PDXK

Pyridoxal (pyridoxine, vitamin B6) kinase
PDB rendering based on 2ajp.
Available structures PDB 2AJP, 2F7K, 2YXT, 2YXU, 3FHX, 3FHY, 3KBI, 3KEU
Identifiers
Symbols	PDXK; C21orf124; C21orf97; DKFZp566A071; FLJ31940; FLJ37311; MGC15873; MGC31754; MGC52346; PKH; PNK
External IDs	OMIM: 179020 MGI: 1351869 HomoloGene: 2731 GeneCards: PDXK Gene
EC number	2.7.1.35
Gene Ontology Molecular function • nucleotide binding • magnesium ion binding • ATP binding • zinc ion binding • pyridoxal kinase activity • pyridoxal kinase activity • transferase activity • pyridoxal phosphate binding • potassium ion binding • sodium ion binding • lithium ion binding • protein homodimerization activity Cellular component • cytoplasm • cytosol • cytosol Biological process • vitamin metabolic process • water-soluble vitamin metabolic process • cell proliferation • pyridoxal 5'-phosphate salvage • vitamin B6 metabolic process • vitamin B6 metabolic process • pyridoxal phosphate biosynthetic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8566	216134
Ensembl	ENSG00000160209	ENSMUSG00000032788
UniProt	O00764	Q8K183
RefSeq (mRNA)	NM_003681	NM_172134.2
RefSeq (protein)	NP_003672	NP_742146.1
Location (UCSC)	Chr 21: 45.14 – 45.19 Mb	Chr 10: 77.9 – 77.93 Mb
PubMed search	[1]	[2]

Pyridoxal kinase is an enzyme that in humans is encoded by the PDXK gene.^[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

1. ^ Hanna MC, Turner AJ, Kirkness EF (May 1997). "Human pyridoxal kinase. cDNA cloning, expression, and modulation by ligands of the benzodiazepine receptor". J Biol Chem 272 (16): 10756–60. doi:10.1074/jbc.272.16.10756. PMID 9099727. 
2. ^ ^{a b} "Entrez Gene: PDXK pyridoxal (pyridoxine, vitamin B₆) kinase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8566. 

Further reading

• Chern CJ, Beutler E (1976). "Biochemical and electrophoretic studies of erythrocyte pyridoxine kinase in white and black Americans". Am. J. Hum. Genet. 28 (1): 9–17. doi:10.1155/2009/308985. PMC 1684914. PMID 2009. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1684914. 
• Merrill AH, Henderson JM, Wang E et al. (1984). "Metabolism of vitamin B-6 by human liver". J. Nutr. 114 (9): 1664–74. PMID 6088736. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• 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. PMID 8510562. 
• Lainé-Cessac P, Cailleux A, Allain P (1997). "Mechanisms of the inhibition of human erythrocyte pyridoxal kinase by drugs". Biochem. Pharmacol. 54 (8): 863–70. doi:10.1016/S0006-2952(97)00252-9. PMID 9354586. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Hattori M, Fujiyama A, Taylor TD et al. (2000). "The DNA sequence of human chromosome 21". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953. 
• 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. PMID 10987144. 
• Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. PMID 14702039. 
• 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. PMID 15082224. 
• 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. PMID 15154080. 
• Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. PMID 16021519. 
• Kimura K, Wakamatsu A, Suzuki Y et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 
• Flanagan JM, Beutler E (2006). "The genetic basis of human erythrocyte pyridoxal kinase activity variation". Haematologica 91 (6): 801–4. PMID 16704963. 
• Hu YH, Warnatz HJ, Vanhecke D et al. (2006). "Cell array-based intracellular localization screening reveals novel functional features of human chromosome 21 proteins". BMC Genomics 7: 155. doi:10.1186/1471-2164-7-155. PMC 1526728. PMID 16780588. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1526728. 
• Musayev FN, di Salvo ML, Ko TP et al. (2007). "Crystal Structure of human pyridoxal kinase: Structural basis of M+ and M2+ activation". Protein Sci. 16 (10): 2184–94. doi:10.1110/ps.073022107. PMC 2204131. PMID 17766369. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2204131.