Mozer T J, Warner H R
J Virol. 1977 Nov;24(2):635-41. doi: 10.1128/JVI.24.2.635-641.1977.
Bacteriophage T5 induced a deoxynucleoside 5'-monophosphatase during its infection of Escherichia coli. The enzyme was purified about 100-fold. It was clearly distinct from the host 5'-nucleotidase activity in its physical characteristics and substrate specificity. The enzyme was active on deoxynucleoside 5'-monophosphates but was not active as a phosphatase on ribonucleotides, deoxynucleoside 5'-triphosphates, deoxynucleoside 3'-monophosphates, or deoxyoligonucleotides. Furthermore, it did not have oligonucleotidase or exonuclease activity. The enzyme could exist in multimeric form but had a monomer molecular weight of about 25,000.
噬菌体T5在感染大肠杆菌的过程中诱导产生了一种脱氧核苷5'-单磷酸酶。该酶被纯化了约100倍。其物理特性和底物特异性与宿主5'-核苷酸酶活性明显不同。该酶对脱氧核苷5'-单磷酸具有活性,但作为磷酸酶对核糖核苷酸、脱氧核苷5'-三磷酸、脱氧核苷3'-单磷酸或脱氧寡核苷酸无活性。此外,它不具有寡核苷酸酶或核酸外切酶活性。该酶可以以多聚体形式存在,但单体分子量约为25,000。