Bleomycin hydrolase
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.40 bleomycin hydrolase
Bleomycin hydrolase is a cytosolic cysteine peptidase that forms a homohexamer; each monomer has a papain-like tertiary structure in peptidase family C1, and the active sites lie on the walls of a central channel, with substrate access obstructed by the channel and by each C-terminus. Although bleomycin is unlikely to be the natural substrate, the enzyme inactivates bleomycin B2, a cytotoxic glycometallopeptide, by hydrolyzing a carboxyamide bond of beta-aminoalanine, and also shows general aminopeptidase activity, preferring amino acid arylamides of Met, Leu and Ala. In cells it contributes to peptide turnover and chemotherapy resistance. It features a ring-shaped hexamer with a catalytic cysteine in each subunit.
Bleomycin hydrolase is a cytosolic cysteine peptidase that forms a homohexamer; each monomer has a papain-like tertiary structure in peptidase family C1, and the active sites lie on the walls of a central channel, with substrate access obstructed by the channel and by each C-terminus. Although bleomycin is unlikely to be the natural substrate, the enzyme inactivates bleomycin B2, a cytotoxic glycometallopeptide, by hydrolyzing a carboxyamide bond of beta-aminoalanine, and also shows general aminopeptidase activity, preferring amino acid arylamides of Met, Leu and Ala. In cells it contributes to peptide turnover and chemotherapy resistance. It features a ring-shaped hexamer with a catalytic cysteine in each subunit.
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