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Literature summary for 1.2.7.5 extracted from

  • Das, S.K.; Biswas, D.; Maiti, R.; Sarkar, S.
    Modeling the tungsten sites of inactive and active forms of hyperthermophilic Pyrococcus furiosus aldehyde ferredoxin oxidoreductase (1996), J. Am. Chem. Soc., 118, 1387-1397.
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of the 3 different cofactor model complexes: 1. [Et4N]2[WVIO(1,2-dicyanoethylenedithiolate)2], 2. [Et4N]2[WIVO(1,2-dicyanoethylenedithiolate)2], and 3. [Et4N]2[WVIO(S2)(1,2-dicyanoethylenedithiolate)2], X-ray structure determination and analysis Pyrococcus furiosus

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum part of a tungsten-molybdopterin cofactor Pyrococcus furiosus
Tungsten part of a tungsten-molybdopterin cofactor Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
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hyperthermophilic archaeon
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
an aldehyde + H2O + oxidized ferredoxin
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Pyrococcus furiosus an acid + H+ + reduced ferredoxin
-
ir
additional information enzyme shows an active and an inactive form Pyrococcus furiosus ?
-
?

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
Pyrococcus furiosus
tungsten-molybdopterin modeling of the tungsten sites of inactive and active enzyme forms Pyrococcus furiosus