Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
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+
-
-
-
?
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin
glycerate 3-phosphate + H+ + reduced ferredoxin
additional information
?
-
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
-
?
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
-
-
-
?
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
-
-
-
?
glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin
glycerate 3-phosphate + H+ + reduced ferredoxin
-
-
-
?
glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin
glycerate 3-phosphate + H+ + reduced ferredoxin
-
-
-
?
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
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
deletion of either subunit results in a distinct growth phenotype on both C5 and C6 sugars, with an increased lag phase, but higher cell densities. GOR functions in parallel with the conventional glyceraldehyde-3-phosphate dehydrogenase
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.
physiological function
-
deletion of either subunit results in a distinct growth phenotype on both C5 and C6 sugars, with an increased lag phase, but higher cell densities. GOR functions in parallel with the conventional glyceraldehyde-3-phosphate dehydrogenase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.; Schnheit, 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)
brenda
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
brenda
Scott, I.M.; Rubinstein, G.M.; Poole, F.L.; Lipscomb, G.L.; Schut, G.J.; Williams-Rhaesa, A.M.; Stevenson, D.M.; Amador-Noguez, D.; Kelly, R.M.; Adams, M.W.W.
The thermophilic biomass-degrading bacterium Caldicellulosiruptor bescii utilizes two enzymes to oxidize glyceraldehyde 3-phosphate during glycolysis
J. Biol. Chem.
294
9995-10005
2019
Caldicellulosiruptor bescii (B9MQI2 and B9MQI1), Caldicellulosiruptor bescii DSM 6725 (B9MQI2 and B9MQI1)
brenda
Hagedoorn, P.L.
Steady-state kinetics of the tungsten containing aldehyde ferredoxin oxidoreductases from the hyperthermophilic archaeon Pyrococcus furiosus
J. Biotechnol.
306
142-148
2019
Pyrococcus furiosus (Q8U3K2), Pyrococcus furiosus
brenda