Article
A single highly mutable catalytic site amino acid is critical for DNA polymerase fidelity.
The Journal of biological chemistry - 16 Feb 2001
Patel P H, Kawate H, Adman E, Ashbach M, Loeb L A
Abstract excerpt
DNA polymerases contain active sites that are structurally superimposable and conserved in amino acid sequence. To probe the biochemical and structure-function relationship of DNA polymerases, a large library (200,000 members) of mutant Thermus aquaticus DNA polymerase I (Taq pol I) was created containing random substitutions within a portion of the dNTP binding site (Motif A; amino acids 605-617), and a fraction...
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