EC - D-aspartate ligase

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IntEnz Enzyme Nomenclature


Accepted name:
D-aspartate ligase
Other names:
UDP-MurNAc-pentapeptide:D-aspartate ligase
D-aspartic acid-activating enzyme
Systematic name:
D-aspartate:[β-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n ligase (ADP-forming)



This enzyme forms part of the peptidoglycan assembly pathway of Gram-positive bacteria grown in medium containing D-Asp. Normally, the side chains the acylate the 6-amino group of the L-lysine residue contain L-Ala-L-Ala but these amino acids are replaced by D-Asp when D-Asp is included in the medium. Hybrid chains containing L-Ala-D-Asp, L-Ala-L-Ala-D-Asp or D-Asp-L-Ala are not formed [4]. The enzyme belongs in the ATP-grasp protein superfamily [3,4]. The enzyme is highly specific for D-aspartate, as L-aspartate, D-glutamate, D-alanine, D-iso-asparagine and D-malic acid are not substrates [4]. In Enterococcus faecium, the substrate D-aspartate is produced by EC, aspartate racemase [4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC50975
Structural data: CSA , EC2PDB
Gene Ontology: GO:0034025


  1. Staudenbauer, W. and Strominger, J.L.
    Activation of D-aspartic acid for incorporation into peptidoglycan.
    J. Biol. Chem. 247: 5095-5102 (1972). [PMID: 4262567]
  2. Staudenbauer, W., Willoughby, E. and Strominger, J.L.
    Further studies of the D-aspartic acid-activating enzyme of Streptococcus faecalis and its attachment to the membrane.
    J. Biol. Chem. 247: 5289-5296 (1972). [PMID: 4626717]
  3. Galperin, M.Y. and Koonin, E.V.
    A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity.
    Protein Sci. 6: 2639-2643 (1997). [PMID: 9416615]
  4. Bellais, S., Arthur, M., Dubost, L., Hugonnet, J.-E., Gutmann, L., van Heijenoort, J., Legrand, R., Brouard, J.-P., Rice, L. and Mainardi, J.-L.
    Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium.
    J. Biol. Chem. 281: 11586-11594 (2006). [PMID: 16510449]

[EC created 2006]