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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / metabolism
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Antiviral Agents / metabolism
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Antiviral Agents / pharmacokinetics
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Binding, Competitive
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Biotransformation
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Bromodeoxyuridine / metabolism
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Cloning, Molecular
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DNA, Viral / genetics
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Herpesvirus 4, Human / enzymology*
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Hydrogen-Ion Concentration
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Kinetics
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Nucleosides / metabolism
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Nucleosides / pharmacokinetics
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Substrate Specificity
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Thymidine / metabolism
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Thymidine Kinase / genetics
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Thymidine Kinase / metabolism*
Substances
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Antiviral Agents
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DNA, Viral
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Nucleosides
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Adenosine Triphosphate
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Thymidine Kinase
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Bromodeoxyuridine
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Thymidine