Pyridoxine 5-dehydrogenase
| pyridoxine 5-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.99.9 | ||||||||
| CAS no. | 9023-39-6 | ||||||||
| 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 5-dehydrogenase (EC 1.1.99.9) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are pyridoxine and an electron acceptor. Its products are isopyridoxal and the corresponding reduced acceptor.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is pyridoxine:acceptor 5-oxidoreductase. Other names in common use include pyridoxal-5-dehydrogenase, pyridoxol 5-dehydrogenase, pyridoxin 5-dehydrogenase, pyridoxine dehydrogenase, pyridoxine 5'-dehydrogenase, and pyridoxine:(acceptor) 5-oxidoreductase. This enzyme participates in vitamin B6 metabolism. It has 2 cofactors: FAD, and PQQ.
References
- ^ Enzyme 1.1.99.9 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.