Abstract
After infection of Escherichia coli by bacteriophage T2, the dUTPase activity increases by 5-10 times in 15 min. This activity has been shown to be separable from the dUTP-ase of the host. It differs from the enzyme of the host primarily in its sensitivity to fluoride, its stability, and its chromatographlc behavior. In addition, unlike host dUTPase which acts only on dUTP, the phage-induced fraction acts both on dUTP and dUDP. The possible role of the new dUTPase activity and its relationship to phage-induced dCMP deaminase in the biosynthesis of thymidylic acid have been discussed.