Cathepsin L
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.15 cathepsin L
Cathepsin L is a lysosomal cysteine endopeptidase in peptidase family C1 (papain family), readily inhibited by the diazomethane inhibitor Z-Phe-Phe-CHN2 or the epoxide inhibitor E-64. It resembles papain in specificity, and compared with cathepsin B it shows much higher activity on protein substrates but little activity on Z-Arg-Arg-NHMec and no peptidyl-dipeptidase activity. In cells it drives lysosomal proteolysis, antigen presentation and, when missecreted, extracellular matrix remodeling and cancer invasion. It features a papain-like catalytic fold.
Cathepsin L is a lysosomal cysteine endopeptidase in peptidase family C1 (papain family), readily inhibited by the diazomethane inhibitor Z-Phe-Phe-CHN2 or the epoxide inhibitor E-64. It resembles papain in specificity, and compared with cathepsin B it shows much higher activity on protein substrates but little activity on Z-Arg-Arg-NHMec and no peptidyl-dipeptidase activity. In cells it drives lysosomal proteolysis, antigen presentation and, when missecreted, extracellular matrix remodeling and cancer invasion. It features a papain-like catalytic fold.
References:
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