ADK (gene)

Adenosine kinase, also known as ADK, is a human gene.cite web | title = Entrez Gene: ADK adenosine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=132| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes adenosine kinase, an abundant enzyme in mammalian tissues. The enzyme catalyzes the transfer of the gamma-phosphate from ATP to adenosine, thereby serving as a regulator of concentrations of both extracellular adenosine and intracellular adenine nucleotides. Adenosine has widespread effects on the cardiovascular, nervous, respiratory, and immune systems and inhibitors of the enzyme could play an important pharmacological role in increasing intravascular adenosine concentrations and acting as anti-inflammatory agents. Alternative splicing results in two transcript variants encoding different isoforms. Both isoforms of the enzyme phosphorylate adenosine with identical kinetics and both require Mg2+ for activity.cite web | title = Entrez Gene: ADK adenosine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=132| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Klobutcher LA, Nichols EA, Kucherlapati RS, Ruddle FH |title=Assignment of the gene for human adenosine kinase to chromosome 10 using a somatic cell hybrid clone panel. |journal=Cytogenet. Cell Genet. |volume=16 |issue= 1-5 |pages= 171–4 |year= 1976 |pmid= 185014 |doi=
*cite journal | author=Spychala J, Datta NS, Takabayashi K, "et al." |title=Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and fructokinases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 3 |pages= 1232–7 |year= 1996 |pmid= 8577746 |doi=
*cite journal | author=Singh B, Hao W, Wu Z, "et al." |title=Cloning and characterization of cDNA for adenosine kinase from mammalian (Chinese hamster, mouse, human and rat) species. High frequency mutants of Chinese hamster ovary cells involve structural alterations in the gene. |journal=Eur. J. Biochem. |volume=241 |issue= 2 |pages= 564–71 |year= 1997 |pmid= 8917457 |doi=
*cite journal | author=McNally T, Helfrich RJ, Cowart M, "et al." |title=Cloning and expression of the adenosine kinase gene from rat and human tissues. |journal=Biochem. Biophys. Res. Commun. |volume=231 |issue= 3 |pages= 645–50 |year= 1997 |pmid= 9070863 |doi= 10.1006/bbrc.1997.6157
*cite journal | author=Mathews II, Erion MD, Ealick SE |title=Structure of human adenosine kinase at 1.5 A resolution. |journal=Biochemistry |volume=37 |issue= 45 |pages= 15607–20 |year= 1998 |pmid= 9843365 |doi= 10.1021/bi9815445
*cite journal | author=Van Rompay AR, Johansson M, Karlsson A |title=Identification of a novel human adenylate kinase. cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein. |journal=Eur. J. Biochem. |volume=261 |issue= 2 |pages= 509–17 |year= 1999 |pmid= 10215863 |doi=
*cite journal | author=Singh B, Lin A, Wu ZC, Gupta RS |title=Gene structure for adenosine kinase in Chinese hamster and human: high-frequency mutants of CHO cells involve deletions of several introns and exons. |journal=DNA Cell Biol. |volume=20 |issue= 1 |pages= 53–65 |year= 2001 |pmid= 11242543 |doi= 10.1089/10445490150504693
*cite journal | author=Maguire PB, Wynne KJ, Harney DF, "et al." |title=Identification of the phosphotyrosine proteome from thrombin activated platelets. |journal=Proteomics |volume=2 |issue= 6 |pages= 642–8 |year= 2003 |pmid= 12112843 |doi= 10.1002/1615-9861(200206)2:6<642::AID-PROT642>3.0.CO;2-I
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Szkotak AJ, Ng AM, Man SF, "et al." |title=Coupling of CFTR-mediated anion secretion to nucleoside transporters and adenosine homeostasis in Calu-3 cells. |journal=J. Membr. Biol. |volume=192 |issue= 3 |pages= 169–79 |year= 2003 |pmid= 12820662 |doi=
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504

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