CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.25 | Alpha Horseshoe |
|
1.25.50 | Zincin-like fold |
|
1.25.50.10 | Peptidase M1, alanyl aminopeptidase, C-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Peptidase M1, alanyl aminopeptidase, C-terminal domain |
| Functional Family | Aminopeptidase N |
Enzyme Information
| 3.4.11.2 |
Membrane alanyl aminopeptidase.
based on mapping to UniProt P04825
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
-!- Is not activated by heavy metal ions. -!- Belongs to peptidase family M1. -!- Formerly EC 3.4.1.2, EC 3.4.3.5 and EC 3.4.13.6.
|
UniProtKB Entries (1)
| P04825 |
AMPN_ECOLI
Escherichia coli K-12
Aminopeptidase N
|
PDB Structure
| PDB | 2DQM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli: Crystal structure and conformational change of the methionine 260 residue involved in substrate recognition
J.Biol.Chem.
|