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Literature summary for 1.13.11.2 extracted from

  • Takemori, S.; Komiyama, T.; Katagiri, M.
    Apo- and reconstituted holoenzymes of metapyrocatechase from Pseudomonas putida (1971), Eur. J. Biochem., 23, 178-184.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ activity is closely related to specific content of iron in this protein Pseudomonas putida
Fe2+ 3 gatom of iron per mol of enzyme Pseudomonas putida

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
140000
-
gel filtration Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
T-2
-
Pseudomonas putida T-2
-
T-2
-

Storage Stability

Storage Stability Organism
4°C, over a month, without loss of activity, crystals of holoenzyme in the presence of acetone Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
catechol + O2
-
Pseudomonas putida 2-hydroxymuconate semialdehyde
-
?
catechol + O2
-
Pseudomonas putida T-2 2-hydroxymuconate semialdehyde
-
?