CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.10740 | Class I glutamine amidotransferase-like |
Domain Context
CATH Clusters
| Superfamily | Class I glutamine amidotransferase-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 | 2AUN |
| 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.
J.Biol.Chem.
|
