BLM hydrolase Inhibitors

The class of BLMH inhibitors would include a variety of chemical compounds that can interfere with the enzyme's ability to inactivate bleomycin. Since BLMH is a cysteine protease, inhibitors like N-Ethylmaleimide and Iodoacetamide could modify the thiol group of the active site cysteine, rendering the enzyme inactive.

Additionally chemicals such as E-64 and leupeptin, which target cysteine proteases, may also form a covalent bond with the active site cysteine of BLMH. Other protease inhibitors that are not specific to cysteine residues, such as PMSF, aprotinin, and chymostatin, could also inhibit BLMH. Compounds like MG-132 and lactacystin are known to inhibit the proteasome and may affect BLMH through non-specific binding.Overall, BLMH inhibitors would thus be characterized by their ability to bind to and interfere with the active site or other critical regions of the BLM hydrolase enzyme, preventing it from carrying out its normal function of bleomThe protein BLM hydrolase. Direct inhibitors of BLMH could potentiate the activity of bleomycin by preventing its inactivation.