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Literature summary extracted from

  • Kita, A.; Kita, S.; Fujisawa, I.; Inaka, K.; Ishida, T.; Horiike, K.; Nozaki, M.; Miki, K.
    An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2 (1999), Structure Fold. Des., 7, 25-34.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.2
-
 Pseudomonas putida mt-2

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.2 Fe2+ the active site comprises three Fe2+ ligands His153, His214 and Glu265 Pseudomonas putida mt-2

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.2 catechol + O2 Pseudomonas putida mt-2 key role in the degradation of aromatic molecules 2-hydroxymuconate semialdehyde
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.2 Pseudomonas putida mt-2 P23103
-
-

Reaction

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.2 catechol + O2
-
 Pseudomonas putida mt-2 2-hydroxymuconate semialdehyde
-
 ?
1.13.11.2 catechol + O2 key role in the degradation of aromatic molecules Pseudomonas putida mt-2 2-hydroxymuconate semialdehyde
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.11.2 homotetramer with each subunit folded into two similar domains Pseudomonas putida mt-2