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Literature summary extracted from

  • Riebe, O.; Fischer, R.J.; Bahl, H.
    Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductase (2007), FEBS Lett., 581, 5605-5610.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.2 expression in Escherichia coli Clostridium acetobutylicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.15.1.2 reduced rubredoxin + superoxide + H+ Clostridium acetobutylicum desulfoferrodoxin is the key factor in the superoxide reductase dependent part of an alternative pathway for detoxification of reactive oxygen species in this obligate anaerobic bacterium rubredoxin + H2O2
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?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Clostridium acetobutylicum Q97GB9 ATCC824, gene cac2450
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 reduced rubredoxin + superoxide + H+ desulfoferrodoxin is the key factor in the superoxide reductase dependent part of an alternative pathway for detoxification of reactive oxygen species in this obligate anaerobic bacterium Clostridium acetobutylicum rubredoxin + H2O2
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?
1.15.1.2 reduced rubredoxin + superoxide + H+ desulfoferrodoxin functions as a superoxide reductase Clostridium acetobutylicum rubredoxin + H2O2
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?

Synonyms

EC Number Synonyms Comment Organism
1.15.1.2 desulfoferrodoxin
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Clostridium acetobutylicum
1.15.1.2 Dfx
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Clostridium acetobutylicum
1.15.1.2 SOR
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Clostridium acetobutylicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.15.1.2 reduced rubredoxin rubredoxin is reduced by ferredoxin:NADP+ reductase from spinach and NADPH Clostridium acetobutylicum