Pyridoxal kinase
| Pyridoxal kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| EC no. | 2.7.1.35 | ||||||||
| CAS no. | 9026-42-0 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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Pyridoxal kinase (EC 2.7.1.35) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from liver converts pyridoxal to the active form of vitamin B6, pyridoxal phosphate (pyridoxal 5' phosphate), by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). A number of other phosphate acceptors can be used in place of pyridoxal to produce the corresponding 5' phosphate, including pyridoxine, pyridoxamine and various derivatives. The 5'-phosphates of pyridoxine and pyridoxamine can be converted to pyridoxal 5'-phosphate by pyridoxine 5′-phosphate oxidase.[1][2]
This enzyme is a transferase, specifically one 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.[3] This enzyme participates in vitamin B6 metabolism.
Humans have one version of this enzyme encoded by the gene PDXK.
Structural studies
As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1LHP, PDB: 1LHR, PDB: 1RFT, PDB: 1RFU, PDB: 1RFV, PDB: 1TD2, PDB: 1VI9, PDB: 1YGJ, PDB: 1YGK, PDB: 1YHJ, PDB: 2AJP, PDB: 2DDM, PDB: 2DDO, PDB: 2DDW, and PDB: 2F7K.
References
- ↑ McCormick DB, Gregory ME, Snell EE (1961). "Pyridoxal phosphokinases. I. Assay, distribution, purification, and properties". J. Biol. Chem. 236 (7): 2076–2084. doi:10.1016/S0021-9258(18)64132-8. PMID 13773826.
- ↑ Trufanov AF; Krisanova JA. "Biosynthesis of pyridoxal phosphate by liver sections of rat in vitro". Byull. Eksp. Biol. Med. 22: 40–43.
- ↑ Enzyme 2.7.1.35 at KEGG Pathway Database.
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