Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The conserved active site motif A of Escherichia coli DNA polymerase I is highly mutable.

The Journal of biological chemistry - 1 Jun 2001

Shinkai A, Patel P H, Loeb L A

Abstract excerpt

Escherichia coli DNA polymerase I participates in DNA replication, DNA repair, and genetic recombination; it is the most extensively studied of all DNA polymerases. Motif A in the polymerase active site has a required role in catalysis and is highly conserved. To assess the tolerance of motif A for amino acid substitutions, we determined the mutability of the 13 constituent amino acids Val(700)-Arg(712) by using...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Motifs
Share to Aspartic Acid
Share to Catalysis

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Conserved Sequence

Share to DNA Polymerase I

Share to Electrophoresis, Polyacrylamide Gel

Share to Isoleucine

Source

Identifiers

PMID: 11278911
DOI: 10.1074/jbc.M011472200

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The conserved active site motif A of Escherichia coli DNA polymerase I is highly mutable.PMID 11278911Read ↗

Mutability of DNA polymerase I: implications for the creation of mutant DNA polymerases.Semantic proximity Read ↗

DNA polymerase active site is highly mutable: evolutionary consequences.Semantic proximity Read ↗

Highly tolerated amino acid substitutions increase the fidelity of Escherichia coli DNA polymerase I.Semantic proximity Read ↗

In vivo mutagenesis by Escherichia coli DNA polymerase I. Ile(709) in motif A functions in base selection.Semantic proximity Read ↗

A single highly mutable catalytic site amino acid is critical for DNA polymerase fidelity.Semantic proximity Read ↗

A strategically located serine residue is critical for the mutator activity of DNA polymerase IV from Escherichia coli.Semantic proximity Read ↗

Directed DNA polymerase evolution: effects of mutations in motif C on the mismatch-extension selectivity of thermus aquaticus DNA polymerase.Semantic proximity Read ↗

Critical amino acids in Escherichia coli UmuC responsible for sugar discrimination and base-substitution fidelity.Semantic proximity Read ↗

Novel Escherichia coli active site dnaE alleles with altered base and sugar selectivity.Semantic proximity Read ↗

The mutability of enzyme active-site shape determinants.Semantic proximity Read ↗

DNA polymerase fidelity: from genetics toward a biochemical understanding.Semantic proximity Read ↗

The microbiology of mutability.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.