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Literature summary for 1.13.11.2 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
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas putida

General Stability

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

Metals/Ions

Metals/Ions Comment Organism Structure
Iron
-
 Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-
Pseudomonas putida mt2
-
-
-

Oxidation Stability

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

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Pseudomonas putida

Renatured (Commentary)

Renatured (Comment) Organism
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

Subunits Comment Organism
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

Synonyms Comment Organism
XylE
-
 Pseudomonas putida