DNA polymerase fidelity: kinetics, structure, and checkpoints.

@article{Joyce2004DNAPF,
  title={DNA polymerase fidelity: kinetics, structure, and checkpoints.},
  author={Catherine M. Joyce and Stephen J Benkovic},
  journal={Biochemistry},
  year={2004},
  volume={43 45},
  pages={14317-24}
}
On careful examination of existing kinetic data for correct and incorrect dNTP incorporations by a variety of DNA polymerases, it is apparent that these enzymes resist a unified description. Instead, the picture that emerges is a rather complex one: for most polymerases, there is evidence for a noncovalent step preceding phosphoryl transfer, but there are less reliable data for determining whether the noncovalent step or phosphoryl transfer is rate-limiting during misincorporation. Although the… CONTINUE READING

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Dynamic characterization of a DNA repair enzyme : NMR studies of [ methyl13 C ] methioninelabeled DNA polymerase â

W. A. Beard, S. H. Wilson, R. E. London
Biochemistry • 2004

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