Pyridoxal kinase
| pyridoxal kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.35 | ||||||||
| CAS no. | 9026-42-0 | ||||||||
| 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 pyridoxal kinase (EC 2.7.1.35) is an enzyme that catalyzes the chemical reaction
- ATP + pyridoxal ADP + pyridoxal 5'-phosphate
Thus, the two substrates of this enzyme are ATP and pyridoxal, whereas its two products are ADP and pyridoxal 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:pyridoxal 5'-phosphotransferase. Other names in common use include pyridoxal kinase (phosphorylating), pyridoxal 5-phosphate-kinase, pyridoxal phosphokinase, and pyridoxine kinase. This enzyme participates in vitamin B6 metabolism.
Structural studies
As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes 1LHP, 1LHR, 1RFT, 1RFU, 1RFV, 1TD2, 1VI9, 1YGJ, 1YGK, 1YHJ, 2AJP, 2DDM, 2DDO, 2DDW, and 2F7K.
References
- McCormick DB, Gregory ME, Snell EE (1961). "Pyridoxal phosphokinases. I. Assay, distribution, purification, and properties". J. Biol. Chem. 236: 2076–2084. PMID 13773826.
- Trufanov AF; Krisanova JA. "Biosynthesis of pyridoxal phosphate by liver sections of rat in vitro". Byull. Eksp. Biol. Med. 22: 40–43.
