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Information on EC 3.4.18.1 - cathepsin X and Organism(s) Mus musculus and UniProt Accession Q9WUU7

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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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This record set is specific for:
Mus musculus
UNIPROT: Q9WUU7 not found.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
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-
-
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cathepsin B2
-
-
-
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cathepsin IV
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-
-
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cathepsin P
-
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cathepsin X
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cathepsin Z
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CATX
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CTSZ
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lysosomal carboxypeptidase B
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
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-
CAS REGISTRY NUMBER
COMMENTARY hide
37217-21-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
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-
?
biotinyl-KKQ20KK + H2O
?
show the reaction diagram
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-
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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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
microglial cell
Manually annotated by BRENDA team
microglial cell
Manually annotated by BRENDA team
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healthy, aging, and pathological, expression patterns of cathepsin X, overview
Manually annotated by BRENDA team
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the enzyme is upregulated in glia cells of degenerating brain regions in a transgenic mouse model of amyotrophic lateral sclerosis
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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tumor-associated
Manually annotated by BRENDA team
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very low enzyme content
Manually annotated by BRENDA team
additional information
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tissue distribution, immunohistochemic analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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somal, enzyme in close proximity to the mitochondria, the rough endoplasmic reticulum, and the nuclear membrane
Manually annotated by BRENDA team
additional information
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subcellular localization in aged and pathological brain tissues, overview, no activity in the extracellular space
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
there is a significant release of cathepsin X from activated BV2 and EOC 13.31 cells following a lipopolysaccharide stimulus that coincides with reduced release of the active form of gamma-enolase
physiological function
up-regulated expression and increased release and activity of microglial cathepsin X leads to microglia activation-mediated neurodegeneration
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CATZ_MOUSE
306
0
33996
Swiss-Prot
Secretory Pathway (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
cathepsin X inhibitor causes neuroprotection via its inhibition of the activation of microglia. Cathepsin X can be a potential therapeutic target for neuroinflammatory disorders
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vasiljeva, O.; Papazoglou, A.; Krueger, A.; Brodoefel, H.; Korovin, M.; Deussing, J.; Augustin, N.; Nielsen, B.S.; Almholt, K.; Bogyo, M.; Peters, C.; Reinheckel, T.
Tumor cell-derived and macrophage-derived cathepsin B promotes progression and lung metastasis of mammary cancer
Cancer Res.
66
5242-5250
2006
Mus musculus
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
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team