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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
6.3.2.4 additional information insertion in the middle of the ddl gene is responsible for inactivation of D-alanine-D-alanine ligase in strain BM4416 Enterococcus faecium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.4 ATP + D-alanine Enterococcus faecium
-
 ADP + phosphate + D-alanyl-D-alanine
-
 ?
6.3.2.4 ATP + D-alanine Enterococcus faecium BM4416
-
 ADP + phosphate + D-alanyl-D-alanine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.2.1 Enterococcus faecium
-
 BM4416
-
6.1.2.1 Enterococcus faecium BM4416
-
 BM4416
-
6.3.2.4 Enterococcus faecium
-
-
-
6.3.2.4 Enterococcus faecium BM4416
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.4 ATP + D-alanine
-
 Enterococcus faecium ADP + phosphate + D-alanyl-D-alanine
-
 ?
6.3.2.4 ATP + D-alanine
-
 Enterococcus faecium BM4416 ADP + phosphate + D-alanyl-D-alanine
-
 ?

General Information

EC Number General Information Comment Organism
6.1.2.1 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