PDXK

PDXK
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2AJP, 2F7K, 2YXT, 2YXU, 3FHX, 3FHY, 3KEU, 4EN4, 4EOH
Identifiers
Aliases	PDXK , C21orf124, C21orf97, HEL-S-1a, PKH, PNK, PRED79, pyridoxal (pyridoxine, vitamin B6) kinase, pyridoxal kinase, HMSN6C
External IDs	OMIM: 179020 MGI: 1351869 HomoloGene: 2731 GeneCards: PDXK
Gene location (Human)
Chr.	Chromosome 21 (human)
End	43,762,307 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	78,300,809 bp
RNA expression pattern
	Top expressed in
	sperm; ; renal medulla; ; anterior pituitary; ; Brodmann area 23; ; Brodmann area 46; ; nucleus accumbens; ; postcentral gyrus; ; Region I of hippocampus proper; ; minor salivary gland; ; inferior olivary nucleus;
	Top expressed in
	entorhinal cortex; ; nucleus accumbens; ; motor neuron; ; superior colliculus; ; morula; ; conjunctival fornix; ; hypothalamus; ; submandibular gland; ; corneal stroma; ; supraoptic nucleus;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity ; nucleotide binding ; protein homodimerization activity ; pyridoxal kinase activity ; zinc ion binding ; potassium ion binding ; sodium ion binding ; metal ion binding ; kinase activity ; lithium ion binding ; pyridoxal phosphate binding ; ATP binding ; magnesium ion binding ;
Cellular component	cytosol ; extracellular exosome ; nucleus ; extracellular region ; cytoplasm ; secretory granule lumen ; specific granule lumen ; nucleoplasm ;
Biological process	pyridoxal phosphate biosynthetic process ; phosphorylation ; pyridoxal 5'-phosphate salvage ; cell population proliferation ; neutrophil degranulation ; vitamin B6 metabolic process ;
	Sources:Amigo / QuickGO
Orthologs
	8566
	216134
	ENSG00000160209
	ENSMUSG00000032788
	O00764
	Q8K183
	NM_003681 ; NM_021941 ; NM_001331030
	NM_172134
	NP_001317959 ; NP_003672
	NP_742146
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 12, 2024

Pyridoxal kinase is an enzyme that in humans is encoded by the PDXK gene.^[5]^[6]

The protein encoded by this gene phosphorylates vitamin B ₆, 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.^[6]

Related Research Articles

<span class="mw-page-title-main">Pyridoxal phosphate</span> Active form of vitamin B6

Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B₆, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates.

Pyridoxine 5′-phosphate oxidase is an enzyme, encoded by the PNPO gene, that catalyzes several reactions in the vitamin B₆ metabolism pathway. Pyridoxine 5′-phosphate oxidase catalyzes the final, rate-limiting step in vitamin B₆ metabolism, the biosynthesis of pyridoxal 5′-phosphate, the biologically active form of vitamin B₆ which acts as an essential cofactor. Pyridoxine 5′-phosphate oxidase is a member of the enzyme class oxidases, or more specifically, oxidoreductases. These enzymes catalyze a simultaneous oxidation-reduction reaction. The substrate oxidase enzymes is hydroxlyated by one oxygen atom of molecular oxygen. Concurrently, the other oxygen atom is reduced to water. Even though molecular oxygen is the electron acceptor in these enzymes' reactions, they are unique because oxygen does not appear in the oxidized product.

Serine/threonine-protein kinase D2 or PKD2 is an enzyme that in humans is encoded by the PRKD2 gene.

Choline kinase alpha is an enzyme that in humans is encoded by the CHKA gene.

55 kDa erythrocyte membrane protein is a protein that in humans is encoded by the MPP1 gene.

Serine/threonine-protein kinase PLK2 is an enzyme that in humans is encoded by the PLK2 gene.

Stanniocalcin-2 is a protein that in humans is encoded by the STC2 gene.

Gamma-adducin is a protein that in humans is encoded by the ADD3 gene.

Dual specificity protein kinase CLK3 is an enzyme that in humans is encoded by the CLK3 gene. The CLK3 gene encodes a serine/threonine type protein kinase with a non-conserved N-terminal domain. A long and short isoform result from alternative splicing and coexist in different tissues. Isoform phclk3/152 lacks the kinase domain.

Serine/threonine-protein kinase PCTAIRE-3 is an enzyme that in humans is encoded by the CDK18 gene.

Fructosamine-3-kinase is an enzyme that in humans is encoded by the FN3K gene.

Protein kinase C and casein kinase substrate in neurons protein 3 is an enzyme that in humans is encoded by the PACSIN3 gene.

CDP-diacylglycerol—inositol 3-phosphatidyltransferase is an enzyme that in humans is encoded by the CDIPT gene.

Glutaredoxin-3 is a protein that in humans is encoded by the GLRX3 gene.

Ubiquitin-conjugating enzyme E2 R2 is a protein that in humans is encoded by the UBE2R2 gene.

Pantothenate kinase 4 is an enzyme that in humans is encoded by the PANK4 gene.

Zinc finger protein 7 is a protein that in humans is encoded by the ZNF7 gene.

Ketosamine-3-kinase is an enzyme that in humans is encoded by the FN3KRP (fructosamine-3-kinase-related-protein) gene.

Pyruvate kinase PKLR is an enzyme that in humans is encoded by the PKLR gene.

Probable lysosomal cobalamin transporter is a protein that in humans is encoded by the LMBRD1 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000160209 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032788 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
1 2 "Entrez Gene: PDXK pyridoxal (pyridoxine, vitamin B₆) kinase".

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. PMC 1684914 . PMID 2009.
Merrill AH, Henderson JM, Wang E, et al. (1984). "Metabolism of vitamin B-6 by human liver". J. Nutr. 114 (9): 1664–74. doi:10.1093/jn/114.9.1664. 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. Bibcode:2000Natur.405..311H. doi: 10.1038/35012518 . PMID 10830953.
Lee HS, Moon BJ, Choi SY, et al. (2001). "Human pyridoxal kinase: overexpression and properties of the recombinant enzyme". Mol. Cells. 10 (4): 452–9. doi:10.1016/S1016-8478(23)17501-7. 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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
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, et al. (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. S2CID 20620865.
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.
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. S2CID 6644433.
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.
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.
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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000160209 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032788 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9099727-5] 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.

[entrez-6] 1 2 "Entrez Gene: PDXK pyridoxal (pyridoxine, vitamin B₆) kinase".

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PDXK

Related Research Articles

References

Further reading