Adenosine diphosphate: thymidine 5'-phosphotransferase, a new enzyme activity, associated with the Herpes simplex virus-induced deoxypyrimidine kinase.

The deoxypyrimidine kinase induced in mouse fibroblasts, strain CLID (TK-) infected with either herpes simplex virus (HSV) type 1 or type 2, possesses besides deoxypyrimidine kinase (ATP:dThd/dCyd phosphotransferase) two further enzyme activities: an AMP:dThd phosphotransferase and an ADP:dThd phosphotransferase. The latter enzyme activity, described in this report, was found to be inhibited by antiserum against the HSV deoxypyrimidine kinase and to be absent after infection with TK- mutant MDK 10 (B 2006). The ADP:dThd phosphotransferase, which had been purified approx. 340-fold, differs by a series of physicochemical properties from the viral AMP:dThd- and ATP:dThd phosphotransferase.