Catechol 2,3-dioxygenase

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
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
Search
PMCarticles
PubMedarticles
NCBIproteins

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.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.