CATH Classification

Domain Context

CATH Clusters

Superfamily LD-carboxypeptidase A C-terminal domain-like
Functional Family

Enzyme Information

3.4.17.13
Muramoyltetrapeptide carboxypeptidase.
based on mapping to UniProt Q9HTZ1
GlcNAc-MurNAc-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanine + H(2)O = GlcNAc-MurNAc-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + D-alanine.
-!- Variants are known from various microorganisms. -!- Involved in peptidoglycan synthesis, catalyzing both decarboxylation and transpeptidation. -!- Stimulated by divalent cations such as magnesium and calcium, but not zinc. -!- Inhibited by thiol-blocking reagents, but unaffected by penicillin.

UniProtKB Entries (1)

Q9HTZ1
LDC_PSEAE
Pseudomonas aeruginosa PAO1
Murein tetrapeptide carboxypeptidase

PDB Structure

PDB 1ZRS
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow.
Korza, H.J., Bochtler, M.
J.Biol.Chem.