CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.710 | Beta-lactamase |
|
3.40.710.10 | DD-peptidase/beta-lactamase superfamily |
Domain Context
CATH Clusters
| Superfamily | DD-peptidase/beta-lactamase superfamily |
| Functional Family |
Enzyme Information
| 3.4.16.4 |
Serine-type D-Ala-D-Ala carboxypeptidase.
based on mapping to UniProt P15555
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)
| P15555 |
DAC_STRSR
Streptomyces sp. R61
D-alanyl-D-alanine carboxypeptidase
|
PDB Structure
| PDB | 1CEF |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases.
Biochemistry
|
