Catechol 2,3-dioxygenase

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Catechol 2,3-dioxygenase
Catechol 2,3-dioxygenase tetramer, Pseudomonas alkylphenolica
Identifiers
EC no.1.13.11.2
CAS no.9029-46-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

Catechol 2,3-dioxygenase (EC 1.13.11.2, 2,3-pyrocatechase, catechol 2,3-oxygenase, catechol oxygenase, metapyrocatechase, pyrocatechol 2,3-dioxygenase) is an enzyme with systematic name catechol:oxygen 2,3-oxidoreductase (decyclizing).[1][2][3][4][5] This enzyme catalyses the following chemical reaction

catechol + O2 2-hydroxymuconate semialdehyde

This enzyme contains Fe(II).

References

  1. ^ Junker F, Field JA, Bangerter F, Ramsteiner K, Kohler HP, Joannou CL, Mason JR, Leisinger T, Cook AM (June 1994). "Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid". The Biochemical Journal. 300 ( Pt 2) (2): 429–36. doi:10.1042/bj3000429. PMC 1138180. PMID 8002948.
  2. ^ Junker F, Leisinger T, Cook AM (July 1994). "3-Sulphocatechol 2,3-dioxygenase and other dioxygenases (EC 1.13.11.2 and EC 1.14.12.-) in the degradative pathways of 2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic acids in Alcaligenes sp. strain O-1". Microbiology. 140 ( Pt 7) (7): 1713–22. doi:10.1099/13500872-140-7-1713. PMID 8075807.
  3. ^ Hayaishi O, Lardy H, Myrbäck K (1963). "Direct oxygenation by O2, oxygenases". In Boyer PD (ed.). The Enzymes. Vol. 8 (2nd ed.). New York: Academic Press. pp. 353–371.
  4. ^ Kojima Y, Itada N, Hayaishi O (August 1961). "Metapyrocatachase: a new catechol-cleaving enzyme". The Journal of Biological Chemistry. 236: 2223–8. PMID 13757654.
  5. ^ Nozaki M, Kagamiyama H, Hayaishi O (1963). "Metapyrocatechase. I. Purification, Crystallization and Some Properties". Biochemische Zeitschrift. 338: 582–90. PMID 14087325.

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