Tryptophan 2-monooxygenase
| Tryptophan 2-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.12.3 | ||||||||
| CAS no. | 37256-65-8 | ||||||||
| 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 | ||||||||
| |||||||||
Tryptophan 2-monooxygenase (EC 1.13.12.3) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-tryptophan and oxygen. Its products are 3-indoleacetamide, carbon dioxide, and water.[1][2][3]
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 with incorporation of one atom of oxygen (internal monooxygenases o internal mixed-function oxidases). The systematic name of this enzyme class is L-tryptophan:oxygen 2-oxidoreductase (decarboxylating). This enzyme participates in tryptophan metabolism, especially in plants, where the product amide can be converted to the auxin hormone indole-3-acetic acid.[1]
Like other similar enzymes which use oxygen to cleave amino acids, this is a flavoprotein.[4] Others include lysine 2-monooxygenase[5] and arginine 2-monooxygenase.[6]
References
- ^ a b Enzyme 1.13.12.3 at KEGG Pathway Database.
- ^ Kosuge T, Heskett MG, Wilson EE (1966). "Microbial synthesis and degradation of indole-3-acetic acid. I. The conversion of L-tryptophan to indole-3-acetamide by an enzyme system from Pseudomonas savastanoi". J. Biol. Chem. 241 (16): 3738–44. PMID 5916389.
- ^ Kuo, TT; Kosuge T (1969). "Factors influencing the production and further metabolism of indole-3-acetic acid by Pseudomonas savastanoi". J. Gen. Appl. Microbiol. 15: 51–63. doi:10.2323/jgam.15.51.
- ^ Emanuele, John J.; Fitzpatrick, Paul F. (1995). "Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 1. Kinetic mechanism". Biochemistry. 34 (11): 3710–3715. doi:10.1021/bi00011a028. PMID 7893667.
- ^ Nakazawa, Teruko; Hori, Kazuko; Hayaishi, Osamu (1972). "Studies on Monooxygenases". Journal of Biological Chemistry. 247 (11): 3439–3444. doi:10.1016/S0021-9258(19)45160-0.
- ^ Olomucki, A.; Pho, D.B; Lebar, R.; Delcambe, L.; Thoai, N.V (1968). "Arginine oxygenase decarboxylante". Biochimica et Biophysica Acta (BBA) - Enzymology. 151 (2): 353–366. doi:10.1016/0005-2744(68)90102-2. PMID 4295160.