Biopolymers and cell. 1985. Volume 1. № 5. 247 - 253

G. A. Nevinsky, S. V. Doronin, O. I. Lavrik

E. COLI DNA POLYMERASE I: PRIMER-TEMPLATE-DEPENDENT ENZYME INACTIVATION BY IMIDAZOLIDES OF DEOXYNUCLEOSIDE-5'-TRIPHOSPHATES

Summary

    Interaction of E. coli DNA-polymerase I with imidazolides of dATP, dCTP, dGTP and dTTP is investigated in the presence and the absence of different primer-template comple¬xes. It is found that the enzyme can be inactivated only in the presence of a primer and a template being complementary to dNTP analogue. From the data obtained it may be supposed that the orientation of analogue polyphosphate chain changes due to the ana¬logue-template complex formation. Such a transformation results in the close proximity of the terminal phosphate of the analogue to nucleophilic. groups of the active enzyme site and in their subsequent phosphorylation.