1.2.7.6: glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
This is an abbreviated version!
For detailed information about glyceraldehyde-3-phosphate dehydrogenase (ferredoxin), go to the full flat file.
Word Map on EC 1.2.7.6
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1.2.7.6
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hyperthermophilic
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furiosus
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archaeon
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embden-meyerhof
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tungsten
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formaldehyde
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tungsten-containing
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adp-dependent
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3-phosphoglycerate
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gluconeogenic
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nonphosphorylating
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6-phosphofructokinase
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adp-forming
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glucokinase
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ferredoxin-dependent
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pterin
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volcanic
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aerophilum
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maripaludis
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degradation
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methanococcus
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eucarya
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pyrobaculum
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tungstoenzymes
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continental
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phosphoglucose
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thermococcus
- 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
Reaction
Synonyms
aldehyde ferredoxin oxidoreductase, Athe_0820, Athe_0821, 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, glyceraldehyde-3-phosphate ferredoxin reductase, glyceraldehyde-3-phosphate:Fd-OR, glyceraldehyde-3-phosphate:ferredoxin oxidoreductase, Gor, PAE1029, PF0464
ECTree
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Substrates Products
Substrates Products on EC 1.2.7.6 - glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
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REACTION DIAGRAM
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 + 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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glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin
glycerate 3-phosphate + H+ + reduced 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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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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3-phospho-D-glycerate + H+ + reduced benzyl viologen
only GAPOR catalyzes D-glyceraldehyde-3-phosphate oxidation, catalysis under autotrophic conditions
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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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?
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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glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
B9MQI2; B9MQI1
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glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin
glycerate 3-phosphate + H+ + reduced ferredoxin
B9MQI2; B9MQI1
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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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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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