CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.390 | Neutral Protease; domain 2 |
|
1.10.390.10 | Neutral Protease Domain 2 |
Domain Context
CATH Clusters
| Superfamily | Neutral Protease Domain 2 |
| Functional Family | Leucyl-cystinyl aminopeptidase |
Enzyme Information
| 3.4.11.3 |
Cystinyl aminopeptidase.
based on mapping to UniProt Q9UIQ6
Release of an N-terminal amino acid, Cys-|-Xaa-, in which the half- cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however.
-!- Belongs to peptidase family M1.
|
UniProtKB Entries (1)
| Q9UIQ6 |
LCAP_HUMAN
Homo sapiens
Leucyl-cystinyl aminopeptidase
|
PDB Structure
| PDB | 5MJ6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity.
J. Med. Chem.
|
