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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Lack of stereospecificity of suid pseudorabies virus thymidine kinase.

We have partially purified suid pseudorabies virus (PRV) thymidine kinase from infected thymidine kinase- mouse cells, and cytosolic swine thymidine kinase from lymphatic glands, and we have found that PRV thymidine kinase, unlike the host enzyme, shows no stereospecificity for D- and L-beta-nucleosides. In vitro, unnatural L-enantiomers, except L-deoxycytidine, function as specific inhibitors for the viral enzyme in the order: L-thymidine >> L-deoxyguanosine > L-deoxyuridine > L-deoxyadenosine. Contrary to human and swine thymidine kinases and like herpes simplex virus-1 and -2 thymidine kinases, PRV thymidine kinase phosphorylates both the natural (D-) and the unnatural (L-) thymidine enantiomers to their corresponding monophosphates with comparable efficiency. The kinetic parameters Vmax/Km for D- and L-thymidine are 3.7 and 2.3 respectively. Our results demonstrate that the lack of stereospecificity might be a common feature of the thymidine kinases that are encoded by human and animal herpes viruses. These observations could lead to the development of a novel class of antiviral drugs.[1]


  1. Lack of stereospecificity of suid pseudorabies virus thymidine kinase. Maga, G., Verri, A., Bonizzi, L., Ponti, W., Poli, G., Garbesi, A., Niccolai, D., Spadari, S., Focher, F. Biochem. J. (1993) [Pubmed]
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