A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
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 |
|---|
| PROSITE | PDOC50975 |
| 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 |
| 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.-.-.-