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
| 3.4.13.22 |
D-Ala-D-Ala dipeptidase.
based on mapping to UniProt Q06241
D-Ala-D-Ala + H(2)O = 2 D-Ala.
-!- Protects Enterococcus faecium from the antibiotic vancomycin, which can bind to the -D-Ala-D-Ala sequence at the C-terminus of the peptidoglycan pentapeptide. -!- Reduces the availability of the free dipeptide D-Ala-D-Ala, which is the precursor for this pentapeptide sequence, allowing D-Ala-(R)- lactate (for which vancomycin has much less affinity) to be added to the cell wall instead. -!- The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala- D-Ala are not substrates. -!- Belongs to peptidase family M15.
|
UniProtKB Entries (1)
| Q06241 |
VANX_ENTFC
Enterococcus faecium
D-alanyl-D-alanine dipeptidase
|
PDB Structure
| PDB | 1R44 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The Structure of VanX Reveals a Novel Amino-Dipeptidase Involved in Mediating Transposon-Based Vancomycin Resistance
Mol.Cell
|