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(2,4-dinitrophenyl)-GFFGW + H2O
(2,4-dinitrophenyl)-GFFG + L-Trp
-
-
-
?
(2,4-dinitrophenyl)-GFFRW + H2O
(2,4-dinitrophenyl)-GFFR + L-Trp
-
-
-
?
(2,4-dinitrophenyl)-GFFW + H2O
(2,4-dinitrophenyl)-GFF + L-Trp
-
-
-
?
(2,4-dinitrophenyl)-GFRFW + H2O
(2,4-dinitrophenyl)-GFR + L-Phe-L-Trp
-
-
-
?
(2,4-dinitrophenyl)-GFRW + H2O
(2,4-dinitrophenyl)-GFR + L-Trp
-
-
-
?
(2,4-dinitrophenyl)-GRFFW + H2O
(2,4-dinitrophenyl)-GRFF + L-Trp
-
-
-
?
(2-aminobenzoyl)-FFF + H2O
(2-aminobenzoyl)-FF + L-Phe
-
-
-
?
(2-aminobenzoyl)-FFFA + H2O
(2-aminobenzoyl)-FFF + L-Ala
-
-
-
?
(2-aminobenzoyl)-FFFP + H2O
(2-aminobenzoyl)-FFF + Pro
-
-
-
?
(2-aminobenzoyl)-FFFR + H2O
(2-aminobenzoyl)-FFF + L-Arg
-
-
-
?
(2-aminobenzoyl)-FFFR-NH2 + H2O
(2-aminobenzoyl)-FFF + Arg-amide
-
-
-
?
(2-aminobenzoyl)-FFFW + H2O
(2-aminobenzoyl)-FFF + L-Trp
-
-
-
?
(2-aminobenzoyl)-FFGW + H2O
(2-aminobenzoyl)-FFG + L-Trp
-
-
-
?
(2-aminobenzoyl)-FFRW + H2O
(2-aminobenzoyl)-FFR + L-Trp
-
-
-
?
(2-aminobenzoyl)-FFRW-NH2 + H2O
(2-aminobenzoyl)-FFR + L-Trp-amide
-
-
-
?
(2-aminobenzoyl)-FRFW-NH2 + H2O
(2-aminobenzoyl)-FR + Phe-Trp-amide
-
-
-
?
2-aminobenzoyl-Ala-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Ala-Arg + 4-nitrophenylalanine
kcat/Km is 20/mM * s
-
-
?
2-aminobenzoyl-Arg-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
2-aminobenzoyl-Arg-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Arg-Arg + 4-nitrophenylalanine
kcat/Km is 5.2/mM * s
-
-
?
2-aminobenzoyl-Asn-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Asn-Arg + 4-nitrophenylalanine
kcat/Km is 17/mM * s
-
-
?
2-aminobenzoyl-Asp-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Asp-Arg + 4-nitrophenylalanine
kcat/Km is 16/mM * s
-
-
?
2-aminobenzoyl-Cys-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Cys-Arg + 4-nitrophenylalanine
kcat/Km is 11/mM * s
-
-
?
2-aminobenzoyl-Gln-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Gln-Arg + 4-nitrophenylalanine
kcat/Km is 43/mM * s
-
-
?
2-aminobenzoyl-Glu-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Glu-Arg + 4-nitrophenylalanine
kcat/Km is 27/mM * s
-
-
?
2-aminobenzoyl-Gly-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Gly-Arg + 4-nitrophenylalanine
kcat/Km is 4.4/mM * s
-
-
?
2-aminobenzoyl-His-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-His-Arg + 4-nitrophenylalanine
kcat/Km is 4.7/mM * s
-
-
?
2-aminobenzoyl-Ile-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Ile-Arg + 4-nitrophenylalanine
kcat/Km is 2.7/mM * s
-
-
?
2-aminobenzoyl-Leu-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
2-aminobenzoyl-Leu-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Leu-Arg + 4-nitrophenylalanine
kcat/Km is 153/mM * s
-
-
?
2-aminobenzoyl-Lys-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Lys-Arg + 4-nitrophenylalanine
kcat/Km is 5.7/mM * s
-
-
?
2-aminobenzoyl-Met-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Met-Arg + 4-nitrophenylalanine
kcat/Km is 28/mM * s
-
-
?
2-aminobenzoyl-Phe-Ala-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Ala + 4-nitrophenylalanine
kcat/Km is 51/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
2-aminobenzoyl-Phe-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Arg + 4-nitrophenylalanine
kcat/Km is 100/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Ala + H2O
2-aminobenzoyl-Phe-Arg + Ala
kcat/Km is 10/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Arg + H2O
2-aminobenzoyl-Phe-Arg + Arg
kcat/Km is 1.7/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Asn + H2O
2-aminobenzoyl-Phe-Arg + Asn
kcat/Km is 5.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Asp + H2O
2-aminobenzoyl-Phe-Arg + Asp
kcat/Km is 8.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Cys + H2O
2-aminobenzoyl-Phe-Arg + Cys
kcat/Km is 73/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Gln + H2O
2-aminobenzoyl-Phe-Arg + Gln
kcat/Km is 4.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Glu + H2O
2-aminobenzoyl-Phe-Arg + Glu
kcat/Km is 7.7/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Gly + H2O
2-aminobenzoyl-Phe-Arg + Gly
kcat/Km is 14/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-His + H2O
2-aminobenzoyl-Phe-Arg + His
kcat/Km is 5.4/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Ile + H2O
2-aminobenzoyl-Phe-Arg + Ile
kcat/Km is 3.4/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Leu + H2O
2-aminobenzoyl-Phe-Arg + Leu
kcat/Km is 7.1/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Lys + H2O
2-aminobenzoyl-Phe-Arg + Lys
kcat/Km is 5.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Met + H2O
2-aminobenzoyl-Phe-Arg + Met
kcat/Km is 9.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Phe + H2O
2-aminobenzoyl-Phe-Arg + Phe
kcat/Km is 15/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Ser + H2O
2-aminobenzoyl-Phe-Arg + Ser
kcat/Km is 48/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Thr + H2O
2-aminobenzoyl-Phe-Arg + Thr
kcat/Km is 5.8/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Trp + H2O
2-aminobenzoyl-Phe-Arg + Trp
kcat/Km is 8.6/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Tyr + H2O
2-aminobenzoyl-Phe-Arg + Tyr
kcat/Km is 8.8/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Val + H2O
2-aminobenzoyl-Phe-Arg + Val
kcat/Km is 5.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Asn-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Asn + 4-nitrophenylalanine
kcat/Km is 13/mM * s
-
-
?
2-aminobenzoyl-Phe-Asp-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Asp + 4-nitrophenylalanine
kcat/Km is 12/mM * s
-
-
?
2-aminobenzoyl-Phe-Cys-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Cys + 4-nitrophenylalanine
kcat/Km is 17/mM * s
-
-
?
2-aminobenzoyl-Phe-Gln-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Gln + 4-nitrophenylalanine
kcat/Km is 73/mM * s
-
-
?
2-aminobenzoyl-Phe-Glu-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Glu + 4-nitrophenylalanine
kcat/Km is 62/mM * s
-
-
?
2-aminobenzoyl-Phe-Gly-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Gly + 4-nitrophenylalanine
kcat/Km is 45/mM * s
-
-
?
2-aminobenzoyl-Phe-His-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-His + 4-nitrophenylalanine
kcat/Km is 3.5/mM * s
-
-
?
2-aminobenzoyl-Phe-Ile-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Ile + 4-nitrophenylalanine
kcat/Km is 4.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Leu-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Leu + 4-nitrophenylalanine
kcat/Km is 2.0/mM * s
-
-
?
2-aminobenzoyl-Phe-Lys-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Lys + 4-nitrophenylalanine
kcat/Km is 79/mM * s
-
-
?
2-aminobenzoyl-Phe-Met-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Met + 4-nitrophenylalanine
kcat/Km is 181/mM * s
-
-
?
2-aminobenzoyl-Phe-Phe-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Phe + 4-nitrophenylalanine
kcat/Km is 108/mM * s
-
-
?
2-aminobenzoyl-Phe-Ser-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Ser + 4-nitrophenylalanine
kcat/Km is 32/mM * s
-
-
?
2-aminobenzoyl-Phe-Thr-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Thr + 4-nitrophenylalanine
kcat/Km is 68/mM * s
-
-
?
2-aminobenzoyl-Phe-Trp-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Trp + 4-nitrophenylalanine
kcat/Km is 1.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Tyr-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Tyr + 4-nitrophenylalanine
kcat/Km is 58/mM * s
-
-
?
2-aminobenzoyl-Phe-Val-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Val + 4-nitrophenylalanine
kcat/Km is 4.8/mM * s
-
-
?
2-aminobenzoyl-Pro-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Pro-Arg + 4-nitrophenylalanine
kcat/Km is 0.2/mM * s
-
-
?
2-aminobenzoyl-Ser-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Ser-Arg + 4-nitrophenylalanine
kcat/Km is 8.2/mM * s
-
-
?
2-aminobenzoyl-Thr-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Thr-Arg + 4-nitrophenylalanine
kcat/Km is 8.7/mM * s
-
-
?
2-aminobenzoyl-Trp-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Trp-Arg + 4-nitrophenylalanine
kcat/Km is 12/mM * s
-
-
?
2-aminobenzoyl-Tyr-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Tyr-Arg + 4-nitrophenylalanine
kcat/Km is 400/mM * s
-
-
?
2-aminobenzoyl-Val-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Val-Arg + 4-nitrophenylalanine
kcat/Km is 31/mM * s
-
-
?
3-aminobenzoyl-FR-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P + H2O
3-aminobenzoyl-FR + (2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P
-
-
-
?
3-aminobenzoyl-LR-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P + H2O
3-aminobenzoyl-LR + (2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P
-
-
-
?
3-aminobenzoyl-RR-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P + H2O
3-aminobenzoyl-RR + (2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P
-
-
-
?
7-methoxycoumarin-4-ylacetyl-RPPGFSAFK-N-epsilon-2,4-dinitrophenol + H2O
?
fluorescence cathepsin X/A-selective substrate
-
-
?
Abz-Phe-Glu-Lys(Dnp)-OH + H2O
?
-
-
-
-
?
AKYNQLMRIEEELGEEARFAGHNFRNPSVL + H2O
?
-
a model peptide derived from rat gamma-enolase carboxyl terminal, overview
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
61% of the activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
34% of the activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-FR-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-FR + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Leu-Glu + 7-amino-4-methylcoumarin
54% of the activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-RR-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-RR + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Val-Arg + 7-amino-4-methylcoumarin
12% of the activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
biotinyl-KKQ20KK + H2O
?
-
-
within the lysosome, the major endoprotease, cathepsin L, carries out an initial attack within the polyglutamine repeat, which generates new C termini, facilitating the actions of the carboxypeptidase cathepsin Z. Extracts containing both cathespin L and Z show multiple cleavages within the polyglutamine sequence of biotinyl-KKQ20KK, generating a variety of fragments, including biotinyl-KKQ4,biotinyl-KKQ8, Q12KK, andQ16KK
-
?
bradykinin + H2O
?
-
the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg, a mainly B2 receptor
an exclusive B1 receptor
-
?
Glucagon + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
hippuryl-L-glutamic acid + H2O
hippuric acid + L-Glu
-
-
-
-
?
KAKFAGRNPRNPLAK + H2O
?
-
a model peptide derived from human alpha-enolase carboxyl terminal, overview
-
-
?
kallidin + H2O
?
-
the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
-
-
?
kallidin + H2O
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
i.e. Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg, a mainly B2 receptor
an exclusive B1 receptor
-
?
lymphocyte function associated antigen-1 + H2O
?
ortho-aminobenzoyl-Arg-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
ortho-aminobenzoyl-Lys-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
ortho-aminobenzoyl-Phe-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
profilin + H2O
L-tyrosine + ?
cathepsin X cleaves profilin 1 C-terminal Tyr139 and influences clathrin-mediated endocytosis. Tyr139 is important for proper function of profilin 1 as a tumor suppressor. Cleaving off Tyr139 prevents the binding of clathrin, a poly-L-proline ligand involved in endocytosis
-
-
?
profilin 1 + H2O
?
the molecular target of cathepsin X in tumor cells is profilin 1, a known tumor suppressor and regulator of actin cytoskeleton dynamics. Cathepsin X cleaves off the C-terminal Tyr139 of profilin 1, affecting binding of poly-L-proline ligands and, consequently, tumor cell migration and invasion. Tyr139 is important for proper function of profilin 1 as a tumor suppressor. Cleaving off Tyr139 prevents the binding of clathrin, a poly-L-proline ligand involved in endocytosis
-
-
?
Proteins + H2O
?
-
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
additional information
?
-
alpha-enolase + H2O
?
-
cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
-
-
?
alpha-enolase + H2O
?
-
cathepsin X cleaves the C-terminal dipeptide
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
CXCL-12 + H2O
?
CXCL-12 is a physiological substrate for secreted cathepsin X
-
-
?
CXCL-12 + H2O
?
chemokine CXCL-12 is a highly potent chemoattractant for HSC secreted by osteoblasts. The exo-peptidase cathepsin X gradually cleaves fifteen amino acids until proline P74 is present at the P2 position
-
-
?
gamma-enolase + H2O
?
-
cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
-
-
?
gamma-enolase + H2O
?
-
cathepsin X cleaves the C-terminal dipeptide
-
-
?
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
-
-
?
lymphocyte function associated antigen-1 + H2O
?
-
cathepsin X cleaves the amino acid residues S769, E768 and A767 from the C-terminal of LFA-1
-
-
?
additional information
?
-
-
no cleavage when Pro in the last or penultimate position
-
-
?
additional information
?
-
-
in addition, enzyme shows cysteine endopeptidase activity degrading gelatin, IgG and type I collagen
-
-
?
additional information
?
-
-
the enzyme normally acts as a carboxymonopeptidase. The preference for Arg in the P1 position is so strong that cathepsin X cleaves substrates with Arg in antepenultimate position, acting also as a carboxypeptidase. A large hydrophobic residue such as Trp is preferred in the P1' position, although the enzyme cleaves all P1' residues investigated (Trp, Phe, Ala, Arg, Pro). The enzyme also cleaves the substrates with amide-blocked C-terminal carboxyl group with rates similar to that of the unblocked substrates
-
?
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
-
-
?
additional information
?
-
-
cathepsin X plays a role not only in the chronic inflammation of gastric mucosa but also in the tumourigenesis of gastric cancer
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
luminal protein-protein interactions between components of the cargo system in the endoplasmic reticulum for secretion of cargo proteins, e.g. cathepsin C or cathepsin Z, involve the cargo transport receptor ERGIC-53, i.e. endoplasmic reticulum-Golgi intermediate compartment protein of 53 kDa, with its luminal interaction partner MCFD2, i.e. multiple coagulation factor deficiency protein 2, MCFD2 is not required for the binding of cathepsin Z and cathepsin C to ERGIC-53 in vivo, overview
-
-
?
additional information
?
-
procathepsin X supports integrin alphavbeta3-dependent attachment and spreading of umbilical vein endothelial cells, overvie
-
-
?
additional information
?
-
-
procathepsin X supports integrin alphavbeta3-dependent attachment and spreading of umbilical vein endothelial cells, overvie
-
-
?
additional information
?
-
-
the enzyme is associated with plaques in Alzheimer patients, overview
-
-
?
additional information
?
-
the enzyme plays a role in immunity to pathogens including Mycobacterium tuberculosis, variation in the melanocortin 3 receptor and cathepsin Z genes play a role in the pathogenesis of tuberculosis in West African populations
-
-
?
additional information
?
-
-
the enzyme plays a role in immunity to pathogens including Mycobacterium tuberculosis, variation in the melanocortin 3 receptor and cathepsin Z genes play a role in the pathogenesis of tuberculosis in West African populations
-
-
?
additional information
?
-
-
the enzyme stimulates macrophage antigen-1 receptor-dependent adhesion and phagocytosis via interaction with integrin beta2 subunit. It plays a role in regulating lymphocyte proliferation via Mac-1 and the other b2 integrin receptor, lymphocyte function-associated antigen-1. Cathepsin X has been shown to suppress proliferation of peripheral blood mononuclear cells, by activation of Mac-1, known as a suppressive factor for lymphocyte proliferation, co-localization of cathepsin X and LFA-1 enhances lymphocyte proliferation, overview
-
-
?
additional information
?
-
cathepsin X interacts with the membrane lectin endoplasmic reticulum Golgi intermediate compartment protein-53, ERGIC-53
-
-
?
additional information
?
-
direct interaction between the enzyme and integrin alphavbeta3, overview
-
-
?
additional information
?
-
-
direct interaction between the enzyme and integrin alphavbeta3, overview
-
-
?
additional information
?
-
luminal protein-protein interactions between components of the cargo system in the endoplasmic reticulum for secretion of cargo proteins, e.g. cathepsin C or cathepsin Z, involve the cargo transport receptor ERGIC-53, i.e. endoplasmic reticulum-Golgi intermediate compartment protein of 53 kDa, with its luminal interaction partner MCFD2, i.e. multiple coagulation factor deficiency protein 2, inactivation of ERGIC-53s lectin domain by the N156A point mutation selectively decreases the interaction of ERGIC-53 with its cargo proteins cathepsin Z and cathepsin C, whereas the N156A mutation does not affect ERGIC-53 oligomerization or its interaction with MCFD2, overview
-
-
?
additional information
?
-
cathepsin X acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins
-
-
?
additional information
?
-
-
cathepsin X acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins
-
-
?
additional information
?
-
cathepsin X is an important regulator of LFA-1 activity, and cathepsin X-upregulated Jurkat T cells exhibit increased homotypic aggregation, cathepsin X induces polarized migration-associated morphology in Jurkat T cells, overview
-
-
?
additional information
?
-
-
co-localization of alpha or gamma enolase and cathepsin X. Cathepsin X impairs survival and neuritogenesis of neuronal cells, e.g. it reduces PC12 cell survival and neuritogenesis
-
-
?
additional information
?
-
-
CATX is an important player in the spinal mechanisms involved in chronic pain induction and maintenance
-
-
?
additional information
?
-
-
CATX is widely expressed in the brain and is implicated in several neurological conditions such as Alzheimer's disease, amyotrophic lateral sclerosis and age-related inflammation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
profilin + H2O
L-tyrosine + ?
cathepsin X cleaves profilin 1 C-terminal Tyr139 and influences clathrin-mediated endocytosis. Tyr139 is important for proper function of profilin 1 as a tumor suppressor. Cleaving off Tyr139 prevents the binding of clathrin, a poly-L-proline ligand involved in endocytosis
-
-
?
profilin 1 + H2O
?
the molecular target of cathepsin X in tumor cells is profilin 1, a known tumor suppressor and regulator of actin cytoskeleton dynamics. Cathepsin X cleaves off the C-terminal Tyr139 of profilin 1, affecting binding of poly-L-proline ligands and, consequently, tumor cell migration and invasion. Tyr139 is important for proper function of profilin 1 as a tumor suppressor. Cleaving off Tyr139 prevents the binding of clathrin, a poly-L-proline ligand involved in endocytosis
-
-
?
Proteins + H2O
?
-
-
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
cathepsin X plays a role not only in the chronic inflammation of gastric mucosa but also in the tumourigenesis of gastric cancer
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
luminal protein-protein interactions between components of the cargo system in the endoplasmic reticulum for secretion of cargo proteins, e.g. cathepsin C or cathepsin Z, involve the cargo transport receptor ERGIC-53, i.e. endoplasmic reticulum-Golgi intermediate compartment protein of 53 kDa, with its luminal interaction partner MCFD2, i.e. multiple coagulation factor deficiency protein 2, MCFD2 is not required for the binding of cathepsin Z and cathepsin C to ERGIC-53 in vivo, overview
-
-
?
additional information
?
-
procathepsin X supports integrin alphavbeta3-dependent attachment and spreading of umbilical vein endothelial cells, overvie
-
-
?
additional information
?
-
-
procathepsin X supports integrin alphavbeta3-dependent attachment and spreading of umbilical vein endothelial cells, overvie
-
-
?
additional information
?
-
-
the enzyme is associated with plaques in Alzheimer patients, overview
-
-
?
additional information
?
-
the enzyme plays a role in immunity to pathogens including Mycobacterium tuberculosis, variation in the melanocortin 3 receptor and cathepsin Z genes play a role in the pathogenesis of tuberculosis in West African populations
-
-
?
additional information
?
-
-
the enzyme plays a role in immunity to pathogens including Mycobacterium tuberculosis, variation in the melanocortin 3 receptor and cathepsin Z genes play a role in the pathogenesis of tuberculosis in West African populations
-
-
?
additional information
?
-
-
the enzyme stimulates macrophage antigen-1 receptor-dependent adhesion and phagocytosis via interaction with integrin beta2 subunit. It plays a role in regulating lymphocyte proliferation via Mac-1 and the other b2 integrin receptor, lymphocyte function-associated antigen-1. Cathepsin X has been shown to suppress proliferation of peripheral blood mononuclear cells, by activation of Mac-1, known as a suppressive factor for lymphocyte proliferation, co-localization of cathepsin X and LFA-1 enhances lymphocyte proliferation, overview
-
-
?
additional information
?
-
cathepsin X acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins
-
-
?
additional information
?
-
-
cathepsin X acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins
-
-
?
additional information
?
-
cathepsin X is an important regulator of LFA-1 activity, and cathepsin X-upregulated Jurkat T cells exhibit increased homotypic aggregation, cathepsin X induces polarized migration-associated morphology in Jurkat T cells, overview
-
-
?
additional information
?
-
-
co-localization of alpha or gamma enolase and cathepsin X. Cathepsin X impairs survival and neuritogenesis of neuronal cells, e.g. it reduces PC12 cell survival and neuritogenesis
-
-
?
additional information
?
-
-
CATX is an important player in the spinal mechanisms involved in chronic pain induction and maintenance
-
-
?
additional information
?
-
-
CATX is widely expressed in the brain and is implicated in several neurological conditions such as Alzheimer's disease, amyotrophic lateral sclerosis and age-related inflammation
-
-
?
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Edge, M.; Forder, C.; Hennam, J.; Lee, I.; Tonge, D.; Hardern, I.; Fitton, J.; Eckersley, K.; East, S.; Shufflebotham, A.; Blakey, D.; Slater, A.
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Homo sapiens
brenda
Afroz, H.; Otto, K.; Mueller, R.; Fuhge, P.
On the specificity of bovine spleen cathepsin B2
Biochim. Biophys. Acta
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1976
Bos taurus
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Ninjoor, V.; Taylor, S.L.; Tappel, A.L.
Purification and characterization of rat liver lysosomal cathepsin B2
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Rattus norvegicus
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De Lumen, B.O.; Tappel, A.L.
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Rattus norvegicus
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Distelmaier, P.; Huebner, H.; Otto, K.
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Rattus norvegicus
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Otto, K.; Riesenknig, H.
Improved purification of cathepsin B1 and cathepsin B2
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Bos taurus
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Klemencic, I.; Carmona, A.K.; Cezari, M.H.; Juliano, M.A.; Juliano, L.; Guncar, G.; Turk, D.; Krizaj, I.; Turk, V.; Turk, B.
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Homo sapiens
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Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease
Structure Fold. Des.
8
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2000
Homo sapiens
brenda
Devanathan, G.; Turnbull, J.L.; Ziomek, E.; Purisima, E.O.; Menard, R.; Sulea, T.
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Homo sapiens (Q9UBR2), Homo sapiens
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Kos, J.; Sekirnik, A.; Premzl, A.; Zavasnik Bergant, V.; Langerholc, T.; Turk, B.; Werle, B.; Golouh, R.; Repnik, U.; Jeras, M.; Turk, V.
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2005
Homo sapiens
brenda
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2006
Homo sapiens
brenda
Ngler, D.K.; Lechner, A.M.; Oettl, A.; Kozaczynska, K.; Scheuber, H.P.; Gippner-Steppert, C.; Bogner, V.; Biberthaler, P.; Jochum, M.
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Homo sapiens
brenda
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Homo sapiens
brenda
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Tumor cell-derived and macrophage-derived cathepsin B promotes progression and lung metastasis of mammary cancer
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66
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2006
Mus musculus
brenda
Cooke, G.S.; Campbell, S.J.; Bennett, S.; Lienhardt, C.; McAdam, K.P.; Sow, O.; Gustafson, P.; Mwangulu, F.; van Helden, P.; Fine, P.; Hoal, E.G.; Hill, A.V.
Mapping of a novel susceptibility locus suggests a role for MC3R and CTSZ in human tuberculosis
Am. J. Respir. Crit. Care Med.
178
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2008
Homo sapiens (Q9UBR2), Homo sapiens
brenda
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Visualization of protein interactions inside the secretory pathway
Biochem. Soc. Trans.
35
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2007
Homo sapiens (Q9UBR2)
brenda
Bettegowda, A.; Patel, O.V.; Lee, K.B.; Park, K.E.; Salem, M.; Yao, J.; Ireland, J.J.; Smith, G.W.
Identification of novel bovine cumulus cell molecular markers predictive of oocyte competence: functional and diagnostic implications
Biol. Reprod.
79
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2008
Bos taurus (P05689)
brenda
Kao, C.M.; Huang, F.L.
Cloning and expression of carp cathepsin Z: Possible involvement in yolk metabolism
Comp. Biochem. Physiol. B
149
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2008
Cyprinus carpio (Q58HG7), Cyprinus carpio
brenda
Wendt, W.; Zhu, X.R.; Luebbert, H.; Stichel, C.C.
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204
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2007
Homo sapiens, Mus musculus
brenda
Obermajer, N.; Repnik, U.; Jevnikar, Z.; Turk, B.; Kreft, M.; Kos, J.
Cysteine protease cathepsin X modulates immune response via activation of beta2 integrins
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124
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2008
Homo sapiens
brenda
Lechner, A.M.; Assfalg-Machleidt, I.; Zahler, S.; Stoeckelhuber, M.; Machleidt, W.; Jochum, M.; Naegler, D.K.
RGD-dependent binding of procathepsin X to integrin alphavbeta3 mediates cell-adhesive properties
J. Biol. Chem.
281
39588-39597
2006
Homo sapiens (Q9UBR2), Homo sapiens
brenda
Nyfeler, B.; Zhang, B.; Ginsburg, D.; Kaufman, R.J.; Hauri, H.P.
Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex
Traffic
7
1473-1481
2006
Homo sapiens (Q9UBR2)
brenda
Ahn, S.J.; Kim, N.Y.; Jeon, S.J.; Sung, J.H.; Je, J.E.; Seo, J.S.; Kim, M.S.; Kim, J.K.; Chung, J.K.; Lee, H.H.
Molecular cloning, tissue distribution and enzymatic characterization of cathepsin X from olive flounder (Paralichthys olivaceus)
Comp. Biochem. Physiol. B
151
203-212
2008
Paralichthys olivaceus (Q58HF4), Paralichthys olivaceus
brenda
Krueger, S.; Kuester, D.; Bernhardt, A.; Wex, T.; Roessner, A.
Regulation of cathepsin X overexpression in H. pylori-infected gastric epithelial cells and macrophages
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217
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Homo sapiens
brenda
Leichsenring, A.; Baecker, I.; Wendt, W.; Andriske, M.; Schmitz, B.; Stichel, C.C.; Luebbert, H.
Differential expression of cathepsin S and X in the spinal cord of a rat neuropathic pain model
BMC Neurosci.
9
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2008
Rattus norvegicus
brenda
Kos, J.; Jevnikar, Z.; Obermajer, N.
The role of cathepsin X in cell signaling
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3
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2009
Homo sapiens (Q9UBR2), Homo sapiens
brenda
Obermajer, N.; Jevnikar, Z.; Doljak, B.; Sadaghiani, A.M.; Bogyo, M.; Kos, J.
Cathepsin X-mediated beta2 integrin activation results in nanotube outgrowth
Cell. Mol. Life Sci.
66
1126-1134
2009
Homo sapiens (Q9UBR2)
brenda
Obermajer, N.; Magister, S.; Kopitar, A.N.; Tepes, B.; Ihan, A.; Kos, J.
Cathepsin X prevents an effective immune response against Helicobacter pylori infection
Eur. J. Cell Biol.
88
461-471
2009
Homo sapiens (Q9UBR2)
brenda
Jevnikar, Z.; Obermajer, N.; Pecar-Fonovi?, U.; Karaoglanovic-Carmona, A.; Kos, J.
Cathepsin X cleaves the beta2 cytoplasmic tail of LFA-1 inducing the intermediate affinity form of LFA-1 and alpha-actinin-1 binding
Eur. J. Immunol.
39
3217-3227
2009
Homo sapiens
brenda
Staudt, N.D.; Aicher, W.K.; Kalbacher, H.; Stevanovic, S.; Carmona, A.K.; Bogyo, M.; Klein, G.
Cathepsin X is secreted by human osteoblasts, digests CXCL-12 and impairs adhesion of hematopoietic stem and progenitor cells to osteoblasts
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95
1452-1460
2010
Homo sapiens (Q9UBR2), Homo sapiens
brenda
Naegler, D.K.; Kraus, S.; Feierler, J.; Mentele, R.; Lottspeich, F.; Jochum, M.; Faussner, A.
A cysteine-type carboxypeptidase, cathepsin X, generates peptide receptor agonists
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10
134-139
2010
Homo sapiens
brenda
Obermajer, N.; Doljak, B.; Jamnik, P.; Fonovic, U.P.; Kos, J.
Cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase and impairs survival and neuritogenesis of neuronal cells
Int. J. Biochem. Cell Biol.
41
1685-1696
2009
Homo sapiens
brenda
Sevenich, L.; Schurigt, U.; Sachse, K.; Gajda, M.; Werner, F.; Mueller, S.; Vasiljeva, O.; Schwinde, A.; Klemm, N.; Deussing, J.; Peters, C.; Reinheckel, T.
Synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice
Proc. Natl. Acad. Sci. USA
107
2497-2502
2010
Mus musculus
brenda
Bak, H.J.; Kim, M.S.; Kim, N.Y.; Go, H.J.; Han, J.W.; In Jo, H.; Ahn, S.J.; Park, N.G.; Chung, J.K.; Lee, H.H.
Molecular cloning, expression, and enzymatic analysis of cathepsin X from starfish (Asterina pectinifera)
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169
847-861
2013
Patiria pectinifera (G1JRK2)
brenda
Chantree, P.; Wanichanon, C.; Phatsara, M.; Meemon, K.; Sobhon, P.
Characterization and expression of cathepsin B2 in Fasciola gigantica
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2012
Fasciola gigantica
brenda
Bhutani, N.; Piccirillo, R.; Hourez, R.; Venkatraman, P.; Goldberg, A.L.
Cathepsins L and Z are critical in degrading polyglutamine-containing proteins within lysosomes
J. Biol. Chem.
287
17471-17482
2012
Mus musculus
brenda
Pislar, A.H.; Zidar, N.; Kikelj, D.; Kos, J.
Cathepsin X promotes 6-hydroxydopamine-induced apoptosis of PC12 and SH-SY5Y cells
Neuropharmacology
82
121-131
2014
Rattus norvegicus
brenda
Zhao, C.F.; Herrington, D.M.
The function of cathepsins B, D, and X in atherosclerosis
Am. J. Cardiovasc. Dis.
6
163-170
2016
Homo sapiens (Q9UBR2)
brenda
Mitrovic, A.; Pecar Fonovic, U.; Kos, J.
Cysteine cathepsins B and X promote epithelial-mesenchymal transition of tumor cells
Eur. J. Cell Biol.
96
622-631
2017
Homo sapiens (Q9UBR2)
brenda
Pislar, A.; Bozic, B.; Zidar, N.; Kos, J.
Inhibition of cathepsin X reduces the strength of microglial-mediated neuroinflammation
Neuropharmacology
114
88-100
2017
Mus musculus (Q9WUU7)
brenda
Pecar Fonovic, U.; Kos, J.
Cathepsin X cleaves profilin 1 C-terminal Tyr139 and influences clathrin-mediated endocytosis
PLoS ONE
10
e0137217
2015
Homo sapiens (Q9UBR2)
brenda