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Literature summary extracted from

  • Arendsen, A.F.; de Vocht, M.; Bulsink, Y.B.M.; Hagen, W.R.
    Redox chemistry of biological tungsten: an EPR study of the aldehyde oxidoreductase from Pyrococcus furiosus (1996), Chemistry, 1, 292-296.
No PubMed abstract available

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.7.5 Iron each subunit carries one [4Fe-4S] cubane and a novel tungsten cofactor containing two pterins. A single iron atom bridges between the subunits. The active-site redox chemistry is based on the pterin part of the cofactor Pyrococcus furiosus
1.2.7.5 Tungsten each subunit carries one [4Fe-4S] cubane and a novel tungsten cofactor containing two pterins. A single iron atom bridges between the subunits Pyrococcus furiosus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.7.5 80000
-
 2 * 80000, SDS-PAGE Pyrococcus furiosus
1.2.7.5 110000
-
 gel filtration Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
1.2.7.5 Pyrococcus furiosus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.7.5
-
 Pyrococcus furiosus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.7.5 10
-
 65°C, pH not specified in the publication Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.7.5 crotonaldehyde + H2O + oxidized ferredoxin
-
 Pyrococcus furiosus crotonate + reduced ferredoxin
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.7.5 homodimer 2 * 80000, SDS-PAGE Pyrococcus furiosus