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Literature summary extracted from

  • Bellais, S.; Arthur, M.; Dubost, L.; Hugonnet, J.E.; Gutmann, L.; van Heijenoort, J.; Legrand, R.; Brouard, J.P.; Rice, L.; Mainardi, J.L.
    Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium (2006), J. Biol. Chem., 281, 11586-11594.
    View publication on PubMed

Application

EC Number Application Comment Organism
6.3.1.12 medicine the enzyme appears as an attractive target for the development of narrow spectrum antibiotics active against multiresistant Enterococcus faecium Enterococcus faecium

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.1.12
-
 Enterococcus faecium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.12 Mg2+ required Enterococcus faecium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.12 ATP + D-aspartate + [beta-GlcNAc-(1,4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n Enterococcus faecium the enzyme is responsible for the addition of D-aspartic acid onto the peptidoglycan precursor. specifically ligates the beta-carboxylate of D-Asp to the epsilon-amino group of L-Lys in the nucleotide precursor UDP-N-acetylmuramyl-pentapeptide [beta-GlcNAc-(1,4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.1.12 Enterococcus faecium
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.1.12
-
 Enterococcus faecium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.12 ATP + D-aspartate + [beta-GlcNAc-(1,4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n the enzyme is responsible for the addition of D-aspartic acid onto the peptidoglycan precursor. specifically ligates the beta-carboxylate of D-Asp to the epsilon-amino group of L-Lys in the nucleotide precursor UDP-N-acetylmuramyl-pentapeptide Enterococcus faecium [beta-GlcNAc-(1,4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate
-
 ?
6.3.1.12 ATP + D-aspartate + [beta-GlcNAc-(1,4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n 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 Enterococcus faecium [beta-GlcNAc-(1,4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate
-
 ?