2,6-dihydroxypyridine 3-monooxygenase
| 2,6-dihydroxypyridine 3-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.10 | ||||||||
| CAS no. | 39279-38-4 | ||||||||
| 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 | ||||||||
| |||||||||
2,6-dihydroxypyridine 3-monooxygenase (EC 1.14.13.10) is an enzyme that catalyzes the chemical reaction
The four substrates of this enzyme are 2,6-dihydroxypyridine, reduced nicotinamide adenine dinucleotide (NADH), oxygen, and a proton. Its products are 2,3,6-trihydroxypyridine, oxidised NAD+, and water.[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. The systematic name of this enzyme class is 2,6-dihydroxypyridine,NADH:oxygen oxidoreductase (3-hydroxylating). This enzyme is also called 2,6-dihydroxypyridine oxidase.[1] It uses flavin adenine dinucleotide as a cofactor.[4]
References
- ^ a b Enzyme 1.14.13.10 at KEGG Pathway Database.
- ^ Holmes PE, Rittenberg SC (1972). "The bacterial oxidation of nicotine. VII. Partial purification and properties of 2,6-dihydroxypyridine oxidase". J. Biol. Chem. 247 (23): 7622–7. doi:10.1016/S0021-9258(19)44570-5. PMID 4344227.
- ^ Holmes PE, Rittenberg SC, Knackmuss HJ (1972). "The bacterial oxidation of nicotine. 8. Synthesis of 2,3,6-trihydroxypyridine and accumulation and partial characterization of the product of 2,6-dihydroxypyridine oxidation". J. Biol. Chem. 247 (23): 7628–33. doi:10.1016/S0021-9258(19)44571-7. PMID 4636328.
- ^ Montersino, Stefania; Tischler, Dirk; Gassner, George T.; Van Berkel, Willem J. H. (2011). "Catalytic and Structural Features of Flavoprotein Hydroxylases and Epoxidases". Advanced Synthesis & Catalysis. 353 (13): 2301–2319. doi:10.1002/adsc.201100384.