Pyridoxal kinase is an enzyme that in humans is encoded by the PDXKgene.[1][2]
The protein encoded by this gene phosphorylates vitamin B6, a step required for the conversion of vitamin B6 to pyridoxal-5-phosphate, an important cofactor in intermediary metabolism. The encoded protein is cytoplasmic and probably acts as a homodimer. Alternatively spliced transcript variants have been described, but their biological validity has not been determined.[2]
References
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Zhang Z, Smith E, Surowiec SM, et al. (1993). "Synthesis of N-(4'-pyridoxyl)sphingosine and its uptake and metabolism by isolated cells". Membrane biochemistry. 10 (1): 53–9. doi:10.3109/09687689309150252. PMID8510562.
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Lee HS, Moon BJ, Choi SY, Kwon OS (2001). "Human pyridoxal kinase: overexpression and properties of the recombinant enzyme". Mol. Cells. 10 (4): 452–9. PMID10987144.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Shin JH, Weitzdoerfer R, Fountoulakis M, Lubec G (2004). "Expression of cystathionine beta-synthase, pyridoxal kinase, and ES1 protein homolog (mitochondrial precursor) in fetal Down syndrome brain". Neurochem. Int. 45 (1): 73–9. doi:10.1016/j.neuint.2003.12.004. PMID15082224.
Fang X, Zhou ZM, Lu L, et al. (2004). "Expression of a novel pyridoxal kinase mRNA splice variant, PKH-T, in human testis". Asian J. Androl. 6 (2): 83–91. PMID15154080.
Wang L, Zhu YF, Guo XJ, et al. (2006). "A two-dimensional electrophoresis reference map of human ovary". J. Mol. Med. 83 (10): 812–21. doi:10.1007/s00109-005-0676-y. PMID16021519.
Flanagan JM, Beutler E (2006). "The genetic basis of human erythrocyte pyridoxal kinase activity variation". Haematologica. 91 (6): 801–4. PMID16704963.