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Pyridoxal kinase

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(Redirected from Pyridoxine phosphokinase)
pyridoxal kinase
Identifiers
EC no.2.7.1.35
CAS no.9026-42-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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. 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.

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.

Humans have one version of this enzyme encoded by the gene PDXK.

Structural studies

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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

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  • 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.