Miller L K, Wells R D
Proc Natl Acad Sci U S A. 1971 Sep;68(9):2298-302. doi: 10.1073/pnas.68.9.2298.
Nucleoside diphosphokinase activity is present in highly purified preparations of DNA polymerase from Micrococcus luteus and Escherichia coli, and in a partially purified DNA polymerase from avian myeloblastosis virus. The activity is also observed in the protein fragment of molecular weight 76,000 that is produced by subtilisin cleavage of DNA polymerase I from E. coli. The NDP kinase activity in DNA polymerase preparations from M. luteus uses various ribo- and deoxyribonucleoside di- and triphosphates as substrates. The presence of this activity in preparations of DNA polymerase results in the apparent use of deoxyribonucleoside diphosphates as substrates for DNA synthesis, provided that some triphosphate is present to serve as a phosphate donor.
核苷二磷酸激酶活性存在于从藤黄微球菌和大肠杆菌高度纯化的DNA聚合酶制剂中,以及从禽成髓细胞瘤病毒部分纯化的DNA聚合酶中。在由枯草杆菌蛋白酶切割大肠杆菌DNA聚合酶I产生的分子量为76,000的蛋白质片段中也观察到该活性。藤黄微球菌DNA聚合酶制剂中的NDP激酶活性使用各种核糖和脱氧核糖核苷二磷酸及三磷酸作为底物。DNA聚合酶制剂中这种活性的存在导致在有一些三磷酸作为磷酸供体的情况下,脱氧核糖核苷二磷酸明显被用作DNA合成的底物。