Biopolym. Cell. 1985; 1(5):247-253.
http://dx.doi.org/10.7124/bc.00018A
Reviews
E. coli DNA polymerase I: primer-template-dependent enzyme inactivation by imidazolides of deoxynucleoside-5'-triphosphates
1Nevinsky G. A., 1Doronin S. V., 1Lavrik O. I.
  1. Institute of Bioorganic Chemistry, Siberian Branch of the Academy of Sciences of the USSR
    Novosibirsk, USSR

Abstract

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 complexes. 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 analogue-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.
Full text: (PDF, in Russian)

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