Abstract：
:Intensive study has been devoted to understanding the kinetic and structural bases underlying the exceptionally high fidelity (low error frequencies) of the typical DNA polymerase. Commonly proposed explanations have included (i) the concept of fidelity check points, in which the correctness of a nascent base pair match is tested at multiple points along the reaction pathway, and (ii) an induced-fit fidelity enhancement mechanism based on a rate-limiting, substrate-induced conformational change. In this article, we consider the evidence and theoretical framework for the involvement of such mechanisms in fidelity enhancement. We suggest that a "simplified" model, in which fidelity is derived fundamentally from differential substrate binding at the transition state of a rate-limiting chemical step, is consistent with known data and sufficient to explain the substrate selectivity of these enzymes.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Showalter AK,Tsai MDdoi
10.1021/bi026021isubject
Has Abstractpub_date
2002-08-27 00:00:00pages
10571-6issue
34eissn
0006-2960issn
1520-4995pii
bi026021ijournal_volume
41pub_type
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