CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.630 | Aminopeptidase |
|
3.40.630.10 | Zn peptidases |
Domain Context
CATH Clusters
| Superfamily | Zn peptidases |
| Functional Family |
Enzyme Information
| 3.4.11.10 |
Bacterial leucyl aminopeptidase.
based on mapping to UniProt Q01693
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
-!- Similar aminopeptidases were isolated from Escherichia coli and Staphylococcus thermophilus. -!- Belongs to peptidase families M17 and M28.
|
UniProtKB Entries (1)
| Q01693 |
AMPX_VIBPR
Vibrio proteolyticus
Bacterial leucyl aminopeptidase
|
PDB Structure
| PDB | 3B7I |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus.
Biochemistry
|
