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Literature summary 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)

EC Number Crystallization (Comment) Organism
1.2.7.5 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

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

Organism

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

Substrates and Products (Substrate)

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

Cofactor

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