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3.4.18.1: cathepsin X

This is an abbreviated version!
For detailed information about cathepsin X, go to the full flat file.

Word Map on EC 3.4.18.1

Reaction

Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity =

Synonyms

acid carboxypeptidase, cathepsin B2, cathepsin IV, cathepsin P, cathepsin X, cathepsin Z, CATX, CTPZ, CTSX, CTSZ, cysteine-type carboxypeptidase, lysosomal carboxypeptidase B, mopre, PoCtX

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.18 Cysteine-type carboxypeptidases
                3.4.18.1 cathepsin X

Natural Substrates Products

Natural Substrates Products on EC 3.4.18.1 - cathepsin X

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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
-
-
?
Proteins + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-