In enzymology, a 2,3-dihydroxyindole 2,3-dioxygenase (EC 1.13.11.23) is an enzyme that catalyzes the chemical reaction
| 2,3-dihydroxyindole 2,3-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.11.23 | ||||||||
| CAS no. | 37256-62-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- 2,3-dihydroxyindole + O2 anthranilate + CO2
Thus, the two substrates of this enzyme are 2,3-dihydroxyindole and O2, whereas its two products are anthranilate and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 2,3-dihydroxyindole:oxygen 2,3-oxidoreductase (decyclizing). This enzyme participates in tryptophan metabolism.
References
edit- Fujioka M, Wada H (1968). "The bacterial oxidation of indole". Biochim. Biophys. Acta. 158 (1): 70–8. doi:10.1016/0304-4165(68)90073-1. PMID 5652436.
