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Literature summary extracted from

  • Katagiri, M.
    Early years of oxygenase research in Bethesda, Osaka, Urbana, and Kanazawa (2005), Biochem. Biophys. Res. Commun., 338, 285-289.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.14.13.1 loses its activity after ammonium sulfate fractionation and dialysis, and its full activity is restored by the addition of a heat-stable factor of rat liver Pseudomonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.1 57000
-
SDS-PAGE Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.1 Pseudomonas sp.
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.1 salicylate + NADH + H+ + O2
-
Pseudomonas sp. catechol + NAD+ + H2O + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.1 salicylate hydroxylase
-
Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.1 FAD 0.9 molecules of FAD bound to one molecule of enzyme Pseudomonas sp.
1.14.13.1 NADH
-
Pseudomonas sp.