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Information on EC 3.4.18.1 - cathepsin X

for references in articles please use BRENDA:EC3.4.18.1

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IUBMB Comments

Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family). The pH optimum is dependent on the substrate and is 5.0 for the carboxypeptidase activity. Unstable above pH 7.0. Compound E-64, leupeptin and antipain are inhibitors, but not cystatin C. Cathepsin X is ubiquitously distributed in mammalian tissues. The propeptide is extremely short (38 amino acid residues) and the proenzyme is catalytically active. Human gene locus: 20q13.

The enzyme appears in viruses and cellular organisms
Reaction Schemes
Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity

Synonyms
cathepsin x, cathepsin z, acid carboxypeptidase, cathepsin b2, lysosomal carboxypeptidase b, poctx, cysteine-type carboxypeptidase, mopre, more

REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity
show the reaction diagram