Adenosine kinase (AdK; EC 2.7.1.20) is an enzyme that catalyzes the transfer of gamma-phosphate from Adenosine triphosphate (ATP) to adenosine (Ado) leading to formation of Adenosine monophosphate (AMP). In addition to its well-studied role in controlling the cellular concentration of Ado, AdK also plays an important role in the maintenance of methylation reactions.[1][2][3][4][5][6][7] All S-adenosylmethionine-dependent transmethylation reactions in cells lead to production of S-adenosylhomocysteine (SAH), which is cleaved by SAH hydrolase into Ado and homocysteine. The failure to efficiently remove these end products (Ado removed by phosphorylation by AdK) can result in buildup of SAH, which is a potent inhibitor of all transmethylation reactions.[4][8][9] The disruption of AdK gene (-/-) in mice causes neonatal hepatic steatosis, a fatal condition characterized by rapid microvesicular fat infiltration, leading to early postnatal death.[6] The liver was the main organ affected in these animals and in it the levels of adenine nucleotides were decreased, while those of SAH were elevated. Recently, missense mutations in the AdK gene in humans which result in AdK deficiency have also been shown to cause hypermethioninemia, encephalopathy and abnormal liver function.[10]
^Lindberg B, Klenow H, Hansen K (February 1967). "Some properties of partially purified mammalian adenosine kinase". The Journal of Biological Chemistry. 242 (3): 350–6. doi:10.1016/S0021-9258(18)96277-0. PMID 4290214.
^Caputto R (April 1951). "The enzymatic synthesis of adenylic acid; adenosinekinase". The Journal of Biological Chemistry. 189 (2): 801–14. doi:10.1016/S0021-9258(18)44897-1. PMID 14832298.
^Kornberg A, Pricer WE (December 1951). "Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside". The Journal of Biological Chemistry. 193 (2): 481–95. doi:10.1016/S0021-9258(18)50904-2. PMID 14907737.
^ abFox IH, Kelley WN (1978). "The role of adenosine and 2'-deoxyadenosine in mammalian cells". Annual Review of Biochemistry. 47: 655–86. doi:10.1146/annurev.bi.47.070178.003255. PMID 209731.
^Kredich NM, Martin DV (December 1977). "Role of S-adenosylhomocysteine in adenosinemediated toxicity in cultured mouse T lymphoma cells". Cell. 12 (4): 931–8. doi:10.1016/0092-8674(77)90157-X. PMID 597863. S2CID 33818372.
^ abBoison D, Scheurer L, Zumsteg V, Rülicke T, Litynski P, Fowler B, Brandner S, Mohler H (May 2002). "Neonatal hepatic steatosis by disruption of the adenosine kinase gene". Proceedings of the National Academy of Sciences of the United States of America. 99 (10): 6985–90. Bibcode:2002PNAS...99.6985B. doi:10.1073/pnas.092642899. PMC 124515. PMID 11997462.
^Park J, Gupta RS (September 2008). "Adenosine kinase and ribokinase--the RK family of proteins". Cellular and Molecular Life Sciences. 65 (18): 2875–96. doi:10.1007/s00018-008-8123-1. PMID 18560757. S2CID 11439854.
^Lawrence De Koning, A. B.; Werstuck, G. H.; Zhou, J.; Austin, R. C. (2003). "Hyperhomocysteinemia and its role in the development of atherosclerosis". Clinical Biochemistry. 36 (6): 431–41. doi:10.1016/S0009-9120(03)00062-6. PMID 12951169.
^Kredich NM, Hershfield MS (May 1979). "S-adenosylhomocysteine toxicity in normal and adenosine kinase-deficient lymphoblasts of human origin". Proceedings of the National Academy of Sciences of the United States of America. 76 (5): 2450–4. Bibcode:1979PNAS...76.2450K. doi:10.1073/pnas.76.5.2450. PMC 383620. PMID 221926.
^Bjursell MK, Blom HJ, Cayuela JA, Engvall ML, Lesko N, Balasubramaniam S, Brandberg G, Halldin M, Falkenberg M, Jakobs C, Smith D, Struys E, von Döbeln U, Gustafsson CM, Lundeberg J, Wedell A (October 2011). "Adenosine kinase deficiency disrupts the methionine cycle and causes hypermethioninemia, encephalopathy, and abnormal liver function". American Journal of Human Genetics. 89 (4): 507–15. doi:10.1016/j.ajhg.2011.09.004. PMC 3188832. PMID 21963049.
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