Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • 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 (1998), J. Biol. Chem., 273, 28149-28154.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.7.6 additional information enzyme is induced during glycolysis Pyrococcus furiosus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.7.6 DNA sequence determination and analysis Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.7.6 Fe2+ enzyme contains iron-sulfur cluster Pyrococcus furiosus
1.2.7.6 Tungsten single tungsten environment is afforded for the reaction Pyrococcus furiosus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.7.6 56000
-
 gel filtration Pyrococcus furiosus
1.2.7.6 64000
-
 1 * 64000, SDS-PAGE Pyrococcus furiosus
1.2.7.6 74000
-
 sequence determination Pyrococcus furiosus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.7.6 D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin Pyrococcus furiosus enzyme is a site for glycolytic regulation 3-phospho-D-glycerate + H+ + reduced ferredoxin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.7.6 Pyrococcus furiosus Q8U3K2
-
-
1.2.7.6 Pyrococcus furiosus Q8U3K2 hyperthermophilic archaeon
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.7.6 35fold, about 95% purity Pyrococcus furiosus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.7.6 D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + 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 Pyrococcus furiosus
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.7.6 25
-
 purified enzyme Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.7.6 D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen artificial electron acceptor Pyrococcus furiosus 3-phospho-D-glycerate + H+ + reduced benzyl viologen
-
 ?
1.2.7.6 D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
-
 Pyrococcus furiosus 3-phospho-D-glycerate + H+ + reduced ferredoxin
-
 ?
1.2.7.6 D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin enzyme is a site for glycolytic regulation Pyrococcus furiosus 3-phospho-D-glycerate + H+ + reduced ferredoxin
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.7.6 monomer 1 * 64000, SDS-PAGE Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
1.2.7.6 glyceraldehyde-3-phosphate ferredoxin oxidoreductase
-
 Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.7.6 50
-
 assay at Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.7.6 8
-
 assay at Pyrococcus furiosus

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.7.6 Ferredoxin dependent on Pyrococcus furiosus