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Kielley, R.K.: Purification and properties of thymidine monophosphate kinase from mouse hepatoma. J. Biol. Chem., 245, 4204–4212 (1970)
Tamiya, N.; Yusa, T.; Yamaguchi, Y.; Tsukifuii, R.; Kuroiwa, N.; Moriyama, Y.; Fujimura, S.: Co-purification of thymidylate kinase and cytosolic thymidine kinase from human term placenta by affinity chromatography. Bio-chim. Biophys. Acta, 995, 28–35 (1989)
Bone, R.; Cheng, Y.C.; Wolfenden, R.: Inhibition of adenosine and thymidylate kinases by bisubstrate analogs. J. Biol. Chem., 261, 16410–16413 (1986)
Jong, A.Y.S.; Campbell, J.L.: Characterization of Saccharomyces cerevisiae thymidylate kinase, the CDC8 gene product. General properties, kinetic analysis, and subcellular localization. J. Biol. Chem., 259, 14394–14398 (1984)
Chen, M.C.; Walker, J.; Prusoff, W.H.: Kinetic studies of herpes simplex virus type 1-encoded thymidine and thymidylate kinase, a multifunctional enzyme. J. Biol. Chem., 254, 10747–10753 (1979)
Lee, L.S.; Cheng, Y.C.: Human thymidylate kinase. Purification, characterization, and kinetic behavior of the thymidylate kinase derived from chronic myelocytic leukemia. J. Biol. Chem., 252, 5686–5691 (1977)
Smith, L.K.; Eakin, R.E.: Partial purification and characterization of thymidylate kinase from embryonic chick liver. Arch. Biochem. Biophys., 167, 61–71 (1975)
Rossi, M.; Woodward, D.O.: Enzymes of deoxythymidine triphosphate biosynthesis in Neurospora crassa mitochondria. J. Bacterid., 121, 640–647 (1975)
Cheng, Y.C.; Prusoff, W.H.: Mouse ascites sarcoma 180 thymidylate kinase. General properties, kinetic analysis, and inhibition studies. Biochemistry, 12, 2612–2619 (1973)
de Groot, E.J.; Schweiger, H.G.: Thymidylate kinase from Acetabularia. I. Properties of the enzyme. J. Cell Sci., 64, 13–25 (1983)
Nelson, D.J.; Carter, C.E.: Purification and characterization of thymidine 5-monophosphate kinase from Escherichia coli B. J. Biol. Chem., 244, 5254–5262 (1969)
Jong, A.Y.S.; Kuo, C.I.; Campbell, J.L.: The CDC8 gene of yeast encodes thymidylate kinase. J. Biol. Chem., 259, 11052–11059 (1984)
Ostermann, N.; Segura-Pena, D.; Meier, C; Veit, T.; Monnerjahn, C; Konrad, M.; Lavie, A.: Structures of human thymidylate kinase in complex with prodrugs: implications for the structure-based design of novel compounds. Biochemistry, 42, 2568–2577 (2003)
Chenal-Francisque, V.; Tourneux, L.; Carniel, E.; Christova, P.; de la Sierra, I.; Barzu, O.; Gilles, A.-M.: The highly similar TMP kinase of Yersinia pestis and Escherichia coli differ markedly in their AZTMP phosphorylating activity. Eur. J. Biochem., 265, 112–119 (1999)
Tourneux, L.; Bucurenci, N.; Lascu, I.; Sakamoto, H.; Briand, G.; Gilles, A.-M.: Substitution of an alanine residue for glycine 146 in TMP kinase from Escherichia coli is responsible for bacterial hypersensitivity to bromodeox-yuridine. J. Bacterid., 180, 4291–4293 (1998)
Petit, CM.; Koretke, K.K.: Characterization of Streptococcus pneumoniae thymidylate kinase: steady-state kinetics of the forward reaction and isothermal titration calorimetry. Biochem. J., 363, 825–831 (2002)
Fioravanti, E.; Haouz, A.; Ursby, T.; Munier-Lehmann, H.; Delarue, M.; Bourgeois, D.: Mycobacterium tuberculosis thymidylate kinase: structural studies of intermediates along the reaction pathway. J. Mol. Biol, 327, 1077–1092 (2003)
terentyev, L.L.; Terentyeva, N.A.; Rasskazov, V.A.: Purification and some properties of thymidylate kinase from sea urchin. Biochemistry, 64, 80–85 (1999)
Jacobsson, B.; Britton, S.; Tornevik, Y.; Eriksson, S.: Decreas in thymidylate kinase activity in peripheral blood mononuclear cells from HIV-infected individuals. Biochem. Pharmacol, 56, 389–395 (1998)
Munier-lehmann, H.; Chaffotte, A.; Pochet, S.; Labesse, G.: Thymidylate kinase of Mycobacterium tuberculosis: a chimera sharing properties common to eukaryotic and bacterial enzymes. Protein Sci., 10, 1195–1205 (2001)
Ostermann, N.; Schlichting, I.; Brundiers, R.; Konrad, M.; Reinstein, J.; Veit, T.; Goody, R.S.; Lavie, A.: Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate. Structure, 8, 629–642 (2000)
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(2007). dTMP Kinase. In: Schomburg, D., Scomburg, I., Chang, A. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 37. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-47818-8_81
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DOI: https://doi.org/10.1007/978-3-540-47818-8_81
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