ENZYME entry: EC 6.3.1.12

Accepted Name
D-aspartate ligase.
Alternative Name(s)
Asl(fm).
D-aspartic acid-activating enzyme.
Reaction catalysed
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
Comment(s)
  • 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.
  • Highly specific for D-aspartate, as L-aspartate, D-glutamate, D-alanine, D-iso-asparagine and D-malic acid are not substrates.
  • In Enterococcus faecium, the substrate D-aspartate is produced by EC 5.1.1.13.
Cross-references
PROSITEPDOC50975
BRENDA6.3.1.12
EC2PDB6.3.1.12
ExplorEnz6.3.1.12
PRIAM enzyme-specific profiles6.3.1.12
KEGG Ligand Database for Enzyme Nomenclature6.3.1.12
IUBMB Enzyme Nomenclature6.3.1.12
IntEnz6.3.1.12
MEDLINEFind literature relating to 6.3.1.12
MetaCyc6.3.1.12
UniProtKB/Swiss-Prot
H8L902, ASL_ENTFU

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.3.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.3.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.-.-.-