CATH Classification

Domain Context

CATH Clusters

Superfamily Cysteine proteinases
Functional Family Aminopeptidase C

Enzyme Information
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)

Saccharomyces cerevisiae S288C
Cysteine proteinase 1, mitochondrial

PDB Structure

External Links
Organism Escherichia
Primary Citation
The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase.
Zheng, W., Johnston, S.A., Joshua-Tor, L.