The Enzymology of Virus-infected Bacteria. Vi. Purification and Properties of the Deoxynucleotide Kinase Induced by Bacteriophage T5.

Extracts prepared from Escherichia coli infected with the T-even bacteriophages catalyze the phosphorylation of deoxyguanylate and deoxythymidylate to the corresponding polyphosphates at 10 to 20 times the rate of comparable extracts prepared from uninfected cells (2, 3). Previous work has indicated that these enzymatic activities are different and separable from the enzyme fractions in the normal cell apparently responsible for catalyzing the same reactions (4, 5). This paper reports on the purification and properties of deoxyguanylate kinase from extracts of T2-infected cells. During this purification, there was a commensurate enrichment of deoxythymidylate and hydroxymethyldeoxycytidylate kinase activity in the deoxyguanylate kinase fractions, and evidence will be presented suggesting that these three activities are associated with one enzyme.