3.4.22.15: cathepsin L
This is an abbreviated version!
For detailed information about cathepsin L, go to the full flat file.
Word Map on EC 3.4.22.15
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3.4.22.15
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cathepsins
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lysosomal
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proteinases
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cystatins
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papain
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metastasis
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peptidase
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fasciola
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hepatica
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fluorogenic
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collagenolytic
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pepstatin
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trematode
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tmprss2
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metacercariae
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stefins
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medicine
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endosomal
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procathepsin
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kininogens
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endolysins
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pharmacology
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papain-like
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fluke
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b-like
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covid-19
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trypanosoma
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mers-cov
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leupeptin
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calpains
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proregions
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excysted
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azocasein
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prodomains
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osteoclast
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coronavirus
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fasciolosis
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collagen
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cruzain
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drug development
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excretory-secretory
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ace2
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heparanase
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legumain
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endopeptidases
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sars-cov-2
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elastinolytic
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propeptide
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gigantica
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diagnostics
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proenzyme
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helminth
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microplus
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surimi
- 3.4.22.15
- cathepsins
- lysosomal
- proteinases
- cystatins
- papain
- metastasis
- peptidase
- fasciola
- hepatica
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fluorogenic
-
collagenolytic
- pepstatin
-
trematode
- tmprss2
-
metacercariae
-
stefins
- medicine
- endosomal
-
procathepsin
- kininogens
- endolysins
- pharmacology
-
papain-like
- fluke
-
b-like
- covid-19
- trypanosoma
- mers-cov
- leupeptin
- calpains
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proregions
-
excysted
- azocasein
- prodomains
- osteoclast
- coronavirus
-
fasciolosis
- collagen
- cruzain
- drug development
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excretory-secretory
- ace2
- heparanase
- legumain
- endopeptidases
- sars-cov-2
-
elastinolytic
- propeptide
- gigantica
- diagnostics
- proenzyme
-
helminth
- microplus
-
surimi
Reaction
similar to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity =
Synonyms
AgCatL, Aldrichina grahami cysteine proteinase, cat L, Cat L-A, Cath L, cath-L, cathepsin L, cathepsin L isoform CRA-b, cathepsin L-A, cathepsin L-A1, cathepsin L-A2, cathepsin L-A3, cathepsin L-B, cathepsin L-like, cathepsin L-like cysteine protease, cathepsin L-like enzyme, cathepsin L-like protease, cathepsin L-like protein, cathepsin L-like proteinase, cathepsin L-like rCPB2.8, cathepsin L1, cathepsin L1H, cathepsin L3, cathepsin-L, cathepsin-L T2V, CathL, CatL, CATL A IV, CATL-1, CATL-2, CatL1G, CatL1H, CatL5, CL1, CL3, CL41.5, CPL, cpl-1, CsCPL, CsCPL-m, CtL, CTSL, CTSL1, CTSL2, Cwp84, FhCL1, FhCL3, Har-CatL, human cathepsin L, major excreted protein, MEP, PDP, progesterone-dependent protein, rhodesain, SMCL1, SoCatL, sperm-histone protease, TsolCL
ECTree
3.4.22.15 cathepsin LAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.22.15 - cathepsin L
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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
actomyosin + H2O
?
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endogenous cathepsin L of red bulleye surimi participates in gel disintegration during kamaboko processing by degrading the myosin heavy chain of actomyosin and consequently hindering the gelation of red bulleye surimi
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-
?
Disrupted in renal carcinoma 2 + H2O
?
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the substrate is proteolytically processed into a N-glycosylated N-terminal and a non-glycosylated C-terminal fragment, respectively. The cleavage site is between amino acid residues 214 and 261
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
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recombinant endorepellin is an in vitro substrate. Inhibition of cathepsin L activity in endothelial cells exposed to pro-apoptotic stimuli prevents release of anti-apoptotic C-terminal fragment of endorepellin without modulating the development of apoptosis. Inhibition of caspase-3 activation in endothelial cells concomitantly prevents cathepsin L release, production of anti-apoptotic C-terminal fragment of endorepellin, and the development of paracrine anti-apoptotic activity
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-
?
interleukin-8 precursor + H2O
?
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enzyme plays an important role in IL-8 processing in inflammatory sites
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?
Nipah virus fusion protein + H2O
?
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proteolytically processed within endosomes by cathepsin L
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-
?
pro-dipeptidyl peptidase I
?
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cathepsin L could be an important activator of dipeptidyl peptidase I in vivo
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?
secretory leukocyte protease inhibitor + H2O
?
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incubation of recombinant secretory leukocyte protease inhibitor with cathepsin L leads to complete loss of activity while encapsulation of recombinant secretory leukocyte protease inhibitor in 1,2-dioleoyl-sn-glycero-3-[phospho-L-serine]-cholesterol liposomes retains 92.6% of its activity after challenge with cathepsin L
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-
?
trypsinogen + H2O
trypsin + ?
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cathepsin L inactivates human trypsinogen, CTSL-induced cleavage of trypsinogen occurs 3 amino acids toward the C-terminus from the cathepsin B activation site and results in a truncated, inactive form of trypsin and an elongated propeptide (trypsinogen activation peptide)
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-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
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-
-
?
Zaire Ebola virus glycoprotein + H2O
?
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three cleavage fragments with masses of 23000, 19000, and 4000 Da. Cleavage removes a glycosylated glycan cap and mucin-like domain (MUC domain) and exposes the conserved core residues implicated in receptor binding
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?
Gelatin + H2O
?
on gelatin-zymography, the purified pro-mature enzyme of cathepsin L is capable of hydrolyzing 0.1% gelatin at pH 7.5
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-
?
histone H3 + H2O
?
-
during embryonic stem cell differentiation, histone H3 is proteolytically cleaved at its N-terminus. H3 cleavage may be regulated by covalent modifications present on the histone tail itself
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-
?
perforin + H2O
?
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CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
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-
?
perforin + H2O
?
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CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
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-
?
proheparanase + H2O
active form of heparanase + ?
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removal of the linker peptide and conversion of proheparanase into its active 8 + 50-kDa form is brought about predominantly by cathepsin L. Excision of a 10-amino acid peptide located at the C terminus of the linker segment between two functional cathepsin L cleavage sites at Y156Q and Y146Q is critical for activation of proheparanase. The entire linker segment of proheparanase is susceptible to multiple endocleavages by cathepsin L, generating small peptides. Processing and activation of proheparanase can be brought about solely by cathepsin L
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-
?
proheparanase + H2O
active form of heparanase + ?
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removal of the linker peptide and conversion of proheparanase into its active 850-kDa form is brought about predominantly by cathepsin L. Excision of a 10-amino acid peptide located at the C terminus of the linker segment between two functional cathepsin L cleavage sites at Y156Q and Y146Q is critical for activation of proheparanase. The entire linker segment of proheparanase is susceptible to multiple endocleavages by cathepsin L, generating small peptides. Processing and activation of proheparanase can be brought about solely by cathepsin L
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-
?
type 1 collagen + H2O
?
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isoform Catl1G completely digests collagen type 1
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-
?
type 1 collagen + H2O
?
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efficient cleavage of type 1 collagen by isoform CatL5 is limited to the beta-and gamma-chains
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-
?
additional information
?
-
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enzyme may involve in invasion of cercaria into fish and development to metacercaria, excystment of metacercaria, and protein digestion of adult
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-
?
additional information
?
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enzyme activity plays a pivotal role in prolactin-induced spermatogonial apoptosis
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?
additional information
?
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isoform CatL1G can cleave substrates with proline residues at P2, isoform CatL1G is unable to digest albumin or hemoglobin, efficiently at either pH 5.5 or 7.0
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-
?
additional information
?
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isoform CatL1G can cleave substrates with proline residues at P2
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-
?
additional information
?
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the enzyme is involved in tissue destruction in arthritis
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-
?
additional information
?
-
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the enzyme plays a crucial role in the degradation of the invariant chain during maturation of major histocompatibility complex class II molecules and antigen processing
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-
?
additional information
?
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differentiation of human macrophages within the lung is accompanied by synthesis and expression of cathepsin L
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-
?
additional information
?
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CAT L plays a significant role in numerous important physiological and pathological processes, such as bone resorption, cancer progression and atherosclerosis
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-
?
additional information
?
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cathepsin L has a pro-survival function within the cell which may be due, at least in part, to its ability to deplete the cells from the proapoptotic molecule caspase-3. The existence of a proteolytic hierarchy between pro-survival and pro-death proteases suggests that changes in cellular proteolytic profiles are likely to have significant consequences not only on its survival but also on the type of death it may undergo in response to a specific stress
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-
?
additional information
?
-
catL is essential for epidermal homeostasis and regular hair follicle morphogenesis and cycling
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-
?
additional information
?
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contributions of cathepsin L and cathepsin B to autophagic protein degradation of cytoplasmic proteins in HeLa and Huh-7 cells are nearly equal. Cathepsin L does not play a general role in the degradation of proteins in the lumen of autophagosomes, but rather is involved specifically in the degradation of autophagosomal membrane markers
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-
?
additional information
?
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pituitary gland may utilize the cathepsin L and prohormone convertase pathways for producing propiomelanocortin-derived peptide hormones
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-
?
additional information
?
-
-
p4165aa, a 65 amino acid segment of the p41 splice variant of major histocompatibility complex class II-associated invariant chain, stabilizes cathepsin L in the extracellular environment and induces a local decrease in the concentration of matrix-degrading enzymes during inflammation. Through its interaction with cathepsin L, complex class II-associated invariant chain Ii may control the migratory response of antigen-presenting cells and/or the recruitment of effectors of the inflammatory response
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?
additional information
?
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upon interferon-gamma activation of peritoneal macrophages, enzymatic activityof cathepsin L is specifically inhibited, such that cathepsin S mediates Ii degradation and regulates MHC class II maturation
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?
additional information
?
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cathepsin L elevates alpha-secretase activity, thereby suppressing amyloid precursor protein Abeta42 level. Cathepsin L reduces the formation of Abeta42 peptides by cleaving amyloid precursor protein within the Abeta peptide sequence. In addition, both cathepsins B and L degrade Abeta42 into less toxic Abeta peptides
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-
?
additional information
?
-
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cathepsin L expression levels regulate cell responsiveness to IGF-type I, function for cathepsin L in the control of the tumorigenic/metastatic phenotype
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-
?
additional information
?
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cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
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-
?
additional information
?
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cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
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-
?
additional information
?
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involved in extracellular food digestion
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-
?
additional information
?
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the enzyme plays a most important role in intralysosomal proteolysis in hepatocytes
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-
?
additional information
?
-
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plays a crucial role in the pathogenesis of adjuvant arthritis
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-
?
additional information
?
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the enzyme is suggested to play a crucial role in the degradation of the basement membranes
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?
additional information
?
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enzyme has a role in the progress of the cell cycle during the cleavage divisions of embryonic development. Inhibition of the protease abolishes the chromatin decondensation after mitosis
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-
?
additional information
?
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granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
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-
?
additional information
?
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granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
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?
