| salicylate 1-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.1 | ||||||||
| CAS no. | 9059-28-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a salicylate 1-monooxygenase (EC 1.14.13.1) is an enzyme that catalyzes the chemical reaction
- salicylate + NADH + 2 H+ + O2 catechol + NAD+ + H2O + CO2
The 4 substrates of this enzyme are salicylate, NADH, H+, and O2, whereas its 4 products are catechol, NAD+, H2O, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. This enzyme participates in 3 metabolic pathways: 1- and 2-methylnaphthalene degradation, naphthalene and anthracene degradation, and fluorene degradation. It employs one cofactor, FAD.
Nomenclature
The systematic name of this enzyme class is salicylate,NADH:oxygen oxidoreductase (1-hydroxylating, decarboxylating).
Other names in common use include:
- salicylate hydroxylase,
- salicylate 1-hydroxylase,
- salicylate monooxygenase, and
- salicylate hydroxylase (decarboxylating)
References
- Suzuki K, Takemori S, Katagiri M (1969). "Mechanism of the salicylate hydroxylase reaction. IV. Fluorimetric analysis of the complex formation". Biochim. Biophys. Acta. 191: 77–85. doi:10.1016/0005-2744(69)90316-7.
- Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M (1969). "Mechanism of the salicylate hydroxylase reaction. II. The enzyme-substrate complex". Biochim. Biophys. Acta. 191 (1): 58–68. doi:10.1016/0005-2744(69)90314-3. PMID 4898626.
- Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M (1969). "Mechanism of the salicylate hydroxylase reaction. 3 Characterization and reactivity of chemically or photochemically reduced enzyme-flavin". Biochim. Biophys. Acta. 191 (1): 69–76. doi:10.1016/0005-2744(69)90315-5. PMID 4309912.
- Yamamoto S, Katagiri M, Maeno H, Hayaishi O (1965). "Salicylate hydroxylase, a monooxygenase requiring flavin adenine dinucleotide". J. Biol. Chem. 240: 3408–3413. PMID 14321380.
This page was last edited on 23 January 2024, at 08:39