Catechol 2,3-dioxygenase

Enzyme

Catechol 2,3-dioxygenase

Catechol 2,3-dioxygenase tetramer, Pseudomonas alkylphenolica

Identifiers
EC no.| 1.13.11.2
CAS no.| 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
| Search

PMC| articles
PubMed| articles
NCBI| proteins

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 ⇌ {\displaystyle \rightleftharpoons } 2-hydroxymuconate semialdehyde

This enzyme contains Fe(II).

## References

[edit]

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 (8): 2223–8\. doi:10.1016/S0021-9258(18)64061-X. PMID 13757654.
5. ^ Nozaki M, Kagamiyama H, Hayaishi O (1963). "Metapyrocatechase. I. Purification, Crystallization and Some Properties". Biochemische Zeitschrift. 338: 582–90\. PMID 14087325.

## External links

[edit]

* Catechol+2,3-dioxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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Oxidoreductases: monooxygenases (EC 1.13)

1.13.11: two atoms of oxygen|

* lipoxygenase: Arachidonate 5-lipoxygenase
* Arachidonate 12-lipoxygenase/ALOX12
* Arachidonate 8-lipoxygenase
* Arachidonate 15-lipoxygenase/ALOX15
* Linoleate 11-lipoxygenase

* other dioxygenase: Catechol dioxygenase
* Homogentisate 1,2-dioxygenase
* Cysteine dioxygenase
* 4-Hydroxyphenylpyruvate dioxygenase
* Indoleamine 2,3-dioxygenase
* Chlorite dismutase

1.13.12: one atom of oxygen|

* Firefly luciferase

1.13.99: other|

* Inositol oxygenase

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

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