title: Substrate specificity of Epstein-Barr virus thymidine kinase.
abstract: Purified recombinant protein encoded by the BXLF-I open reading frame of the Epstein-Barr virus genome has thymidine kinase activity. The substrate behaviors of various nucleosides toward this enzyme were tested. Halogenated deoxyuridines, zidovudine, and bromovinyldeoxyuridine are efficient substrates, while acyclovir and dihydroxypropylmethylguanine are relatively poor substrates for the Epstein-Barr virus thymidine kinase.
authors: Department of Therapeutic Radiology, Yale University School of Medicine, New Haven, Connecticut 06520-8040.
authors: P P
authors: PP
authors: Tung
authors: W C
authors: WC
authors: Summers
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000998:Antiviral Agents / Q000378:metabolism / Q000493:pharmacokinetics; D001667:Binding, Competitive; D001711:Biotransformation; D001973:Bromodeoxyuridine / Q000378:metabolism; D003001:Cloning, Molecular; D004279:DNA, Viral / Q000235:genetics; D004854:Herpesvirus 4, Human / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009705:Nucleosides / Q000378:metabolism / Q000493:pharmacokinetics; D013379:Substrate Specificity; D013936:Thymidine / Q000378:metabolism; D013937:Thymidine Kinase / Q000235:genetics / Q000378:metabolism*
chemical_list: D000998:Antiviral Agents; D004279:DNA, Viral; D009705:Nucleosides; D000255:Adenosine Triphosphate; D013937:Thymidine Kinase; D001973:Bromodeoxyuridine; D013936:Thymidine