Tryptophan 2'-dioxygenase
| tryptophan 2'-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.99.3 | ||||||||
| CAS no. | 64295-81-4 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a tryptophan 2'-dioxygenase (EC 1.13.99.3) is an enzyme that catalyzes the chemical reaction
2 + H+
(indol-3-yl)glycolaldehyde + CO
2 + NH+
4
Thus, the 3 substrates of this enzyme are L-tryptophan, O
2 and H+
, whereas its 3 products are (indol-3-yl)glycolaldehyde, CO
2, and NH+
4.
Classification
[edit]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 O miscellaneous.
Nomenclature
[edit]The systematic name of this enzyme class is L-tryptophan:oxygen 2'-oxidoreductase (side-chain-cleaving). Other names in common use include indole-3-alkane alpha-hydroxylase, tryptophan side-chain alpha,beta-oxidase, tryptophan side chain oxidase II, tryptophan side-chain oxidase, TSO, indolyl-3-alkan alpha-hydroxylase, tryptophan side chain oxidase type I, TSO I, TSO II, and tryptophan side chain oxidase.
Biological role
[edit]This enzyme participates in tryptophan metabolism. It employs one cofactor, heme.
References
[edit]- Roberts J, Rosenfeld HJ (1977). "Isolation, crystallization, and properties of indolyl-3-alkane alpha-hydroxylase. A novel tryptophan-metabolizing enzyme". J. Biol. Chem. 252 (8): 2640–7. PMID 15994.
- Takai K, Ushiro H, Noda Y, Narumiya S, Tokuyama T (1977). "Crystalline hemoprotein from Pseudomonas that catalyzes oxidation of side chain of tryptophan and other indole derivatives". J. Biol. Chem. 252 (8): 2648–56. PMID 15995.
