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Literature summary for 1.13.11.2 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

Inhibitors Comment Organism Structure
m-phenanthroline
-
Pseudomonas putida
o-Nitrophenol
-
Pseudomonas putida

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
Pseudomonas putida

Organic Solvent Stability

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

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
ATCC 23973
-

Reaction

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

Substrates and Products (Substrate)

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