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The exonuclease and endonuclease activities of the DNA polymerases, which extend their proof-reading capabilities and maintain high fidelity in the replication process, apparently conflict with the principle of microscopic reversibility. However, deeper mechanistic analysis of the reaction leads to fascinating insights into the kinetic and thermodynamic effects controlling the replication of the primary genetic material. Thus, nucleotide addition and excision apparently involve different pathways, although violation of microscopic reversibility is avoided as the overall reaction does not reach equilibrium. Intriguingly, however, this allows the fidelity levels to exceed those expected from simple kinetic control.

Nuclease Activity of the DNA Polymerases: An Evasion of Microscopic Reversibility Leading to Fidelity in Excess of Kinetic Control Levels