|Gene:||gor||Accession Number: G-9179 (MetaCyc)|
Synonyms: glyceraldehyde 3-phosphate oxidoreductase
Species: Pyrococcus furiosus
In bacteria and eukaryotes, this reaction is catalyzed by two enzymes, NAD-dependent glyceraldehyde-3-phosphate dehydrogenase and the ATP-generating phosphoglycerate kinase. In Pyrococcus furiosus this enzyme catalyzes the reaction in one step, independent of phosphate. It is responsible for the lack of net ATP production during the oxidation of glucose to pyruvate by Pyrococcus furiosus [Verhees03]. As a result no NAD(P)H is formed and only ferredoxin serves as the electon acceptor in glycolysis [Schut07]. The reason for this is the presence of a membrane bound hydrogenase (MBH) which uses reduced ferredoxin to evolve H2 and generate ATP via a proton motive force in Pyrococcus furiosus [Sapra03].
The enzyme is a member of the aldehyde oxidoreductase family of tungsten-containing enzymes [Verhees03]. It contains a tungsten atom (W), a [4Fe-4S] cluster and a molybdopterin. The tungsten is thought to be present as a tungstopterin center [Mukund95, Roy01, Hagedoorn99]. The molecular mass was determined by SDS-PAGE [Mukund95].
Gene Citations: [vanderOost98]
Molecular Weight of Polypeptide: 73.851 kD (from nucleotide sequence), 63 kD (experimental) [Mukund95 ]
Unification Links: Entrez:AAC70892
Relationship Links: Entrez-Nucleotide:PART-OF:U74298
Enzymatic reaction of: glyceraldehyde-3-phosphate ferredoxin oxidoreductase
EC Number: 220.127.116.11
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
This reaction is reversible.
In Pathways: glycolysis V (Pyrococcus)
The Km value for glyceraldehyde-3-phosphate was determined at 70 deg. C using Pyrococcus furiosus ferredoxin as electron carrier. The enzyme is highly substrate-specific [Mukund95, Roy01, Hagedoorn99].
Hagedoorn99: Hagedoorn PL, Freije JR, Hagen WR (1999). "Pyrococcus furiosus glyceraldehyde 3-phosphate oxidoreductase has comparable W(6+/5+) and W(5+/4+) reduction potentials and unusual [4Fe-4S] EPR properties." FEBS Lett 462(1-2);66-70. PMID: 10580093
Mukund95: Mukund S, Adams MW (1995). "Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus." J Biol Chem 1995;270(15);8389-92. PMID: 7721730
Park06: Park YJ, Yoo CB, Choi SY, Lee HB (2006). "Purifications and characterizations of a ferredoxin and its related 2-oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon, Sulfolobus solfataricus P1." J Biochem Mol Biol 39(1);46-54. PMID: 16466637
Schut07: Schut GJ, Bridger SL, Adams MW (2007). "Insights into the metabolism of elemental sulfur by the hyperthermophilic archaeon Pyrococcus furiosus: characterization of a coenzyme A- dependent NAD(P)H sulfur oxidoreductase." J Bacteriol 189(12);4431-41. PMID: 17449625
vanderOost98: van der Oost J, Schut G, Kengen SW, Hagen WR, Thomm M, de Vos WM (1998). "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(43);28149-54. PMID: 9774434
Verhees03: Verhees CH, Kengen SW, Tuininga JE, Schut GJ, Adams MW, De Vos WM, Van Der Oost J (2003). "The unique features of glycolytic pathways in Archaea." Biochem J 375(Pt 2);231-46. PMID: 12921536
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