Salicylate 1-monooxygenase
| 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 | ||||||||
| |||||||||
Salicylate 1-monooxygenase (EC 1.14.13.1) is an enzyme that catalyzes the chemical reaction
The four substrates of this enzyme are salicylic acid, reduced nicotinamide adenine dinucleotide (NADH), oxygen, and a proton, Its products are catechol, oxidised NAD+, water, and carbon dioxide.[1][2][3]
The enzyme is a flavin-containing monooxygenase that uses molecular oxygen as oxidant and incorporates one of its atoms into the starting material. This enzyme participates in metabolic pathways involving the degradation of naphthalene and anthracene and some of their derivatives. It uses flavin adenine dinucleotide as a cofactor.[4][5]
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
- ^ Enzyme 1.14.13.1 at KEGG Pathway Database.
- ^ Suzuki K, Takemori S, Katagiri M (1969). "Mechanism of the salicylate hydroxylase reaction. IV. Fluorimetric analysis of the complex formation". Biochim. Biophys. Acta. 191 (1): 77–85. doi:10.1016/0005-2744(69)90316-7. PMID 4390441.
- ^ 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 (8): 3408–3413. doi:10.1016/S0021-9258(18)97232-7. PMID 14321380.