Pyridoxine 4-oxidase
| pyridoxine 4-oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.3.12 | ||||||||
| CAS no. | 37250-82-1 | ||||||||
| 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, pyridoxine 4-oxidase (EC 1.1.3.12) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are pyridoxine and oxygen. Its products are pyridoxal and hydrogen peroxide.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyridoxine:oxygen 4-oxidoreductase. Other names in common use include pyridoxin 4-oxidase, and pyridoxol 4-oxidase. This enzyme participates in vitamin B6 metabolism. It employs one cofactor, FAD.
References
- ^ Enzyme 1.1.3.12 at KEGG Pathway Database.
- ^ Sundaram TK, Snell EE (1969). "The bacterial oxidation of vitamin B6. V. The enzymatic formation of pyridoxal and isopyridoxal from pyridoxine". J. Biol. Chem. 244 (10): 2577–84. doi:10.1016/S0021-9258(18)83439-1. PMID 5769992.