pyridoxine 5-dehydrogenase | |||||||||
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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 | ||||||||
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In enzymology, a pyridoxine 5-dehydrogenase (EC 1.1.99.9) is an enzyme that catalyzes the chemical reaction
- pyridoxine + acceptor isopyridoxal + reduced acceptor
Thus, the two substrates of this enzyme are pyridoxine and acceptor, whereas its two products are isopyridoxal and reduced acceptor.
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.
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Vitamin B6: Pyridoxal Phosphate
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Transamination reaction mechanism
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Protein / Amino Acid Metabolism (Part 3 of 8) - Transamination Reactions and Aminotransferases
Transcription
References
- 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. PMID 5769992.