CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.80 | D-tyrosyl-trna(Tyr) Deacylase; Chain: A; |
|
3.50.80.20 | D-Ala-D-Ala carboxypeptidase C, peptidase S13 |
Domain Context
CATH Clusters
| Superfamily | D-Ala-D-Ala carboxypeptidase C, peptidase S13 |
| Functional Family |
Enzyme Information
| 3.4.16.4 |
Serine-type D-Ala-D-Ala carboxypeptidase.
based on mapping to UniProt P39045
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)
| P39045 |
DAC_ACTSP
Actinomadura sp. R39
D-alanyl-D-alanine carboxypeptidase
|
PDB Structure
| PDB | 1W8Q |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal Structure of the Actinomadura R39 Dd-Peptidase Reveals New Domains in Penicillin-Binding Proteins.
J.Biol.Chem.
|