作者: Nicolas Z. Rudinger , Ramon Kranaster , Andreas Marx
DOI: 10.1016/J.CHEMBIOL.2006.11.016
关键词: DNA polymerase 、 Biology 、 Primase 、 DNA polymerase I 、 Polymerase 、 Biophysics 、 Biochemistry 、 Base pair 、 DNA clamp 、 Processivity 、 DNA polymerase II
摘要: Summary DNA polymerase fidelity is of immense biological importance due to the fundamental requirement for accurate synthesis in both replicative and repair processes. Subtle hydrogen-bonding networks between polymerases their primer/template substrates are believed have impact on selectivity. We show that deleting defined interactions kind by rationally designed hydrophobic substitution mutations can result in a more selective enzyme. Furthermore, a single-atom replacement within substrate through chemical modification, which leads an altered acceptor potential steric demand substrate, further increased selectivity developed systems. Accordingly, this study about alterations selectivity—enzyme wise—further highlights relevance shape complementary polar