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 P24228
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.
3.4.21.-
Serine endopeptidases.
based on mapping to UniProt P24228

UniProtKB Entries (1)

P24228
DACB_ECOLI
Escherichia coli K-12
D-alanyl-D-alanine carboxypeptidase DacB

PDB Structure

PDB 2EX9
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics
Kishida, H., Unzai, S., Roper, D.I., Lloyd, A., Park, S.-Y., Tame, J.R.H.
Biochemistry