CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.70 | Cathepsin B; Chain A |
|
3.90.70.10 | Cysteine proteinases |
Domain Context
CATH Clusters
| Superfamily | Cysteine proteinases |
| Functional Family | Aminopeptidase C |
Enzyme Information
| 3.4.22.40 |
Bleomycin hydrolase.
based on mapping to UniProt Q01532
Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred.
-!- The active sites are on the walls of a central channel through the molecule, and access of substrate molecules to them is obstructed by this and by the C-terminus of each polypeptide chain. -!- Bleomycin can scarcely be the natural substrate, and there are reports of limited endopeptidase activity. -!- Known from bacteria as well as eukaryotic organisms. -!- Hydrolase H from chicken muscle has many similarities to bleomycin hydrolase, but hydrolyzes Ph-CO-Arg-2-naphthylamine as well as aminopeptidase substrates. -!- Belongs to peptidase family C1.
|
UniProtKB Entries (1)
| Q01532 |
BLH1_YEAST
Saccharomyces cerevisiae S288C
Cysteine proteinase 1, mitochondrial
|
PDB Structure
| PDB | 3GCB |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase.
Cell(Cambridge,Mass.)
|
