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Literature summary extracted from

  • Hugo, N.; Armengaud, J.; Gaillard, J.; Timmis, K.N.; Jouanneau, Y.
    A novel -2Fe-2S- ferredoxin from Pseudomonas putida mt2 promotes the reductive reactivation of catechol 2,3-dioxygenase. (1998), J. Biol. Chem., 273, 9622-9629.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.2 expression in Escherichia coli Pseudomonas putida

General Stability

EC Number General Stability Organism
1.13.11.2 25°C, half-life of 69 min in air, 37°C, half-life of 70 min in argon Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.2 Iron
-
 Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.2 Pseudomonas putida
-
-
-
1.13.11.2 Pseudomonas putida mt2
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.13.11.2 25°C, half-life of 69 min in air, 37°C, half-life of 70 min in argon Pseudomonas putida

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.2 recombinant protein Pseudomonas putida

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.13.11.2 inactivation of XylE enzyme by 4-methylcatechol results in oxidation of the active site iron to a high spin ferric state. Soluble [2Fe-2S] ferredoxin protein XylT reactivates XylE through reduction of the iron atom in the active site of the enzyme. XylE reactivation involves catalytic nonstoichiometric amounts of XylT Pseudomonas putida

Subunits

EC Number Subunits Comment Organism
1.13.11.2 More interaction of inactive enzyme with soluble [2Fe-2S] ferredoxin protein XylT for reactivation through reduction of the iron atom in the active site of the enzyme Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
1.13.11.2 XylE
-
 Pseudomonas putida