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EC Number
Natural Substrates
Commentary (Nat. Sub.)
alpha-enolase + H2O
cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
bradykinin + H2O
the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
CXCL-12 + H2O
CXCL-12 is a physiological substrate for secreted cathepsin X
gamma-enolase + H2O
cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
kallidin + H2O
the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
lymphocyte function associated antigen-1 + H2O
cathepsin X cleaves the beta2 cytoplasmic tail of LFA-1 inducing the intermediate affinity form of LFA-1 and alpha-actinin-1 binding. Cleavage by cathepsin X of the amino acid residues S769, E768 and A767 from the C-terminal of the b2 cytoplasmic tail of LFA-1 promotes binding of the actin-binding protein a-actinin-1
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active cathepsin X mediates the function of beta2 integrin receptors during cell adhesion. It could also be involved in other processes associated with beta2 integrin receptors such as phagocytosis and T cell activation
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cathepsin X plays a role not only in the chronic inflammation of gastric mucosa but also in the tumourigenesis of gastric cancer
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cathespin X is involved in phagocytosis and regulation of immune response, not involved in degradation of extracellular matrix, a proteolytic event leading to tumor cell invasion and metastasis
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cathepsin X binds to the membrane lectin endoplasmic reticulum Golgi intermediate compartment protein-53, ERGIC-53, involving the soluble luminal interaction partner multiple coagulation factor deficiency protein 2, MCFD2, which form a cargo receptor complex in the early secretory pathway, but is dispensable for enzyme binding, overview
Results 1 - 10 of 21 > >>