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

ucFabV Requires Functional Reductase Activity to Confer Reduced Triclosan Susceptibility in Escherichia coli.

Journal of molecular microbiology and biotechnology - 1 Jan 2015

Fischer Taylor L, White Robert J, Mares Katherine F K, Molnau Devin E, Donato Justin J

Abstract excerpt

BACKGROUND/AIMS: We previously identified the Triclo1 fosmid in a functional metagenomic selection for clones that increased triclosan tolerance in Escherichia coli. The active enzyme encoded by Triclo1 is ucFabV. Although ucFabV is homologous to FabV from other organisms, ucFabV contains substitutions at key positions that would predict differences in substrate binding. Therefore, a detailed characterization of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Anti-Infective Agents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Resistance, Bacterial

Share to Enzyme Activation

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Oxidoreductases

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 26683704
DOI: 10.1159/000441640

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

ucFabV Requires Functional Reductase Activity to Confer Reduced Triclosan Susceptibility in Escherichia coli.PMID 26683704Read ↗

Fatty acid biosynthesis inhibitors fabimycin and triclosan trigger distinct resistance mutations in FabI and potently kill Gram-negative pathogensSemantic proximity Read ↗

An Efficient and Economical Assay to Screen for Triclosan Binding to FabI.Semantic proximity Read ↗

Mutations upstream of fabI in triclosan resistant Staphylococcus aureus strains are associated with elevated fabI gene expression.Semantic proximity Read ↗

Inhibition of the bacterial enoyl reductase FabI by triclosan: a structure-reactivity analysis of FabI inhibition by triclosan analogues.Semantic proximity Read ↗

A functional metagenomic approach for expanding the synthetic biology toolbox for biomass conversion.Semantic proximity Read ↗

Structure-activity studies of the inhibition of FabI, the enoyl reductase from Escherichia coli, by triclosan: kinetic analysis of mutant FabIs.Semantic proximity Read ↗

Multi-omics approach to study global changes in a triclosan-resistant mutant strain of Acinetobacter baumannii ATCC 17978.Semantic proximity Read ↗

Escherichia coli FadR positively regulates transcription of the fabB fatty acid biosynthetic gene.Semantic proximity Read ↗

A novel resistance mechanism to triclosan that suggests horizontal gene transfer and demonstrates a potential selective pressure for reduced biocide susceptibility in clinical strains of Staphylococcus aureus.Semantic proximity Read ↗

Structural basis for the variation in triclosan affinity to enoyl reductases.Semantic proximity Read ↗

The Fatty Acid Regulator FadR Influences the Expression of the Virulence Cascade in the El Tor Biotype of Vibrio cholerae by Modulating the Levels of ToxT via Two Different Mechanisms.Semantic proximity Read ↗

Proteomic and phenotypic analysis of triclosan tolerant verocytotoxigenic Escherichia coli O157:H19.Semantic proximity Read ↗

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