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 | ||||||||
| |||||||||
In enzymology, a 2,6-dihydroxypyridine 3-monooxygenase (EC 1.14.13.10) is an enzyme that catalyzes the chemical reaction
- 2,6-dihydroxypyridine + NADH + H+ + O2 2,3,6-trihydroxypyridine + NAD+ + H2O
The 4 substrates of this enzyme are 2,6-dihydroxypyridine, NADH, H+, and O2, whereas its 3 products are 2,3,6-trihydroxypyridine[1], NAD+, and H2O.
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. 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. It has 2 cofactors: FAD, and Flavoprotein.
References[edit]
- 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. 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. PMID 4636328.
