CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.70 | Cathepsin D, subunit A; domain 1 |
|
2.40.70.10 | Acid Proteases |
Domain Context
CATH Clusters
| Superfamily | Acid Proteases |
| Functional Family | Endothiapepsin |
Enzyme Information
| 3.4.23.18 |
Aspergillopepsin I.
based on mapping to UniProt P0CU33
Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.
-!- Found in a variety of Aspergillus species (imperfect fungi): A.awamori, A.foetidus, A.fumigatus, A.kawachii, A.niger, A.oryzae, A.saitoi, and A.sojae. -!- Belongs to peptidase family A1. -!- Formerly EC 3.4.23.6.
|
UniProtKB Entries (1)
| P0CU33 |
PEPA_ASPOZ
Aspergillus oryzae
Aspergillopepsin-1
|
PDB Structure
| PDB | 1IZE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structures of Aspergillus oryzae aspartic proteinase and its complex with an inhibitor pepstatin at 1.9A resolution.
J.Mol.Biol.
|
