The efficiency of dNTP complex formation with human placenta DNA polymerase alpha as demonstrated by affinity modification.
The interaction of deoxyribonucleoside 5'-mono-, di- and triphosphates with human placenta DNA polymerase alpha was examined. Dissociation constants of enzyme complex formation with dNMP, dNDP and dNTP were determined from the data on enzyme affinity modification by imidazolide of dTMP. The basic role of the primary template-primer interaction with the enzyme in dNTP complex formation is shown. The template-dependent nucleotide interaction does not occur in the case of dNMP and dNDP in comparison with dNTP. The significant contribution of the gamma-phosphate of dNTP in this process is demonstrated.
D001667:Binding, Competitive; D004257:DNA Polymerase II / Q000378:metabolism*; D003854:Deoxyribonucleotides / Q000378:metabolism*; D006801:Humans; D007093:Imidazoles / Q000378:metabolism; D010920:Placenta / Q000201:enzymology; D011061:Poly A / Q000378:metabolism; D011485:Protein Binding; D013329:Structure-Activity Relationship; D013698:Templates, Genetic; D013816:Thermodynamics
D003854:Deoxyribonucleotides; D007093:Imidazoles; D011061:Poly A; C015465:poly(dA); D004257:DNA Polymerase II