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Literature summary for 6.1.2.1 extracted from

  • Perichon, B.; Casadewall, B.; Reynolds, P.; Courvalin, P.
    Glycopeptide-resistant Enterococcus faecium BM4416 is a VanD-type strain with an impaired D-alanine:D-alanine ligase (2000), Antimicrob. Agents Chemother., 44, 1346-1348.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Enterococcus faecium
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 BM4416
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Enterococcus faecium BM4416
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 BM4416
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General Information

General Information Comment Organism
physiological function resistance to glycopeptides in Enterococcus faecium BM4416 is due to synthesis of late peptidoglycan precursors ending in D-Ala–D-Lac. Strain BM4416 mainly produces UDP-MurNAc-pentadepsipeptide, 69%, terminating in D-Ala–D-Lac, UDP-MurNAc-tetrapeptide, 24%, and UDP-MurNAc-tripeptide, 7%. No significant amounts of UDP-MurNAc-pentapeptide are found. Constitutive resistance is encoded by a vanD operon closely related to that of Enterococcus faecium BM4339 and also located in the chromosome. Both VanD-type strains produce an inactivated D-Ala:D-Ala ligase due to an insertion in the ddl gene Enterococcus faecium