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 | Aspartic protease pep1 |
Enzyme Information
| 3.4.23.20 |
Penicillopepsin.
based on mapping to UniProt P00798
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.
-!- From the imperfect fungus Penicillium janthinellum. -!- Closely related enzymes have been isolated from P.roqueforti and P.duponti. -!- Belongs to peptidase family A1. -!- Formerly EC 3.4.4.17, EC 3.4.23.6 and EC 3.4.23.7.
|
UniProtKB Entries (1)
| P00798 |
PEPA1_PENJA
Penicillium janthinellum
Penicillopepsin-1
|
PDB Structure
| PDB | 1APT |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystallographic Analysis of a Pepstatin Analogue Binding to the Aspartyl Proteinase Penicillopepsin at 1.8 Angstroms Resolution
Peptides: Structure and Function, Proceedings of the of the Eighth American Peptide Symposium
|
