CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1720 | endopeptidase fold (from Nostoc punctiforme) |
|
3.90.1720.10 | endopeptidase domain like (from Nostoc punctiforme) |
Domain Context
CATH Clusters
| Superfamily | endopeptidase domain like (from Nostoc punctiforme) |
| Functional Family | Bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase |
Enzyme Information
| 3.4.17.13 |
Muramoyltetrapeptide carboxypeptidase.
based on mapping to UniProt P0AFV4
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.
|
| 3.4.-.- |
Acting on peptide bonds (peptidases).
based on mapping to UniProt P0AFV4
|
UniProtKB Entries (1)
| P0AFV4 |
MEPS_ECOLI
Escherichia coli K-12
Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase
|
PDB Structure
| PDB | 2K1G |
| External Links | |
| Method | SOLUTION NMR |
| Organism | Escherichia |
| Primary Citation |
Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad.
Biochemistry
|