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 Q12567
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)
| Q12567 |
PEPA_ASPPH
Aspergillus phoenicis
Aspergillopepsin-1
|
PDB Structure
| PDB | 1IBQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of aspergillopepsin I from Aspergillus phoenicis: variations of the S1'-S2 subsite in aspartic proteinases.
Acta Crystallogr.,Sect.D
|