CATH Classification

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.
Kuzin, A.P., Liu, H., Kelly, J.A., Knox, J.R.
Biochemistry