| Official Name |
| Bleomycin hydrolase.
|
| Alternative Name(s) |
| Aminopeptidase C (Lactococcus lactis). |
| Reaction catalysed |
| 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 |
| Comment(s) |
- 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.
|
| Cross-references |
| PROSITE | PDOC00126 |
| BRENDA | 3.4.22.40 |
| PUMA2 | 3.4.22.40 |
| PRIAM enzyme-specific profiles | 3.4.22.40 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.22.40 |
| IUBMB Enzyme Nomenclature | 3.4.22.40 |
| IntEnz | 3.4.22.40 |
| MEDLINE | Find literature relating to 3.4.22.40 |
| MetaCyc | 3.4.22.40 |
| UniProtKB/Swiss-Prot |
| Q01532, BLH1_YEAST; | P87362, BLMH_CHICK; | Q13867, BLMH_HUMAN; |
| Q8R016, BLMH_MOUSE; | P13019, BLMH_RABIT; | P70645, BLMH_RAT; |
| Q48543, PEPC_LACDL; | Q10744, PEPC_LACHE; | Q9CEG3, PEPC_LACLA; |
| Q04723, PEPC_LACLC; | Q928V0, PEPC_LISIN; | O69192, PEPC_LISMO; |
| Q56115, PEPC_STRTR; |
|