CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.1380 | Muramoyl-pentapeptide Carboxypeptidase; domain 2 |
|
3.30.1380.10 |
Domain Context
CATH Clusters
| Superfamily | 3.30.1380.10 |
| Functional Family |
Enzyme Information
| 3.4.16.4 |
Serine-type D-Ala-D-Ala carboxypeptidase.
based on mapping to UniProt Q47746
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
-!- A group of bacterial enzymes, membrane-bound. -!- Inhibited by beta-lactam antibiotics, which acylate the active site serine in the enzyme. -!- Distinct from EC 3.4.17.14. -!- Belongs to peptidase families S11, S12 and S13.
|
UniProtKB Entries (1)
| Q47746 |
VANY_ENTFA
Enterococcus faecalis V583
D-alanyl-D-alanine carboxypeptidase
|
PDB Structure
| PDB | 6A6A |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis for the substrate recognition of peptidoglycan pentapeptides by Enterococcus faecalis VanYB.
Int. J. Biol. Macromol.
|
