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Pathway Description
Adefovir Dipivoxil Metabolism Pathway
Homo sapiens
Drug Metabolism Pathway
Created: 2013-09-11
Last Updated: 2019-08-16
Adefovir dipivoxil is an ester prodrug of adefovir, a nucleotide analogue used in the treatment of chronic hepatitis B. Adefovir dipivoxil is taken up into the liver cell and is cleaved into adefovir by intracellular esterases. Adefovir is subsequently phosphorylated first by adenylate kinases and then by nucleoside diphosphate kinases into adefovir diphosphate. Adefovir diphosphate is an analogue of deoxyadenosine triphosphate (dATP) and competes with dATP for binding to the viral DNA polymerase and subsequent incorporation into the growing DNA strand. Once incorporated into the DNA, adefovir causes chain termination, thus preventing viral replication.
References
Adefovir Dipivoxil Pathway References
Dando T, Plosker G: Adefovir dipivoxil: a review of its use in chronic hepatitis B. Drugs. 2003;63(20):2215-34.
Pubmed: 14498759
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Pubmed: 183954
Matsuura S, Igarashi M, Tanizawa Y, Yamada M, Kishi F, Kajii T, Fujii H, Miwa S, Sakurai M, Nakazawa A: Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase. J Biol Chem. 1989 Jun 15;264(17):10148-55.
Pubmed: 2542324
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Pubmed: 15489334
Lee Y, Kim JW, Lee IA, Kang HB, Choe YK, Lee HG, Lim JS, Kim HJ, Park C, Choe IS: Cloning and characterization of cDNA for human adenylate kinase 2A. Biochem Mol Biol Int. 1996 Jul;39(4):833-42.
Pubmed: 8843353
Lee Y, Kim JW, Lee SM, Kim HJ, Lee KS, Park C, Choe IS: Cloning and expression of human adenylate kinase 2 isozymes: differential expression of adenylate kinase 1 and 2 in human muscle tissues. J Biochem. 1998 Jan;123(1):47-54. doi: 10.1093/oxfordjournals.jbchem.a021915.
Pubmed: 9504408
Noma T, Song S, Yoon YS, Tanaka S, Nakazawa A: cDNA cloning and tissue-specific expression of the gene encoding human adenylate kinase isozyme 2. Biochim Biophys Acta. 1998 Jan 7;1395(1):34-9. doi: 10.1016/s0167-4781(97)00193-0.
Pubmed: 9434148
Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. doi: 10.1038/342177a0.
Pubmed: 2509941
Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9.
Pubmed: 1851158
Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20.
Pubmed: 7916650
Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9.
Pubmed: 1988104
Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. doi: 10.1126/science.8392752.
Pubmed: 8392752
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