Catechol 2,3-dioxygenase

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Catechol 2,3-dioxygenase
Identifiers
EC number 1.13.11.2
CAS number 9029-46-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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

Degradation of catechol.svg
catechol + O2 2-hydroxymuconate semialdehyde

This enzyme contains Fe(II).

References[edit]

  1. ^ Junker, F.; Field, J.A.; Bangerter, F.; Ramsteiner, K.; Kohler, H.-P.; Joannou, C.L.; Mason, J.R.; Leisinger, T.; Cook, A.M. (1994). "Dioxygenation and spontaneous deamination of 2-aminobenzene sulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid". Biochem. J. 300: 429–436. PMC 1138180Freely accessible. PMID 8002948. 
  2. ^ Junker, F.; Leisinger, T.; Cook, A.M. (1994). "3-Sulphocatechol dioxygenase and other dioxygenases (1.13.11.2 and 1.14.12.-) in the degradative pathways of 2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic acids in Alcaligenes sp. strain O-1". J. Gen. Microbiol. 140: 1713–1722. doi:10.1099/13500872-140-7-1713. PMID 8075807. 
  3. ^ Hayaishi, O.; Lardy, H.; Myrbäck, K. (1963). "Direct oxygenation by O2, oxygenases". In Boyer, P.D. The Enzymes. 8 (2nd ed.). New York: Academic Press. pp. 353–371. 
  4. ^ Kojima, Y.; Itada, N.; Hayaishi, O. (1961). "Metapyrocatechase: a new catechol-cleaving enzyme". J. Biol. Chem. 236: 2223–2228. PMID 13757654. 
  5. ^ Nozaki, M.; Kagamiyama, H.; Hayaishi, O. (1963). "Metapyrocatechase. I. Purification, crystallization and some properties". Biochem. Z. 338: 582–590. PMID 14087325. 

External links[edit]