Bleomycin hydrolase (BLMH)

Bleomycin hydrolase is a **neutral cysteine protease enzyme** encoded by the BLMH gene in humans, best known for its role in inactivating bleomycin, an anticancer glycopeptide, via hydrolysis of the β-aminoalanine amide group, thereby limiting drug-induced DNA damage and toxicity[1][2][4][5][7]. It belongs to the papain superfamily, is widely expressed in human tissues, and shows significant evolutionary conservation[2][5]. BLMH has additional key physiological roles: in the **skin**, it aids in the final degradation steps of filaggrin, contributing to natural moisturizing factors and skin barrier integrity, with loss of function linked to conditions such as atopic dermatitis and psoriasis[3][5]. It also processes homocysteine thiolactone, potentially conferring neuroprotective effects, and participates in immune antigen processing and regulation of inflammatory chemokine release[3][5][6]. BLMH deficiency or dysfunction can result in hypersensitivity to bleomycin, increased risk of drug-induced pulmonary fibrosis, skin barrier compromise, and aberrant wound healing responses[3][5]. Genetic polymorphisms of BLMH have clinical relevance as predictors of patient responses and side effects to bleomycin-containing chemotherapy regimens[3][4][5].

Other names

BLMHBHBMHBLM hydrolasebleomycin hydrolase

Hydrolysis (inactivation) of bleomycin via deamidation[1][2][4][5][7]; Protection against bleomycin-induced DNA damage and toxicity[1][4][5]