CATH Classification

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.
Sauvage, E., Herman, R., Petrella, S., Duez, C., Bouillenne, F., Frere, J.M., Charlier, P.
J.Biol.Chem.