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Literature summary for 1.2.7.5 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

Metals/Ions Comment Organism Structure
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
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]

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

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus furiosus

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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