceraldehyde, acetaldehyde or formaldehyde
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additional information
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enzyme shows high specificity for glyceraldehyde-3-phosphate and does not use glyceraldehyde, acetaldehyde or formaldehyde
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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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?
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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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the enzyme is involved in the modified Embden-Meyerhof pathway
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?
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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?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
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ir
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 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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?
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molybdopterin
content of Mo-GAPOR expressed in Escherichia coli strain BL21(DE3) is estimated to be 0.35 g-atoms per mol of protein
tungsto-bispterin cofactor
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Ferredoxin
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Ferredoxin
dependent on
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tungsten-molybdopterin
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tungstopterin center
tungsten-molybdopterin
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structure
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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additional information
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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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Mg2+
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contains 1 molecule per enzyme
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
Zn2+
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contains 2 molecules per enzyme
Fe2+
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Fe2+
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determination of the redox potential
Fe2+
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enzyme contains iron-sulfur cluster
Fe2+
enzyme contains iron-sulfur cluster
Fe2+
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1 [4Fe-4S]2+ cluster per enzyme molecule
Fe2+
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5-6 iron g-atoms per mol of enzyme
Tungsten
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1 tungsten center per molecule of enzyme
Tungsten
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determination of the redox potential
Tungsten
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0.85 tungsten g-atoms per mol of enzyme, part of a tungsten-molybdopterin cofactor
Tungsten
single tungsten environment is afforded for the reaction
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ATP
0.001-0.01 mM completely inhibits
crotonaldehyde
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25% inhibition at 10 mM
D-Glyceraldehyde-3-phosphate
recombinant GAPOR is posttranscriptionally regulated as it exhibits pronounced and irreversible substrate inhibition. Inhibition is independent of benzyl viologen
formaldehyde
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25% inhibition at 10 mM
glyceraldehyde-3-phosphate
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substrate inhibition above 0.5 mM
O2
reversibly inactivates GAPOR purified from M9/Mo+ cultures. GAPOR activity of crude lysates is irreversibly inactivated
Dithionite
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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
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additional information
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addition of 0.001 mM AMP, NADH, or NADPH has no effect on GAPOR activity
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2,3-bisphosphoglycerate
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stimulates
3-phosphoglycerate
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stimulates
acetyl phosphate
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stimulates
Ionic strength
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particularly by polyanions
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isopropyl-beta-D-thiogalactopyranoside
1 mM induces cultures at the exponential phase of growth
L-cysteine
reversibly activates GAPOR purified from M9/Mo+ cultures
maltose
stimulates about 4fold
potassium chloride
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3.5fold activation at 200 mM
potassium phosphate
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3.5fold activation at 200 mM
Sodium arsenate
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3.5fold activation at 200 mM
Sodium citrate
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3.5fold activation at 200 mM
Sodium sulfate
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3.5fold activation at 200 mM
Tungsten
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stimulates cell growth when added to the medium
additional information
enzyme is induced during glycolysis
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additional information
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enzyme is induced during glycolysis
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0.043 - 0.28
D-glyceraldehyde 3-phosphate
0.028 - 0.043
D-Glyceraldehyde-3-phosphate
1
Oxidized benzyl viologen
pH 7.8, 50°C
0.006
oxidized ferredoxin
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pH 8.4, 70°C
0.043
D-glyceraldehyde 3-phosphate
pH 7.8, 50°C
0.28
D-glyceraldehyde 3-phosphate
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cosubstrate: benzyl viologen, 50°C, pH not specified in the publication
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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0.043
D-Glyceraldehyde-3-phosphate
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with benzyl viologen as electron acceptor, pH 8.4, 70°C
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0.07
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substrate: D-glyceraldehyde 3-phosphate (cosubstrate: benzyl viologen), 50°C, pH not specified in the publication, enzyme from starch-grown cells
0.15
cell free extract, at 50°C
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)
additional information
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strictly anaerobic assay conditions
17
113fold purified, at 50°C, with a yield of 0.2%
25
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purified enzyme
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7.7
60% of maximum activity
8.3
60% of maximum activity
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50
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assay at
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brenda
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brenda
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no activity in Aeropyrum pernix
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brenda
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UniProt
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UniProt
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UniProt
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SwissProt
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hyperthermophilic archaeon
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hyperthermophilic archaeon
SwissProt
brenda
strain DSM 3638
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brenda
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specific activity is 10fold higher in starch-grown cells than in lactate-grown cells
brenda
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brenda
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physiological function
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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
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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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GAPOR_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
653
0
73948
Swiss-Prot
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A0A7J9PB81_METMI
613
0
70548
TrEMBL
-
A0A7J9P9K1_METMI
613
0
70874
TrEMBL
-
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
-
A0A7J9PSS9_METMI
613
0
70559
TrEMBL
-
A0A7J9P083_METMI
613
0
70709
TrEMBL
-
A0A7G2DAZ2_9EURY
652
0
73851
TrEMBL
-
A0A2L1C7Y5_METMI
613
0
70675
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
-
A0A401HPM6_9EURY
637
0
73956
TrEMBL
-
A0A0U3SF57_9EURY
659
0
75089
TrEMBL
-
A4FXX8_METM5
Methanococcus maripaludis (strain C5 / ATCC BAA-1333)
613
0
70911
TrEMBL
-
A5G4V6_GEOUR
Geobacter uraniireducens (strain Rf4)
623
0
70827
TrEMBL
-
A0A7J9NHF5_METMI
613
0
70534
TrEMBL
-
A1RTV9_PYRIL
Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)
619
0
69887
TrEMBL
-
V4JQX4_9CREN
654
0
72216
TrEMBL
-
A0A7R9N0X8_9EURY
629
0
70617
TrEMBL
-
A0A7J9NNT5_METMI
613
0
70925
TrEMBL
-
A0A7J9RZ19_METMI
613
0
70900
TrEMBL
-
A0A7J9S2A5_METMI
613
0
70680
TrEMBL
-
A0A7J9NTL5_METMI
613
0
70920
TrEMBL
-
D5U0S7_THEAM
Thermosphaera aggregans (strain DSM 11486 / M11TL)
651
0
73868
TrEMBL
-
A0A160VT44_9EURY
653
0
74057
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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63000
-
1 * 63000, SDS-PAGE
64000
1 * 64000, SDS-PAGE
65000
1 * 65000, SDS-PAGE
66000
1 * 66000, SDS-PAGE
74000
sequence determination
74089
tandem mass spectrometry
60000
-
gel filtration
70000
gel filtration
70000
PAE1029, represents the GAPOR encoding gene gapor, sequence analysis
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?
x * 74089, tandem mass spectrometry
monomer
gel filtration
monomer
1 * 65000, SDS-PAGE
monomer
1 * 66000, SDS-PAGE
monomer
-
1 * 66000, SDS-PAGE
-
monomer
-
1 * 63000, SDS-PAGE
monomer
1 * 64000, SDS-PAGE
monomer
-
1 * 73000, SDS-PAGE
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7.7 - 8.3
60% activity at pH 7.7 and 8.3
692377
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100
retains 70% of its activity upon incubation for 2 h (half-life, 500 min)
100
2 h, 70% residual activity
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aerobic conditions: loss of about 50% activity in cell extract after 12 h at 23°C
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644692
O2-sensitive, t1/2 at 23°C: 6 h
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644691
sensitive against O2
-
644692
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-20°C, Tris-HCl buffer, pH 9, several weeks
23°C, under argon, 12 h, no loss of activity in cell extract
-
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30fold, under strictly anaerobic conditions
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by gel filtration, 113fold, to homogeneity
to more than 75% homogeneity, by gel filtration
-
-
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DNA sequence determination and analysis
pET46-Ek/LIC-GAPOR vector expressed in Escherichia coli strains BL21(DE3) or Rosetta-gami 2(DE3)
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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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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
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Pyrococcus furiosus (Q8U3K2), Pyrococcus furiosus
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Methanococcus maripaludis (A4FXX8), Methanococcus maripaludis
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Methanococcus maripaludis, Methanococcus maripaludis MM901
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Pyrococcus furiosus (Q8U3K2)
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