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Information on EC 3.4.18.1 - cathepsin X and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.18 Cysteine-type carboxypeptidases
                3.4.18.1 cathepsin X
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acid carboxypeptidase
-
-
-
-
cathepsin B2
-
-
-
-
cathepsin IV
-
-
-
-
cathepsin X
cathepsin Z
CATX
-
-
CTSX
-
-
cysteine-type carboxypeptidase
-
-
lysosomal carboxypeptidase B
-
-
-
-
mopre
cathepsin X belongs to the CA clan of cysteine peptidases
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
37217-21-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2,4-dinitrophenyl)-GFFGW + H2O
(2,4-dinitrophenyl)-GFFG + L-Trp
show the reaction diagram
-
-
-
?
(2,4-dinitrophenyl)-GFFRW + H2O
(2,4-dinitrophenyl)-GFFR + L-Trp
show the reaction diagram
-
-
-
?
(2,4-dinitrophenyl)-GFFW + H2O
(2,4-dinitrophenyl)-GFF + L-Trp
show the reaction diagram
-
-
-
?
(2,4-dinitrophenyl)-GFRFW + H2O
(2,4-dinitrophenyl)-GFR + L-Phe-L-Trp
show the reaction diagram
-
-
-
?
(2,4-dinitrophenyl)-GFRW + H2O
(2,4-dinitrophenyl)-GFR + L-Trp
show the reaction diagram
-
-
-
?
(2,4-dinitrophenyl)-GRFFW + H2O
(2,4-dinitrophenyl)-GRFF + L-Trp
show the reaction diagram
-
-
-
?
(2-aminobenzoyl)-FFF + H2O
(2-aminobenzoyl)-FF + L-Phe
show the reaction diagram
-
-
-
?
(2-aminobenzoyl)-FFFA + H2O
(2-aminobenzoyl)-FFF + L-Ala
show the reaction diagram
-
-
-
?
(2-aminobenzoyl)-FFFP + H2O
(2-aminobenzoyl)-FFF + Pro
show the reaction diagram
-
-
-
?
(2-aminobenzoyl)-FFFR + H2O
(2-aminobenzoyl)-FFF + L-Arg
show the reaction diagram
-
-
-
?
(2-aminobenzoyl)-FFFR-NH2 + H2O
(2-aminobenzoyl)-FFF + Arg-amide
show the reaction diagram
-
-
-
?
(2-aminobenzoyl)-FFFW + H2O
(2-aminobenzoyl)-FFF + L-Trp
show the reaction diagram
-
-
-
?
(2-aminobenzoyl)-FFGW + H2O
(2-aminobenzoyl)-FFG + L-Trp
show the reaction diagram
-
-
-
?
(2-aminobenzoyl)-FFRW + H2O
(2-aminobenzoyl)-FFR + L-Trp
show the reaction diagram
-
-
-
?
(2-aminobenzoyl)-FFRW-NH2 + H2O
(2-aminobenzoyl)-FFR + L-Trp-amide
show the reaction diagram
-
-
-
?
(2-aminobenzoyl)-FRFW-NH2 + H2O
(2-aminobenzoyl)-FR + Phe-Trp-amide
show the reaction diagram
-
-
-
?
2-aminobenzoyl-Ala-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Ala-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 20/mM * s
-
-
?
2-aminobenzoyl-Arg-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Arg-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Arg-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 5.2/mM * s
-
-
?
2-aminobenzoyl-Asn-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Asn-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 17/mM * s
-
-
?
2-aminobenzoyl-Asp-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Asp-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 16/mM * s
-
-
?
2-aminobenzoyl-Cys-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Cys-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 11/mM * s
-
-
?
2-aminobenzoyl-Gln-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Gln-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 43/mM * s
-
-
?
2-aminobenzoyl-Glu-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Glu-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 27/mM * s
-
-
?
2-aminobenzoyl-Gly-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Gly-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 4.4/mM * s
-
-
?
2-aminobenzoyl-His-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-His-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 4.7/mM * s
-
-
?
2-aminobenzoyl-Ile-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Ile-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 2.7/mM * s
-
-
?
2-aminobenzoyl-Leu-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Leu-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Leu-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 153/mM * s
-
-
?
2-aminobenzoyl-Lys-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Lys-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 5.7/mM * s
-
-
?
2-aminobenzoyl-Met-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Met-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 28/mM * s
-
-
?
2-aminobenzoyl-Phe-Ala-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Ala + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 51/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Phe-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 100/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Ala + H2O
2-aminobenzoyl-Phe-Arg + Ala
show the reaction diagram
kcat/Km is 10/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Arg + H2O
2-aminobenzoyl-Phe-Arg + Arg
show the reaction diagram
kcat/Km is 1.7/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Asn + H2O
2-aminobenzoyl-Phe-Arg + Asn
show the reaction diagram
kcat/Km is 5.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Asp + H2O
2-aminobenzoyl-Phe-Arg + Asp
show the reaction diagram
kcat/Km is 8.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Cys + H2O
2-aminobenzoyl-Phe-Arg + Cys
show the reaction diagram
kcat/Km is 73/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Gln + H2O
2-aminobenzoyl-Phe-Arg + Gln
show the reaction diagram
kcat/Km is 4.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Glu + H2O
2-aminobenzoyl-Phe-Arg + Glu
show the reaction diagram
kcat/Km is 7.7/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Gly + H2O
2-aminobenzoyl-Phe-Arg + Gly
show the reaction diagram
kcat/Km is 14/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-His + H2O
2-aminobenzoyl-Phe-Arg + His
show the reaction diagram
kcat/Km is 5.4/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Ile + H2O
2-aminobenzoyl-Phe-Arg + Ile
show the reaction diagram
kcat/Km is 3.4/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Leu + H2O
2-aminobenzoyl-Phe-Arg + Leu
show the reaction diagram
kcat/Km is 7.1/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Lys + H2O
2-aminobenzoyl-Phe-Arg + Lys
show the reaction diagram
kcat/Km is 5.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Met + H2O
2-aminobenzoyl-Phe-Arg + Met
show the reaction diagram
kcat/Km is 9.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Phe + H2O
2-aminobenzoyl-Phe-Arg + Phe
show the reaction diagram
kcat/Km is 15/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Ser + H2O
2-aminobenzoyl-Phe-Arg + Ser
show the reaction diagram
kcat/Km is 48/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Thr + H2O
2-aminobenzoyl-Phe-Arg + Thr
show the reaction diagram
kcat/Km is 5.8/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Trp + H2O
2-aminobenzoyl-Phe-Arg + Trp
show the reaction diagram
kcat/Km is 8.6/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Tyr + H2O
2-aminobenzoyl-Phe-Arg + Tyr
show the reaction diagram
kcat/Km is 8.8/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Val + H2O
2-aminobenzoyl-Phe-Arg + Val
show the reaction diagram
kcat/Km is 5.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Asn-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Asn + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 13/mM * s
-
-
?
2-aminobenzoyl-Phe-Asp-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Asp + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 12/mM * s
-
-
?
2-aminobenzoyl-Phe-Cys-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Cys + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 17/mM * s
-
-
?
2-aminobenzoyl-Phe-Gln-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Gln + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 73/mM * s
-
-
?
2-aminobenzoyl-Phe-Glu-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Glu + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 62/mM * s
-
-
?
2-aminobenzoyl-Phe-Gly-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Gly + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 45/mM * s
-
-
?
2-aminobenzoyl-Phe-His-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-His + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 3.5/mM * s
-
-
?
2-aminobenzoyl-Phe-Ile-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Ile + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 4.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Leu-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Leu + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 2.0/mM * s
-
-
?
2-aminobenzoyl-Phe-Lys-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Lys + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 79/mM * s
-
-
?
2-aminobenzoyl-Phe-Met-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Met + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 181/mM * s
-
-
?
2-aminobenzoyl-Phe-Phe-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Phe + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 108/mM * s
-
-
?
2-aminobenzoyl-Phe-Ser-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Ser + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 32/mM * s
-
-
?
2-aminobenzoyl-Phe-Thr-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Thr + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 68/mM * s
-
-
?
2-aminobenzoyl-Phe-Trp-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Trp + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 1.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Tyr-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Tyr + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 58/mM * s
-
-
?
2-aminobenzoyl-Phe-Val-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Val + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 4.8/mM * s
-
-
?
2-aminobenzoyl-Pro-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Pro-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 0.2/mM * s
-
-
?
2-aminobenzoyl-Ser-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Ser-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 8.2/mM * s
-
-
?
2-aminobenzoyl-Thr-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Thr-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 8.7/mM * s
-
-
?
2-aminobenzoyl-Trp-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Trp-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 12/mM * s
-
-
?
2-aminobenzoyl-Tyr-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Tyr-Arg + 4-nitrophenylalanine
show the reaction diagram
kcat/Km is 400/mM * s
-
-
?
2-aminobenzoyl-Val-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Val-Arg + 4-nitrophenylalanine
show the reaction diagram
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
show the reaction diagram
-
-
-
?
3-aminobenzoyl-LR-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P + H2O
3-aminobenzoyl-LR + (2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P
show the reaction diagram
-
-
-
?
3-aminobenzoyl-RR-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P + H2O
3-aminobenzoyl-RR + (2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P
show the reaction diagram
-
-
-
?
7-methoxycoumarin-4-ylacetyl-RPPGFSAFK-N-epsilon-2,4-dinitrophenol + H2O
?
show the reaction diagram
fluorescence cathepsin X/A-selective substrate
-
-
?
Abz-Phe-Glu-Lys(Dnp)-OH + H2O
?
show the reaction diagram
-
-
-
-
?
AKYNQLMRIEEELGEEARFAGHNFRNPSVL + H2O
?
show the reaction diagram
-
a model peptide derived from rat gamma-enolase carboxyl terminal, overview
-
-
?
alpha-enolase + H2O
?
show the reaction diagram
benzyloxycarbonyl-FR-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-FR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-RR-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-RR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
bradykinin + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg, a mainly B2 receptor
an exclusive B1 receptor
-
?
CXCL-12 + H2O
?
show the reaction diagram
gamma-enolase + H2O
?
show the reaction diagram
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-L-glutamic acid + H2O
hippuric acid + L-Glu
show the reaction diagram
-
-
-
-
?
KAKFAGRNPRNPLAK + H2O
?
show the reaction diagram
-
a model peptide derived from human alpha-enolase carboxyl terminal, overview
-
-
?
kallidin + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
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
?
show the reaction diagram
ortho-aminobenzoyl-Arg-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
ortho-aminobenzoyl-Lys-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
ortho-aminobenzoyl-Phe-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
profilin + H2O
L-tyrosine + ?
show the reaction diagram
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
?
show the reaction diagram
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
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-enolase + H2O
?
show the reaction diagram
-
cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
-
-
?
bradykinin + H2O
?
show the reaction diagram
-
the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
-
-
?
CXCL-12 + H2O
?
show the reaction diagram
CXCL-12 is a physiological substrate for secreted cathepsin X
-
-
?
gamma-enolase + H2O
?
show the reaction diagram
-
cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
-
-
?
kallidin + H2O
?
show the reaction diagram
-
the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
-
-
?
lymphocyte function associated antigen-1 + H2O
?
show the reaction diagram
-
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 + ?
show the reaction diagram
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
?
show the reaction diagram
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
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMS36
irreversible inhibitor
CA-074
-
-
chicken cystatin
-
-
-
cystatin C
-
-
-
GFG-semicarbazone
-
-
Stefin A
-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018
(2,4-dinitrophenyl)-GFFGW
-
pH 5.1, 37°C
0.0036
(2,4-dinitrophenyl)-GFFRW
-
pH 5.1, 37°C
0.001
(2,4-dinitrophenyl)-GFFW
-
pH 5.1, 37°C
0.0024
(2,4-dinitrophenyl)-GFRFW
-
pH 5.1, 37°C
0.0042
(2,4-dinitrophenyl)-GFRW
-
pH 5.1, 37°C
0.0046
(2,4-dinitrophenyl)-GRFFW
-
pH 5.1, 37°C
0.063
CBZ-FR-7-amido-4-methylcoumarin
-
pH 5.1, 37°C
0.13
CBZ-RR-7-amido-4-methylcoumarin
-
pH 5.1, 37°C
0.69
hippuryl-L-Arg
-
D253R mutant
0.0083
ortho-aminobenzoyl-Arg-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro +
-
pH 5.1, 37°C
-
0.0105
ortho-aminobenzoyl-Lys-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro
-
pH 5.1, 37°C
-
0.0037
ortho-aminobenzoyl-Phe-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro
-
pH 5.1, 37°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
(2,4-dinitrophenyl)-GFFGW
-
pH 5.1, 37°C
0.3
(2,4-dinitrophenyl)-GFFRW
-
pH 5.1, 37°C
0.07
(2,4-dinitrophenyl)-GFFW
-
pH 5.1, 37°C
0.03
(2,4-dinitrophenyl)-GFRFW
-
pH 5.1, 37°C
0.7
(2,4-dinitrophenyl)-GFRW
-
pH 5.1, 37°C
0.23
(2,4-dinitrophenyl)-GRFFW
-
pH 5.1, 37°C
0.06
2-aminobenzoyl-Arg-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro +
-
pH 5.1, 37°C
-
0.02
2-aminobenzoyl-Leu-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro +
-
pH 5.1, 37°C
-
0.07
2-aminobenzoyl-Phe-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro +
-
pH 5.1, 37°C
-
0.22
benzyloxycarbony-FR-4-methylcoumaryl-7-amide
-
pH 5.1, 37°C
0.63 - 6.08
benzyloxycarbony-RR-4-methylcoumaryl-7-amide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.17
bradykinin
-
pH 5.5
5.75
kallidin
-
pH 5.5
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000015
chicken cystatin
-
pH 5.5, 25°C
-
0.000012
cystatin C
-
pH 5.5, 25°C
-
0.0166
GFG-semicarbazone
-
pH 5.5, 25°C
0.0000017
Stefin A
-
pH 5.5, 25°C
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
assay at
5
-
reaction with 3-aminobenzoyl-FR-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P
5 - 5.5
-
reaction with benzyloxycarbonyl-RR-4-methylcoumaryl-7-amide
5 - 6
-
reaction with (2,4-dinitrophenyl)-GFFW
5.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 5.5
-
pH 3.5: about 50% of maximal activity, pH 5.5: about 50% of maximal activity, reaction with 3-aminobenzoyl-FR-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P
4 - 6.5
-
pH 4.0: about 45% of maximal activity, reaction with benzyloxycarbonyl-RR-methylcoumarinamide
4.5 - 6.5
-
pH 4.5: about 45% of maximal activity, pH 6.5: about 10% of maximal activity, reaction with (2,4-dinitrophenyl)-GFFW
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
cathepsin X can be secreted by nonhematopoietic bone marrow cells in an activated form
Manually annotated by BRENDA team
-
the enzyme is associated with plaques in Alzheimer patients, overview
Manually annotated by BRENDA team
an osteoblastic cell line
Manually annotated by BRENDA team
-
of healthy individuals and Alzheimer patients
Manually annotated by BRENDA team
-
upregulation in gastric cancer compared to non-neoplastic mucosa. Patients with Helicobacter pylori gastritis show significantly higher cathepsin X mRNA (2.5fold) and protein (1.6fold) expression than Helicobacter pylori-negative partients
Manually annotated by BRENDA team
a bone marrow stromal cell line
Manually annotated by BRENDA team
a bone marrow stromal cell line
Manually annotated by BRENDA team
-
protein level of cathespin X does not differ significantly between matched pairs of lung tumor and adjacent lung tissue ontained from patients with lung cancer
Manually annotated by BRENDA team
-
protein level of cathespin X does not differ significantly between matched pairs of lung tumor and adjacent lung tissue ontained from patients with lung cancer
Manually annotated by BRENDA team
-
human gastric epithelial cell
Manually annotated by BRENDA team
the enzyme accumulates in vesicles at lamellipodia
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
cathepsin X is localized on the cell surface of primary osteoblasts
Manually annotated by BRENDA team
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, overview
Manually annotated by BRENDA team
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, overview
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CATZ_HUMAN
303
1
33868
Swiss-Prot
Secretory Pathway (Reliability: 4)
A0A7P0T8I6_HUMAN
334
1
37088
TrEMBL
Secretory Pathway (Reliability: 4)
Q5U000_HUMAN
303
1
33868
TrEMBL
Secretory Pathway (Reliability: 4)
A0A7P0T989_HUMAN
289
0
32003
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour diffusion, structure determined at 2.67 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D253K
-
reversed polarity and improved activity
D253R
-
reversed polarity and improved activity
G251T/D253K
-
double mutant, improved activity
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Pichia pastoris by cation exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cathepsin X stable expression in Jurkat T cells
-
DNA and amino acid sequence determination and anaylsis, expression of wild-type and mutant procathepsin X
expression of procathepsin X in Pichia pastoris as an alpha-factor fusion
-
expression of recombinants in Escherichia coli
-
expression of the proenzyme in Pichia pastoris
-
genotype distributions of CTSZ and CTSZ3P in South African coloured population in metropolitan Cape Town, South Africa, genotyping, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Helicobacter pylori antigens from subjects with gastritis, who are successful in eradicating the infection after antibiotic therapy, decrease the membrane expression of cathepsin X in THP-1 cells
Helicobacter pylori antigens from subjects with gastritis, who are unsuccessful in eradicating the infection after antibiotic therapy, increase the membrane expression of cathepsin X in THP-1 cells
the enzyme is upregulated in several types of cancer
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Edge, M.; Forder, C.; Hennam, J.; Lee, I.; Tonge, D.; Hardern, I.; Fitton, J.; Eckersley, K.; East, S.; Shufflebotham, A.; Blakey, D.; Slater, A.
Engineered human carboxypeptidase B enzymes that hydrolyse hippuryl-L-glutamic acid: reversed-polarity mutants
Protein Eng.
11
1229-1234
1998
Homo sapiens
Manually annotated by BRENDA team
Klemencic, I.; Carmona, A.K.; Cezari, M.H.; Juliano, M.A.; Juliano, L.; Guncar, G.; Turk, D.; Krizaj, I.; Turk, V.; Turk, B.
Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase
Eur. J. Biochem.
267
5404-5412
2000
Homo sapiens
Manually annotated by BRENDA team
Guncar, G.; Klemencic, I.; Turk, B.; Turk, V.; Karaoglanovic-Carmona, A.; Juliano, L.; Turk, D.
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
305-313
2000
Homo sapiens
Manually annotated by BRENDA team
Devanathan, G.; Turnbull, J.L.; Ziomek, E.; Purisima, E.O.; Menard, R.; Sulea, T.
Carboxy-monopeptidase substrate specificity of human cathepsin X
Biochem. Biophys. Res. Commun.
329
445-452
2005
Homo sapiens (Q9UBR2), Homo sapiens
Manually annotated by BRENDA team
Kos, J.; Sekirnik, A.; Premzl, A.; Zavasnik Bergant, V.; Langerholc, T.; Turk, B.; Werle, B.; Golouh, R.; Repnik, U.; Jeras, M.; Turk, V.
Carboxypeptidases cathepsins X and B display distinct protein profile in human cells and tissues
Exp. Cell Res.
306
103-113
2005
Homo sapiens
Manually annotated by BRENDA team
Obermajer, N.; Premzl, A.; Zavasnik Bergant, T.; Turk, B.; Kos, J.
Carboxypeptidase cathepsin X mediates beta(2)-integrin-dependent adhesion of differentiated U-937 cells
Exp. Cell Res.
312
2515-2527
2006
Homo sapiens
Manually annotated by BRENDA team
Ngler, D.K.; Lechner, A.M.; Oettl, A.; Kozaczynska, K.; Scheuber, H.P.; Gippner-Steppert, C.; Bogner, V.; Biberthaler, P.; Jochum, M.
An enzyme-linked immunosorbent assay for human cathepsin X, a potential new inflammatory marker
J. Immunol. Methods
308
241-250
2006
Homo sapiens
Manually annotated by BRENDA team
Krueger, S.; Kalinski, T.; Hundertmark, T.; Wex, T.; Kuster, D.; Peitz, U.; Ebert, M.; Nagler, D.K.; Kellner, U.; Malfertheiner, P.; Naumann, M.; Rocken, C.; Roessner, A.
Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer
J. Pathol.
207
32-42
2005
Homo sapiens
Manually annotated by BRENDA team
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
203-207
2008
Homo sapiens (Q9UBR2), Homo sapiens
Manually annotated by BRENDA team
Nyfeler, B.; Hauri, H.P.
Visualization of protein interactions inside the secretory pathway
Biochem. Soc. Trans.
35
970-973
2007
Homo sapiens (Q9UBR2)
Manually annotated by BRENDA team
Wendt, W.; Zhu, X.R.; Luebbert, H.; Stichel, C.C.
Differential expression of cathepsin X in aging and pathological central nervous system of mice
Exp. Neurol.
204
525-540
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Obermajer, N.; Repnik, U.; Jevnikar, Z.; Turk, B.; Kreft, M.; Kos, J.
Cysteine protease cathepsin X modulates immune response via activation of beta2 integrins
Immunology
124
76-88
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Krueger, S.; Kuester, D.; Bernhardt, A.; Wex, T.; Roessner, A.
Regulation of cathepsin X overexpression in H. pylori-infected gastric epithelial cells and macrophages
J. Pathol.
217
581-588
2009
Homo sapiens
Manually annotated by BRENDA team
Kos, J.; Jevnikar, Z.; Obermajer, N.
The role of cathepsin X in cell signaling
Cell Adh. Migr.
3
164-166
2009
Homo sapiens (Q9UBR2), Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Haematologica
95
1452-1460
2010
Homo sapiens (Q9UBR2), Homo sapiens
Manually annotated by BRENDA team
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
Int. Immunopharmacol.
10
134-139
2010
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team