6.3.1.12: D-aspartate ligase

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For detailed information about D-aspartate ligase, go to the full flat file.

Word Map on EC 6.3.1.12

6.3.1.12

enterococcus

multiresistant

faecalis

peptidoglycan

atp-grasp

narrow-spectrum

faecium

bond-forming

medicine

drug development

Reaction

[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

Synonyms

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

ECTree

6 Ligases

6.3 Forming carbon-nitrogen bonds

6.3.1 Acid—ammonia (or amine) ligases (amide synthases)

6.3.1.12 D-aspartate ligase

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Systematic Name on EC 6.3.1.12 - D-aspartate ligase

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D-aspartate:[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-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 5.1.1.13, aspartate racemase [4]