EC 6.1.2.1 - D-alanine—(R)-lactate ligase

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IntEnz Enzyme Nomenclature
EC 6.1.2.1

Names

Accepted name:
D-alanine—(R)-lactate ligase
Other names:
VanA
VanB
VanD
Systematic name:
D-alanine:(R)-lactate ligase (ADP-forming)

Reaction

Comments:

The product of this enzyme, the depsipeptide D-alanyl-(R)-lactate, can be incorporated into the peptidoglycan pentapeptide instead of the usual D-alanyl-D-alanine dipeptide, which is formed by EC 6.3.2.4, D-alanine—D-alanine ligase. The resulting peptidoglycan does not bind the glycopeptide antibiotics vancomycin and teicoplanin, conferring resistance on the bacteria.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Bugg, T. D., Wright, G. D., Dutka-Malen, S., Arthur, M., Courvalin, P., Walsh, C. T.
    Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA.
    Biochemistry 30: 10408-10415 (1991). [PMID: 1931965]
  2. Meziane-Cherif, D., Badet-Denisot, M. A., Evers, S., Courvalin, P., Badet, B.
    Purification and characterization of the VanB ligase associated with type B vancomycin resistance in Enterococcus faecalis V583.
    FEBS Lett. 354: 140-142 (1994). [PMID: 7957913]
  3. Perichon, B., Reynolds, P., Courvalin, P.
    VanD-type glycopeptide-resistant Enterococcus faecium BM4339.
    Antimicrob. Agents Chemother. 41: 2016-2018 (1997). [PMID: 9303405]

[EC 6.1.2.1 created 2010]