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 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 | 2Y4A |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Unexpected Tricovalent Binding Mode of Boronic Acids within the Active Site of a Penicillin- Binding Protein.
J.Am.Chem.Soc.
|