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Literature summary for 6.1.2.1 extracted from

  • Perichon, B.; Reynolds, P.; Courvalin, P.
    VanD-type glycopeptide-resistant Enterococcus faecium BM4339 (1997), Antimicrob. Agents Chemother., 41, 2016-2018.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.2.1

Organism

Organism UniProt Comment Textmining
Enterococcus faecium
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 BM4339
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Enterococcus faecium BM4339
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 BM4339
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Synonyms

Synonyms Comment Organism
VanD
-
 Enterococcus faecium

General Information

General Information Comment Organism
physiological function the vanD gene encodes a D-Ala:D-Lac ligase related to VanA and VanB which is not transferable by conjugation. It renders the cells constitutively resistant to vancomycin with a minimum inhibitory concentration MIC of 0.064 mg/ml and to low levels of teicoplanin, MIC 0.004 mg/ml. Cytoplasmic peptidoglycan precursors that accumulate are mainly UDP-MurNAc-pentadepsipeptide, UDP-MurNAc-tetrapeptide, and UDP-MurNAc-tripeptide. The large proportion of UDP-MurNAc-pentadepsipeptide indicates that the mechanism of vancomycin resistance in BM4339 is similar to that in VanA and VanB strains. The presence of UDP-MurNAc-tripeptide implies that the rate of synthesis of D-Ala–D-Ala or D-Ala–D-Lac substrates is limiting Enterococcus faecium