3.4.18.1	alpha-enolase + H2O	cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity	
3.4.18.1	bradykinin + H2O	the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand	
3.4.18.1	CXCL-12 + H2O	CXCL-12 is a physiological substrate for secreted cathepsin X	
3.4.18.1	gamma-enolase + H2O	cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity	
3.4.18.1	kallidin + H2O	the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand	
3.4.18.1	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	
3.4.18.1	additional information	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	
3.4.18.1	additional information	cathepsin X plays a role not only in the chronic inflammation of gastric mucosa but also in the tumourigenesis of gastric cancer	
3.4.18.1	additional information	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	
3.4.18.1	additional information	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