D-aspartate ligase;
Aslfm;
UDP-MurNAc-pentapeptide:D-aspartate ligase;
D-aspartic acid-activating enzyme

Ligases;
Forming carbon-nitrogen bonds;
Acid-D-ammonia (or amine) ligases (amide synthases)

D-aspartate:[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n ligase (ADP-forming)

ATP + D-aspartate + [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n = [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 [RN:R09590]

R09590

ATP [CPD:C00002];
D-aspartate [CPD:C00402];
[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n [CPD:C19695]

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 5.1.1.13, aspartate racemase [4]

1  [PMID:4262567]

Staudenbauer W, Strominger JL.

Activation of D-aspartic acid for incorporation into peptidoglycan.

J. Biol. Chem. 247 (1972) 5095-102.

Streptococcus faecalis, Lactobacillus casei

2  [PMID:4626717]

Staudenbauer W, Willoughby E, Strominger JL.

Further studies of the D-aspartic acid-activating enzyme of Streptococcus faecalis and its attachment to the membrane.

J. Biol. Chem. 247 (1972) 5289-96.

Streptococcus faecalis

3  [PMID:9416615]

Galperin MY, Koonin EV.

A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity.

Protein. Sci. 6 (1997) 2639-43.

4  [PMID:16510449]

Bellais S, Arthur M, Dubost L, Hugonnet JE, Gutmann L, van Heijenoort J, Legrand R, Brouard JP, Rice L, Mainardi JL.

Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium.

J. Biol. Chem. 281 (2006) 11586-94.

Enterococcus faecium, Enterococcus faecalis