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Article

DNA polymerase active site is highly mutable: evolutionary consequences.

Proceedings of the National Academy of Sciences of the United States of America - 9 May 2000

Patel P H, Loeb L A

Abstract excerpt

DNA polymerases contain active sites that are structurally superimposable and highly conserved in sequence. To assess the significance of this preservation and to determine the mutational burden that active sites can tolerate, we randomly mutated a stretch of 13 amino acids within the polymerase catalytic site (motif A) of Thermus aquaticus DNA polymerase I. After selection, by using genetic complementation, we...

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Identifiers

PMID: 10805772
DOI: 10.1073/pnas.97.10.5095
PMCID: PMC25787

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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