background:
Bleomycin hydrolase (BMH) is a cytoplasmic cysteine peptidase that is highly conserved through evolution; however, the only known activity of the enzyme is metabolic inactivation of the glycopeptide bleomycin (BLM), an essential component of combination chemotherapy regimens for cancer. The protein contains the signature active site residues of the cysteine protease papain superfamily. [provided by RefSeq, Jul 2008].
Function:
BLMH is a member of the peptidase C1 family and exists as a homohexamer. While its normal physiological function is not known, it protects normal and malignant cells from the glycopeptide antitumor drug BLM. It inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine and also shows general aminopeptidase activity. The specificity varies but amino acid arylamides of Met, Leu and Ala are preferred.
Subunit:
Homohexamer.
Subcellular Location:
Cytoplasmic
Similarity:
Belongs to the peptidase C1 family.
Database links:
UniProtKB/Swiss-Prot: Q13867.
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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