Cathepsin X
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.18 Cysteine-type carboxypeptidases > 3.4.18.1 cathepsin X
Cathepsin X (cathepsin P) is a lysosomal cysteine peptidase of family C1 (papain family); pH optimum depends on substrate and is 5.0 for carboxypeptidase activity, the enzyme is unstable above pH 7.0, inhibited by E-64, leupeptin and antipain but not cystatin C, ubiquitously distributed in mammalian tissues, the propeptide is extremely short (38 residues) and the proenzyme is catalytically active, with human gene locus 20q13; it releases C-terminal amino-acid residues with broad specificity but lacks action on C-terminal proline and shows weak endopeptidase activity. By trimming C-terminal residues it participates in lysosomal protein turnover and immune regulation. It appears in viruses and cellular organisms.
Cathepsin X (cathepsin P) is a lysosomal cysteine peptidase of family C1 (papain family); pH optimum depends on substrate and is 5.0 for carboxypeptidase activity, the enzyme is unstable above pH 7.0, inhibited by E-64, leupeptin and antipain but not cystatin C, ubiquitously distributed in mammalian tissues, the propeptide is extremely short (38 residues) and the proenzyme is catalytically active, with human gene locus 20q13; it releases C-terminal amino-acid residues with broad specificity but lacks action on C-terminal proline and shows weak endopeptidase activity. By trimming C-terminal residues it participates in lysosomal protein turnover and immune regulation. It appears in viruses and cellular organisms.
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