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Information on EC 3.4.18.1 - cathepsin X
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3.4.18.1 cathepsin XSpecify your search results
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- 3.4.18.1
- cathepsins
-
papain-like
-
procathepsins
- saitoi
- diagnostics
-
galactosialidosis
- medicine
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid carboxypeptidase
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-
-
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cathepsin B2
cathepsin IV
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cathepsin X
cathepsin Z
CATX
CTSZ
lysosomal carboxypeptidase B
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-
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cathepsin B2
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-
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity
Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity
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Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity
the catalytic triad is formed by Cys84, His233, and Asn254
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY
37217-21-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2,4-dinitrophenyl)-GFRFW + H2O
(2,4-dinitrophenyl)-GFR + L-Phe-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
?
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-
-
-
?
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
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-
?
2-aminobenzoyl-Phe-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
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-
-
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?
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
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-
?
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
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?
2-aminobenzoyl-Phe-Arg-Cys + H2O
2-aminobenzoyl-Phe-Arg + Cys
kcat/Km is 73/mM * s
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?
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
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-
?
2-aminobenzoyl-Phe-Arg-His + H2O
2-aminobenzoyl-Phe-Arg + His
kcat/Km is 5.4/mM * s
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-
?
2-aminobenzoyl-Phe-Arg-Ile + H2O
2-aminobenzoyl-Phe-Arg + Ile
kcat/Km is 3.4/mM * s
-
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?
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
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?
2-aminobenzoyl-Phe-Arg-Met + H2O
2-aminobenzoyl-Phe-Arg + Met
kcat/Km is 9.3/mM * s
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?
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
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?
2-aminobenzoyl-Phe-Arg-Thr + H2O
2-aminobenzoyl-Phe-Arg + Thr
kcat/Km is 5.8/mM * s
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?
2-aminobenzoyl-Phe-Arg-Trp + H2O
2-aminobenzoyl-Phe-Arg + Trp
kcat/Km is 8.6/mM * s
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?
2-aminobenzoyl-Phe-Arg-Tyr + H2O
2-aminobenzoyl-Phe-Arg + Tyr
kcat/Km is 8.8/mM * s
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?
2-aminobenzoyl-Phe-Arg-Val + H2O
2-aminobenzoyl-Phe-Arg + Val
kcat/Km is 5.9/mM * s
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?
2-aminobenzoyl-Phe-Asn-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Asn + 4-nitrophenylalanine
kcat/Km is 13/mM * s
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?
2-aminobenzoyl-Phe-Asp-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Asp + 4-nitrophenylalanine
kcat/Km is 12/mM * s
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?
2-aminobenzoyl-Phe-Cys-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Cys + 4-nitrophenylalanine
kcat/Km is 17/mM * s
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?
2-aminobenzoyl-Phe-Gln-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Gln + 4-nitrophenylalanine
kcat/Km is 73/mM * s
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?
2-aminobenzoyl-Phe-Glu-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Glu + 4-nitrophenylalanine
kcat/Km is 62/mM * s
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?
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
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?
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
-
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?
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
-
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?
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
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-
?
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
-
-
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?
3-aminobenzoyl-RR-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P + H2O
3-aminobenzoyl-RR + (2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P
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-
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?
7-methoxycoumarin-4-ylacetyl-RPPGFSAFK-N-epsilon-2,4-dinitrophenol + H2O
?
fluorescence cathepsin X/A-selective substrate
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?
AKYNQLMRIEEELGEEARFAGHNFRNPSVL + H2O
?
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a model peptide derived from rat gamma-enolase carboxyl terminal, overview
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?
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
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?
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
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-
-
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?
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
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?
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
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?
bradykinin + H2O
?
-
the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
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-
?
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
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i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg, a mainly B2 receptor
an exclusive B1 receptor
-
?
KAKFAGRNPRNPLAK + H2O
?
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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
-
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?
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
-
?
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
?
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-
-
-
?
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
-
-
?
alpha-enolase + H2O
?
-
cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
-
-
?
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
-
-
?
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
?
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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
-
-
?
additional information
?
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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
-
-
?
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
?
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-
procathepsin X supports integrin alphavbeta3-dependent attachment and spreading of umbilical vein endothelial cells, overvie
-
-
?
additional information
?
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-
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
?
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-
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
?
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-
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
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-
?
additional information
?
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direct interaction between the enzyme and integrin alphavbeta3, overview
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-
?
additional information
?
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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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Aprotinin
0.1 mM, proPoCtX: 31.9% inhibition, native PoCtX: 51.3% inhibition
chymostatin
0.1 mM, proPoCtX: 35.4% inhibition, native PoCtX: 96.9% inhibition
E-64
0.1 mM, proPoCtX: 25.6% inhibition, native PoCtX: 98.6% inhibition
E64
treatment of cumulus-oocyte-complexes with E64 enhances subsequent rates of blastocyst development following parthenogenetic activation
leupeptin
0.1 mM, proPoCtX: 99.1% inhibition, native PoCtX: 95.6% inhibition
NEM
0.1 mM, proPoCtX: 44.6% inhibition, native PoCtX: 67.0% inhibition
pepstatin A
0.1 mM, proPoCtX: 0% inhibition, native PoCtX: 36.0% inhibition
PMSF
0.1 mM, proPoCtX: 42.2% inhibition, native PoCtX: 37.2% inhibition
1,10-phenanthroline
0.1 mM, proPoCtX: 51.3% inhibition, native PoCtX: 56.6% inhibition
antipain
0.1 mM, proPoCtX: 98.6% inhibition, native PoCtX: 97.6% inhibition
EDTA
0.1 mM, proPoCtX: 5.1% inhibition, native PoCtX: 14.2% inhibition
EGTA
0.1 mM, proPoCtX: 2.2% inhibition, native PoCtX: 25.6% inhibition
additional information
-
the addition of the specific MEK1/2 inhibitor U0126 reduces Helicobacter pylori-stimulated CTSX expression in U937 monocytes, but not in NCI-N87 cells. In NCIN87 cells, the regulation is controlled by p38 and JNK. Inhibition by SB203580 and SP600125 completely abolish the stimulated CTSX protein expression of NCI-N87 cells in response to Helicobacter pylori infection
-
additional information
inhibition of cathepsin X with either AMS36 or 2F12mAb
-
additional information
-
cathepsin X inhibition by mAb 2F12. Migration of primary T cell is reduced by mAb 2F12 by 0.27fold
-
additional information
recombinant proPoCtX is inhibited by antipain and leupeptin
-
additional information
-
recombinant proPoCtX is inhibited by antipain and leupeptin
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
CagA, upregulation of CTSX is more intense in tissue samples of patients with CagA+ Helicobacter pylori than in those with CagA- Helicobacter pylori
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE