Tryptophan alpha,beta-oxidase
| tryptophan alpha,beta-oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.3.10 | ||||||||
| CAS no. | 156859-19-7 | ||||||||
| 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, tryptophan alpha,beta-oxidase (EC 1.3.3.10) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-tryptophan and oxygen. Its products are α,β-didehydrotryptophan and hydrogen peroxide.[1][2][3]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is L-tryptophan:oxygen alpha,beta-oxidoreductase. Other names in common use include L-tryptophan 2',3'-oxidase, and L-tryptophan alpha,beta-dehydrogenase. It employs one cofactor, heme.
References
- ^ Enzyme 1.3.3.10 at KEGG Pathway Database.
- ^ Genet R, Denoyelle C, Menez A (1994). "Purification and partial characterization of an amino acid alpha,beta- dehydrogenase, L-tryptophan 2',3'-oxidase from Chromobacterium violaceum". J. Biol. Chem. 269 (27): 18177–84. doi:10.1016/S0021-9258(17)32432-8. PMID 8027079.
- ^ Genet R, Benetti PH, Hammadi A, Menez A (1995). "L-tryptophan 2',3'-oxidase from Chromobacterium violaceum. Substrate specificity and mechanistic implications". J. Biol. Chem. 270 (40): 23540–5. doi:10.1074/jbc.270.40.23540. PMID 7559518.