ENZYME entry: EC 6.3.1.12
Accepted Name |
D-aspartate ligase.
|
Alternative Name(s) |
Aslfm. |
D-aspartic acid-activating enzyme. |
Reaction catalysed |
[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n) + n ATP + n D-aspartate <=> [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + n ADP + n H(+) + n 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 |
BRENDA | 6.3.1.12 |
EC2PDB | 6.3.1.12 |
ExplorEnz | 6.3.1.12 |
PRIAM enzyme-specific profiles | 6.3.1.12 |
KEGG Ligand Database for Enzyme Nomenclature | 6.3.1.12 |
IUBMB Enzyme Nomenclature | 6.3.1.12 |
IntEnz | 6.3.1.12 |
MEDLINE | Find literature relating to 6.3.1.12 |
MetaCyc | 6.3.1.12 |
Rhea expert-curated reactions | 6.3.1.12 |
UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
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.-.-.-