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Article

Characterization of the vanD glycopeptide resistance gene cluster from Enterococcus faecium BM4339.

Journal of bacteriology - 1 Jun 1999

Casadewall B, Courvalin P

Abstract excerpt

VanD-type resistance to glycopeptides in Enterococcus faecium BM4339 is due to constitutive synthesis of D-alanyl-D-lactate-terminating peptidoglycan precursors (B. Périchon, P. Reynolds, and P. Courvalin, Antimicrob. Agents Chemother. 41:2016-2018, 1997). The sequence of a 5,780-bp fragment was determined and revealed six open reading frames. The 3' distal part encoded the VanHD dehydrogenase, the VanD ligase,...

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

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Source

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Identifiers

PMID: 10368136
DOI: 10.1128/JB.181.12.3644-3648.1999
PMCID: PMC93839

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

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of the vanD glycopeptide resistance gene cluster from Enterococcus faecium BM4339.PMID 10368136Read ↗

Characterization of a divergent vanD-type resistance element from the first glycopeptide-resistant strain of Enterococcus faecium isolated in Brazil.Semantic proximity Read ↗

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<i>vanM</i> , a New Glycopeptide Resistance Gene Cluster Found in <i>Enterococcus faecium</i>Semantic proximity Read ↗

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Elucidation of host diversity of the VanD-carrying genomic islands in enterococci and anaerobesSemantic proximity Read ↗

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Genomic and expression analysis of the vanG-like gene cluster of Clostridium difficileSemantic proximity Read ↗

Old and New Glycopeptide Antibiotics: Action and ResistanceSemantic proximity Read ↗

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