CATH Classification

Domain Context

CATH Clusters

Superfamily Cysteine proteinases
Functional Family Bleomycin hydrolase

Enzyme Information

3.4.22.40
Bleomycin hydrolase.
based on mapping to UniProt Q13867
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)

Q13867
BLMH_HUMAN
Homo sapiens
Bleomycin hydrolase

PDB Structure

PDB 1CB5
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of human bleomycin hydrolase, a self-compartmentalizing cysteine protease.
O'Farrell, P.A., Gonzalez, F., Zheng, W., Johnston, S.A., Joshua-Tor, L.
Structure Fold.Des.