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Literature summary extracted from

  • Hori, K.; Hashimoto, T.; Nozaki, M.
    Kinetic studies on the reaction mechanism of dioxygenases (1973), J. Biochem., 74, 375-384.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.2 m-phenanthroline
-
 Pseudomonas putida
1.13.11.2 o-Nitrophenol
-
 Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.2 0.0025
-
 catechol
-
 Pseudomonas putida
1.13.11.2 0.009
-
 O2
-
 Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.2 Fe2+
-
 Pseudomonas putida

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.13.11.2 2-mercaptoethanol no significant protection of the enzyme from inactivation Pseudomonas putida
1.13.11.2 Acetone protects enzyme almost completely from inactivation by air Pseudomonas putida
1.13.11.2 Ethanol protects enzyme almost completly from inactivation by air Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.2 Pseudomonas putida
-
 ATCC 23973
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.2 catechol + O2 = 2-hydroxymuconate-6-semialdehyde ordered bi uni mechanism Pseudomonas putida
a

Substrates and Products (Substrate)

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