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Enzyme Nomenclature
Information on EC 3.4.22.15 - cathepsin L
for references in articles please use BRENDA:EC3.4.22.15
Word Map on EC 3.4.22.15
- 3.4.22.15
-
cathepsins
- lysosomal
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proteinases
- papain
-
cystatins
- metastasis
- macrophage
- collagen
- fasciola
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fluorogenic
- endolysins
-
elastinolytic
-
azocasein
-
excretory-secretory
-
papain-like
- hepatica
-
anti-cathepsin
- leupeptin
-
b-like
-
proenzyme
-
calpains
- medicine
-
propeptide
- fluke
-
surimi
-
collagenolytic
- legumain
-
trematode
-
proregions
- osteoclast
- pepstatin
- coronavirus
-
metacercariae
-
excysted
-
fasciolosis
-
procathepsin
- gigantica
- heparanase
-
sars-cov
-
endopeptidases
- trypanosoma
- cruzipain
-
s-layer
-
kininogens
- resorption
-
subsite
-
helminth
- pharmacology
-
prodomains
-
ii-associated
-
stefins
- endosomal
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.4.22.15
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RECOMMENDED NAME
GeneOntology No.
cathepsin L
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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-
endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY
60616-82-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
up-regulation of catfish cathepsin H and L transcripts during the early stage of Edwardsiella ictaluri infection
UniProt
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36622, 647898, 647900, 647902, 647914, 647916, 647919, 647920, 647921, 647926, 647932, 647933, 647938, 647950, 647972, 650415, 650454, 651075, 651159, 651591, 652733, 667194, 667305, 667428, 667863, 668142, 668508, 669158, 669460, 669793, 670358, 677507, 678515, 678521, 678529, 679227, 680861, 680890, 681321, 682070, 682739, 695965, 696091, 696405, 696565, 696623, 696630, 696743, 697621, 697939, 698753, 698768, 698807, 699226, 699442, 699608, 699624, 699913, 700241, 700295, 700324, 700689, 701145, 707591, 707626, 708264, 710701, 710810, 711055, 711056, 711298, 711345, 711349, 711385, 711400, 711708, 711857, 711939, 711945, 712089, 712140, 712412, 712480, 712554, 712729, 712904, 712921, 713010, 713069, 713516, 713582, 713584, 731127, 731440, 731639
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UniProt
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647911, 647913, 652657, 667867, 668138, 668959, 680861, 681531, 681907, 682970, 697238, 698753, 699405, 699757, 700521, 700963, 710807, 711141, 711963, 712140, 713022, 713155, 713190, 713582, 717223, 717285
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
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inhibition of cathepsin L by specific inhibitors results in a significant decrease of intraocular neovascularization, a similar decrease of neovascularization is found in cathepsin L-deficient mice
malfunction
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inhibition of cathepsin L results in a decrease in tumor cell migration
malfunction
-
cathepsin L pharmacological inhibition significantly attenuates lysosomal membrane permeabilization, mitochondrial membrane permeabilization, and apoptosis
malfunction
-
ablation of cathepsin L in a cystatin M/E-deficient background (Cst6-/-Ctsl-/-double-knockout mice) restores viability and results in normalization of stratum corneum morphology
malfunction
-
severity of pancreatitis is reduced in cathepsin L-deficient mice, whereas apoptosis and intrapancreatic trypsin activity are increased
malfunction
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inhibition of cathepsin L can decrease metastatic tumor development
malfunction
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cathepsin L knockout mouse brains show extensive decreases in dynorphin A, dynorphin B, and alpha-neoendorphin that are reduced by 75%, 83%, and 90%, respectively
malfunction
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deficiency for cathepsin L promotes enhanced tumor progression and metastasis in mouse epidermis, Ctsl deficiency potentiates neoplastic progression in K14-HPV16 transgenic mice but does not alter immune cell infiltration or angiogenesis during neoplastic progression in HPV16 mice
malfunction
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in cathepsin L knockout mice, cholecystokinin 8 levels are substantially reduced in brain cortex by an average of 75%
malfunction
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in cathepsin L knockou mice, brain levels of (Met)enkephalin are reduced to 44%, brain levels of neuropeptide Y are reduced to 22%, brain levels of cholecystokinin are reduced to 75%, brain levels of dynorphin A are reduced to 25% , brain levels of dynorphin B are reduced to 17%, brain levels of alpha-neoendorphin are reduced to 10%, brain levels of adrenocorticotropin hormone are reduced to 23%, brain levels of beta-endorphin are reduced to 18%, and brain levels of alpha-MSH are reduced to 7% of the wild type level
physiological function
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cathepsin L plays a critical role in intraocular angiogenesis
physiological function
-
cat L mediates resveratrol-induced apoptotic cell death in cervical cancer cells
physiological function
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cathepsin L does not seem to play a general role in the degradation of proteins in the lumen of autophagosomes, but is involved more specifically in the degradation of autophagosomal membrane markers
physiological function
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cathepsin L is involved in bone remodeling processes and contributes to facilitate bone metastasis formation
physiological function
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cathepsin L plays a minimal, if any, role in Ebola virus infection in human dendritic cells
physiological function
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the cystatin M/E-cathepsin L balance is essential for tissue homeostasis in epidermis, hair follicles, and cornea. Activation of cathepsin D and transglutaminase-1 are downstream events, dependent of cathepsin L activity
physiological function
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cathepsin L inactivates trypsinogen and counteracts the ability of cathepsin B to form active trypsin
physiological function
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granule-bound cathepsins are essential for processing perforin to its active form, and CatL is an important, but not exclusive, participant in this process
physiological function
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granule-bound cathepsins are essential for processing perforin to its active form, and CatL is an important, but not exclusive, participant in this process
physiological function
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CatL cleavage of Zaire Ebola virus glycoprotein exposes its receptor-binding domain, thereby facilitating access to a putative cellular receptor in steps that lead to membrane fusion
physiological function
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cathepsin L plays a role in the immune system, in particular by degrading the invariant chain in MHC class II processing. Cathepsin L plays a part in recycling processes during axon outgrowth and synapse formation in the developing postnatal central nervous system
physiological function
-
cathepsin L plays a prominent role, jointly with PC1/3 and PC2, for production of dynorphins in brain
physiological function
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Ctsl is critical for the termination of growth factor signaling in the endosomal/lysosomal compartment of keratinocytes and, therefore, functions as an anti-tumor protease
physiological function
-
cathepsin L functions as a major protease responsible for cholecystokinin 8 production in mouse brain cortex, and participates with prohormone convertase 1/3 for cholecystokinin 8 production in pituitary cells
physiological function
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cathepsin L is required for ecotropic murine leukemia virus infection in NIH-3T3 cells
physiological function
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cathepsin L in secretory vesicles functions as a key protease for proteolytic processing of proneuropeptides (including enkephalin, neuropeptide Y, dynorphins, cholecystokinin, and others) and prohormones into active neuropeptides that are released to mediate cell-cell communication in the nervous system for neurotransmission. Cathepsin L is a key protease responsible for cholecystokinin 8 production in brain
physiological function
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the enzyme plays a role in host tissue migration and immune evasion
physiological function
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cathepsin L plays a role in glutamate receptor-induced nuclear factor-kappa B activation and excitotoxicity in rat striatal neurons
physiological function
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cathepsin L activity is required for calicivirus replication
physiological function
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cathepsin L activity is required for calicivirus replication
physiological function
-
cathepsin L activity is required for calicivirus replication
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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-aminobenzoic acid-Lys-Leu-Ala-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ala + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
-
-
?
2-aminobenzoyl-Ala-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Ala-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
-
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?
2-aminobenzoyl-Arg-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Arg-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
-
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?
2-aminobenzoyl-Asn-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Asn-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Gln-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gln-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
-
-
?
2-aminobenzoyl-Glu-Glu-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Glu-epsilon-amino-caproic acid-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
-
-
?
2-aminobenzoyl-Glu-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
-
-
?
2-aminobenzoyl-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Gly-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-His-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-His-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
-
-
?
2-aminobenzoyl-Ile-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Ile-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
-
-
?
2-aminobenzoyl-Leu-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Leu-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Arg-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Arg-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
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?
2-aminobenzoyl-Lys-Asn-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Asn-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
-
-
?
2-aminobenzoyl-Lys-Asp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Asp-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
-
-
?
2-aminobenzoyl-Lys-Gln-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Gln-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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-
-
-
?
2-aminobenzoyl-Lys-Glu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Glu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Gly-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Gly-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-His-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-His-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Ile-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Ile-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Arg-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Arg-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Asn-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Asn-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Gln-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Gln-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Glu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Glu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Gly-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Gly-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-His-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + His-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ile-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ile-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Leu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Leu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Phe-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Phe-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Pro-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Pro-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ala-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ala-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Arg-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Arg-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gln-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Gln-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Glu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Glu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gly-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Gly-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-His-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-His-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ile-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ile-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Leu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Leu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Phe-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Phe-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Pro-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Pro-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Val-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Val-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Val-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Val-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Asn-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Asn + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Asp-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Asp + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Gln-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Gln + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Glu-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Glu + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Gly-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Gly + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-His-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-His + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Ile-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ile + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Lys-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Lys + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Met-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Met + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Phe-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Phe + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Pro-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Pro + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Ser-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ser + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Thr-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Thr + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Val-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Val + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Lys-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Lys-epsilon-amino-caproic acid-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Met-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Met-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Phe-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Phe-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Pro-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Pro-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Ser-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Ser-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Thr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Thr-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Trp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Trp-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Tyr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Tyr-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Val-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Val-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Met-Ile-Ser-Leu-Met-Lys-Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Ile-Trp-NH2 + H2O
2-aminobenzoyl-Met-Ile-Ser-Leu-Met-Lys + Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg + 2-aminobenzoyl-Met-Ile-Ser-Leu-Met + Lys-Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg + Ser-Ser-Arg-Ile-Trp-NH2
-
-
-
-
?
2-aminobenzoyl-Phe-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Phe-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Val-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Val-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
3-carboxypropionyl-Ala-Phe-Lys-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
48 kDa intermediate of cathepsin D + H2O
34 kDa mature cathepsin D + ?
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Ala-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Ala-3-nitrotyrosineamide
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Gln-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Gln-3-nitrotyrosineamide
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Ser-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Ser-3-nitrotyrosineamide
-
-
-
-
?
actomyosin + H2O
?
-
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
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
benzoyl-Phe-Ala-Arg-4-methoxy-2-naphtylamide + H2O
benzoyl-Phe-Ala-Arg + 4-methoxy-2-naphthylamine
-
-
-
?
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
28.61% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
88.77% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-L-citrulline-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-L-citrulline 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Leu-L-Leu-L-Glu-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-L-Leu-L-Glu + 7-amino-4-methylcoumarin
76.66% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-trifluoromethylcoumarin
-
cathepsin L specific synthetic substrate
-
-
?
benzyloxycarbonyl-Leu-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methyl-coumarin
-
-
-
-
-
benzyloxycarbonyl-Leu-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Lys-Gln-Lys-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
-
preferred substrate
-
-
?
benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
benzyloxycarbonyl-Lys + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Phe-Arg + 4-methoxy-beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Val-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Cbz-Phe-Arg-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
CCAAT-displacement protein/cut homeobox protein + H2O
p90 isoform of CCAAT-displacement protein/cut homeobox protein + p110 isoform of CCAAT-displacement protein/cut homeobox protein + ?
-
-
-
-
?
D-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Disrupted in renal carcinoma 2 + H2O
?
-
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
-
-
?
dynamin + H2O
?
-
CatL is highly reactive toward recombinant dynamin at pH 5.0 and 6.0
-
-
?
interleukin-8 precursor + H2O
?
-
enzyme plays an important role in IL-8 processing in inflammatory sites
-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
28.66% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
L-arginine 7-amido-4-methylcoumarin + H2O
?
-
very poor substrate
-
-
?
L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
L-Val-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
L-Val-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-Tyr-7-amido-4-methylcoumarin + H2O
Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
N-acetyl-Phe-Arg-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-Phe-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-2-(4-methoxynaphthylamide) + H2O
N-benzyloxycarbonyl-Phe-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
N-carbobenzoxy-L-arginine-L-arginine 7-amido-4-methylcoumarin + H2O
?
-
7% of the activity with N-carbobenzoxy-L-phenylalanine-L-arginine 7-amido-4-methylcoumarin
-
-
?
N-carbobenzoxy-L-phenylalanine-L-arginine 7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-Arg 2-naphthylamide + H2O
Nalpha-benzoyl-L-Arg + 2-naphthylamine
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
precursor form 77IL-8 of interleukin-8 + H2O
precursor form 72IL-8 of interleukin-8 + ?
-
cleavage between Arg5 and Ser6
-
?
pro-neuropeptide Y + H2O
neuropeptide Y + ?
-
cathepsin L cleaves pro-neuropeptide Y (1-70) to generate neuropeptide Y-Gly (1-38) and the COOH-terminal peptide fragment (39-70)
-
-
?
Pro-Phe-Arg-4-methylcoumarin 7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
-
secretory leukocyte protease inhibitor + H2O
?
-
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
-
-
?
succinyl-Ala-Phe-Lys-4-methylcoumarin 7-amide + H2O
succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Arg-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Val-Pro-Arg-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
1% activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
thyroglobulin type-1 domain + H2O
?
-
the thyroglobulin type-1 domain is a protein module that occurs in a variety of secreted and membrane proteins and is recognised as a potent inhibitor of cysteine proteases. Nevertheless, at high enzyme and inhibitor concentrations in the mircomolar range cathepsin L degrades thyroglobulin type-1 domain
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
trypsinogen + H2O
trypsin + ?
-
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)
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg + H2O
Tyr-Gly + Gly-Phe-Leu-Arg-Arg
-
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
Tyr-Gly + Gly-Phe-Leu-Arg-Arg-Ile
-
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Gly-Leu + H2O
?
-
cleavage sites Gly-Gly and Met-Arg
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Phe + H2O
?
-
cleavage sites: Gly-Gly and Met-Arg
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Phe-NH2 + H2O
?
-
cleavage sites Gly-Gly and Met-Arg
-
-
?
Zaire Ebola virus glycoprotein + H2O
?
-
-
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
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
no activity
-
-
-
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
-
7% activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
no activity
-
-
-
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
weak activity
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
weak activity
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
9% activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
100% activity
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
100% 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
preferred substrate
-
-
?
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
-
-
-
?
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
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
substrate for both cathepsin L and cathepsin B
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
100% 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
most efficient substrate
-
-
?
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
-
substrate for both cathepsin L and cathepsin B
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Collagen + H2O
?
-
selective cleavage of terminal peptides leads to conversion of beta- and higher components mainly to alpha-chains
-
-
?
Collagen + H2O
?
-
conversion of cross-linked beta-chain dimers into uncross-linked alpha-chain monomers
-
-
?
D-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
D-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Elastin + H2O
?
-
the enzyme shows distinctive preferences in degrading elastins from bovine neck ligament, aorta, and lung
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
-
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
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
-
recombinant endorepellin is an in vitro substrate
-
-
?
fibronectin + H2
?
-
enzyme cleaves fibronectin to produce two bands
-
?
fibronectin + H2
?
-
enzyme cleaves fibronectin to produce two bands
-
?
Gelatin + H2O
?
on gelatin-zymography, the purified pro-mature enzyme of cathepsin L is capable of hydrolyzing 0.1% gelatin at pH 7.5
-
-
?
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
-
-
?
Insulin B-chain + H2O
?
-
preferential cleavage at: Glu13-Ala14, Leu17-Val18, and Tyr26-Thr27
-
-
?
Insulin B-chain + H2O
?
-
main cleavage sites: Glu13-Ala14 and Tyr26-Thr27, minor cleavage sites: Val2-Asn3, Asn3-Gln4, Cys7-Glu8, Tyr16-Leu17, Leu17-Val18
-
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
preferred substrate for isoform CatL5
-
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-pyroglutamyl-L-Phe-Leu-p-nitroanilide + H2O
L-pyroglutamyl-L-Phe-Leu + p-nitroaniline
-
-
-
-
?
L-pyroglutamyl-L-Phe-Leu-p-nitroanilide + H2O
L-pyroglutamyl-L-Phe-Leu + p-nitroaniline
-
-
-
-
?
Nipah virus fusion protein + H2O
?
-
proteolytically processed within endosomes by cathepsin L
-
-
?
Nipah virus fusion protein + H2O
?
-
cathepsin L specifically converts Nipah virus fusion protein to a mature and fusogenic form
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
pro-dipeptidyl peptidase I
?
-
cathepsin L could be an important activator of dipeptidyl peptidase I in vivo
-
?
proheparanase + H2O
active form of heparanase + ?
-
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
-
-
?
proheparanase + H2O
active form of heparanase + ?
-
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
-
-
?
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
preferred substrate for isoform CatL1G
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
type 1 collagen + H2O
?
-
isoform Catl1G completely digests collagen type 1
-
-
?
type 1 collagen + H2O
?
-
efficient cleavage of type 1 collagen by isoform CatL5 is limited to the beta-and gamma-chains
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Arg + H2O
Tyr-Gly + Gly-Phe-Met-Arg-Arg
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
-
enzyme may involve in invasion of cercaria into fish and development to metacercaria, excystment of metacercaria, and protein digestion of adult
-
-
-
additional information
?
-
proteolytic activity only under reducing conditions, e.g. in presence of dithiothreitol. No substrate: type IV collagen
-
-
-
additional information
?
-
proteolytic activity only under reducing conditions, e.g. in presence of dithiothreitol. No substrate: type IV collagen
-
-
-
additional information
?
-
-
enzyme activity plays a pivotal role in prolactin-induced spermatogonial apoptosis
-
?
additional information
?
-
-
3% with benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin and 1% with both L-Arg-7-amido-4-methylcoumarin and Boc-Phe-Ser-Arg-7-amido-4-methylcoumarin. No activity with Boc-Gln-Arg-Arg-7-amido-4-methylcoumarin and succinyl-Leu-Leu-Tyr-7-amido-4-methylcoumarin
-
-
-
additional information
?
-
-
the cathepsin B and H specific synthetic substrates benzyloxycarbonyl-L-Ala-L-Ala-7-amido-4-trifluoromethylcoumarin and L-Arg-7-amido-4-methylcoumarin do not show any hydrolysis with the partially purified enzyme
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
isoform CatL1G can cleave substrates with proline residues at P2
-
-
-
additional information
?
-
-
no activity with benzyloxycarbonyl-Phe-Ala-4-methylcoumarin 7-amide and with benzyloxycarbonyl-Phe-Met-4-methylcoumarin 7-amide
-
-
-
additional information
?
-
-
the enzyme is involved in tissue destruction in arthritis
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
differentiation of human macrophages within the lung is accompanied by synthesis and expression of cathepsin L
-
-
-
additional information
?
-
-
CAT L plays a significant role in numerous important physiological and pathological processes, such as bone resorption, cancer progression and atherosclerosis
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
catL is essential for epidermal homeostasis and regular hair follicle morphogenesis and cycling
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
pituitary gland may utilize the cathepsin L and prohormone convertase pathways for producing propiomelanocortin-derived peptide hormones
-
-
-
additional information
?
-
-
the enzyme does not hydrolyze ortho-aminobenzoic acid-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-KPVSTEQLAQ-N-[2,4-dinitrophenyl]ethylenediamine , Ortho-aminobenzoic acid-KPPVVLLPDQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine, and ortho-aminobenzoic acid-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
-
-
additional information
?
-
no activity towards benzyloxycarbonyl-Gly-Gly-L-Arg-7-amido-4-methylcoumarin
-
-
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
cathepsin L expression levels regulate cell responsiveness to IGF-type I, function for cathepsin L in the control of the tumorigenic/metastatic phenotype
-
-
-
additional information
?
-
-
cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
-
-
-
additional information
?
-
-
the enzyme has a preference for hydrophobic amino acids in P2 and P3 residues
-
-
-
additional information
?
-
-
the enzyme removes the Ca-sensitivity of ATPase activity of myofibrils
-
-
-
additional information
?
-
-
involved in extracellular food digestion
-
-
-
additional information
?
-
the recombinant enzyme is inefficient in hydrolyzing azocasein, fibrinogen, and bovine serum albumin
-
-
-
additional information
?
-
-
the enzyme plays a most important role in intralysosomal proteolysis in hepatocytes
-
-
-
additional information
?
-
-
plays a crucial role in the pathogenesis of adjuvant arthritis
-
-
-
additional information
?
-
-
basement membrane of larval brains contains two substrate proteins
-
?
additional information
?
-
-
the enzyme is suggested to play a crucial role in the degradation of the basement membranes
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
-
-
-
additional information
?
-
-
granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
-
-
-
additional information
?
-
-
leucine is preferred over phenylalanine in position P2
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
?
-
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
-
-
?
Disrupted in renal carcinoma 2 + H2O
?
-
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 + ?
-
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
-
-
?
interleukin-8 precursor + H2O
?
-
enzyme plays an important role in IL-8 processing in inflammatory sites
-
?
Nipah virus fusion protein + H2O
?
-
proteolytically processed within endosomes by cathepsin L
-
-
?
pro-dipeptidyl peptidase I
?
-
cathepsin L could be an important activator of dipeptidyl peptidase I in vivo
-
?
secretory leukocyte protease inhibitor + H2O
?
-
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
-
-
?
trypsinogen + H2O
trypsin + ?
-
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)
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Zaire Ebola virus glycoprotein + H2O
?
-
-
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
-
?
Gelatin + H2O
?
A5HJW4
on gelatin-zymography, the purified pro-mature enzyme of cathepsin L is capable of hydrolyzing 0.1% gelatin at pH 7.5
-
-
?
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
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
proheparanase + H2O
active form of heparanase + ?
-
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
-
-
?
proheparanase + H2O
active form of heparanase + ?
-
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
-
-
?
type 1 collagen + H2O
?
-
isoform Catl1G completely digests collagen type 1
-
-
?
type 1 collagen + H2O
?
-
efficient cleavage of type 1 collagen by isoform CatL5 is limited to the beta-and gamma-chains
-
-
?
additional information
?
-
-
enzyme may involve in invasion of cercaria into fish and development to metacercaria, excystment of metacercaria, and protein digestion of adult
-
-
-
additional information
?
-
-
enzyme activity plays a pivotal role in prolactin-induced spermatogonial apoptosis
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
isoform CatL1G can cleave substrates with proline residues at P2
-
-
-
additional information
?
-
-
the enzyme is involved in tissue destruction in arthritis
-
-
-
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
-
-
-
additional information
?
-
-
differentiation of human macrophages within the lung is accompanied by synthesis and expression of cathepsin L
-
-
-
additional information
?
-
-
CAT L plays a significant role in numerous important physiological and pathological processes, such as bone resorption, cancer progression and atherosclerosis
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
catL is essential for epidermal homeostasis and regular hair follicle morphogenesis and cycling
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-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
pituitary gland may utilize the cathepsin L and prohormone convertase pathways for producing propiomelanocortin-derived peptide hormones
-
-
-
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
-
?
additional information
?
-
P06797
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
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
cathepsin L expression levels regulate cell responsiveness to IGF-type I, function for cathepsin L in the control of the tumorigenic/metastatic phenotype
-
-
-
additional information
?
-
-
cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
-
-
-
additional information
?
-
-
involved in extracellular food digestion
-
-
-
additional information
?
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-
the enzyme plays a most important role in intralysosomal proteolysis in hepatocytes
-
-
-
additional information
?
-
-
plays a crucial role in the pathogenesis of adjuvant arthritis
-
-
-
additional information
?
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-
the enzyme is suggested to play a crucial role in the degradation of the basement membranes
-
?
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
-
-
-
additional information
?
-
Q8IT42
granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
-
-
-
additional information
?
-
-
granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(13alpha,17alpha,20S,24Z)-3-hydroxylanosta-7,24-dien-26-oic acid
-
competitive inhibition
(13alpha,17alpha,20S,24Z)-3-oxolanosta-7,24-dien-26-oic acid
-
competitive inhibition
(2E)-2-[(3-bromophenyl)(3,4,5-trifluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3,5-dichlorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3,5-difluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)[3-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)[4-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(4-bromophenyl)[4-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[[3,5-bis(trifluoromethyl)phenyl](3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-[(3E)-28-methoxy-28-oxours-12-en-3-ylidene]acetic acid
-
competitive inhibition
(2R,3R)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-isonipecotyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-isonipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-3-([(2S)-1-[(8-carbamimidamidooctyl)amino]-4-methyl-1-oxopentan-2-yl]carbamoyl)oxirane-2-carboxylic acid
-
-
(2S,3S)-dibenzyl-1-[1-[N-(tert-butoxycarbonyl)-(R)-leucyl]-(S)-aziridine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[1-[N-(tert-butoxycarbonyl)-(S)-leucyl]-(S)-aziridine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(R)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-prolyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R+S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-pipecolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-isonipecotyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-oxirane-2,3-dicarboxylic acid 2-[((S)-1-benzylcarbamoyl-2-phenyl-ethyl)-amide] 3-[[2-(4-hydroxy-phenyl)-ethyl]-amide]
(2S,3S)-trans-epoxysuccinyl-L-leucylamido-3-methylbutane ethyl ester
0.1 mM
(2S,3S+2R,3R)-dibenzyl-1-[desthiobiotinyl-6-aminohexanoyl]-aziridine-2,3-dicarboxylate
-
-
(2Z)-2-[(3-bromo-2-fluorophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromo-4-fluorophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2,3,4,5-tetrafluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2,3-difluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2,6-difluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[[3,5-bis(trifluoromethyl)phenyl](4-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetic acid
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
(E)N-[(S)1-[(S)2-cyano-1-pyrrolidinecarbonyl]-3-methylbutyl]-2,3-diphenylacrylamide
-
selective towards cathepsin L over cathepsin B
(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucine(3-methylbutyl)-amide
-
0.01 mg/ml
(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L-isoleucyl-L-proline methyl ester
-
CA-074Me, more than 99% inhibition at 0.1 mM
(R)-S-2-(2-ethylphenylamino)-2-oxoethyl 2-(2-(tert-butoxycarbonylamino)-3-(1H-indol-3-yl)propanoyl)hydrazinecarbothioate
-
R-enantiomer, thiol ester containing a diacyl hydrazine functionality and one stereogenic center
(S)-2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl 2-(2-(tert-butoxycarbonylamino)-3-(1H-indol-3-yl)propanoyl)hydrazinecarboxylate
-
-
(S)-S-2-(2-ethylphenylamino)-2-oxoethyl 2-(2-(tert-butoxycarbonylamino)-3-(1H-indol-3-yl)propanoyl)hydrazinecarbothioate
-
S-enantiomer, thiol ester containing a diacyl hydrazine functionality and one stereogenic center
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([2-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-3-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-4-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(thiophen-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[methyl(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(methylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(phenylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-([[4-([[(dimethylamino)methyl]sulfonyl]amino)phenyl]carbonyl]amino)-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([2-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-fluoro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([4-[(ethylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2,4-dimethyl-1,3-thiazol-5-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-(methylsulfamoyl)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-([[4-(1-methylethyl)-1,3-thiazol-2-yl]sulfonyl]amino)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-sulfamoylphenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methyl-1H-imidazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methylethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2,2,2-trifluoroethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2-methylphenyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methylpyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(5-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[4-methyl-N-(thiophen-3-ylcarbonyl)-L-leucyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(benzylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(butylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(cyclopropylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-chloropyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(3-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(4-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(cyclohexylmethyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1- (L-trans-epoxysuccinyl-leucylamino)-4-guanidinobutane
-
i.e. E-64, 0.1 mM, complete loss of activity
1-nathalenesulfonyl-Ile-Trp-CHO
-
treatment of cells results in suppression of cellular proliferation and the induction of a cell death with no detecable caspase-3 activation or DNA fragmentation. Cell death is associated with increased accumulation of cathepsin D, cellular vacuolization, expression of the mannose 6-phosphate recepto, and the autophagy marker LC-II
2,3,7,8-tetrachlorodibenzodioxin
-
treatment of cells results in resistance to apoptosis, increased expression of the tumor marker cathepsin L, and a high degree of invasiveness
2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarboxylate
-
unreactive to transesterification by cysteine and dithiothreitol nucleophiles. Inhibitor remains intact for greater than 24 h when incubated with cathepsin L under stoichiometric conditions, and in the presence of assay buffer
2-cyano-4-(2-hydroxyethoxy)-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-4-[(1,4-dioxaspiro[4.5]dec-8-ylmethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
-
-
2-cyano-4-[(2-cyclopentylethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
-
-
2-cyano-4-[(6,8-dioxaspiro[3.5]non-7-ylmethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
-
-
2-cyano-4-[(cyclohexylmethyl)(methyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
-
2-cyano-4-[(cyclohexylmethyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
-
2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-N-(2-phenylethyl)-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-4-[[(4,4-difluorocyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
-
2-cyano-4-[[(4,4-dimethylcyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
-
2-cyano-4-[[1-(2-hydroxyethyl)piperidin-4-yl]methoxy]-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-(1-methyl-4-phenylpiperidin-4-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-(2-phenylethyl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-(4,5-dimethoxybiphenyl-2-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-methyl-4-(piperidin-4-ylmethoxy)-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-methyl-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-methyl-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[4.5]dec-8-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-methyl-4-[(spiro[3.5]non-7-ylmethyl)amino]-6-[(2,2,6,6-tetramethylpiperidin-4-yl)oxy]pyrimidine-5-carboxamide
-
-
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-methyl-4-[[1-(1-methylethyl)piperidin-4-yl]methoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-[(1-methyl-4-phenylpiperidin-4-yl)methyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-[(1R)-2-pyridin-2-yl-1-(pyrrolidin-1-ylmethyl)ethyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-cyano-N-[5-[(1-methylpiperidin-4-yl)oxy]biphenyl-2-yl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
2-[cyclohexyl(methyl)amino]-4H-3,1-benzothiazin-4-one
-
selective towards cathepsin L over cathepsin G, chymotrypsin, trypsin, human angiotensin-converting enzyme, human leukocyte elastase, acetylcholinesterase
2RS,3RS)-2-benzyl-3-ethyl-1-[N-(benzyloxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
3-chloro-N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]benzamide
-
pH and temperature not specified in the publication
3-[[(2S)-2-[([3-acetyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
3-[[(2S)-2-[[(4-[[(4-aminophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
4-[(1-acetylpiperidin-4-yl)methoxy]-2-cyano-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
-
4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
-
-
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzoic acid
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
5-bromo-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
-
-
6-(4-chlorobenzyl)-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclooctylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-piperidin-1-ylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(3,3-dimethylbutyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(3-cyclohexylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(4,4-dimethylpentyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-[2-(3-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-[[4-(1-acetyl-1,2,3,6-tetrahydropyridin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
6-[[4-(1-acetylpiperidin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
6-[[4-(4-acetyl-1,4-diazepan-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)-2-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-[[4-(4-acetylpiperazin-1-yl)-3-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4,4-difluorocyclohexyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2-cyclohexylethyl)-6-(4-methoxybenzyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-(phenoxymethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(phenylamino)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(pyridin-2-yloxy)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(pyridin-2-ylsulfanyl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[[methyl(phenyl)amino]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
benzofuran-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-2-naphthylen-2-yl)amide
-
-
benzofuran-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-2-phenyl-ethyl)amide
-
-
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxo-3-(1,1':4',1''-terphenyl-4-yl)propan-2-yl]carbamate
-
-
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(2'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(3'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(4'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-3-(3'-aminobiphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-3-(3'-chlorobiphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-3-(biphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
-
benzyloxycarbonyl-Phe-Arg-diazomethyl ketone
-
more than 99% inhibition at 0.1 mM
benzyloxycarbonyl-Phe-Phe fluoromethylketone
-
cell-permeable irreversible cathepsin inhibitor
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(2-phenylethyl)amide
-
the inhibitor shows a 310fold and 210fold selectivity for cathepsin L over cathepsin K and B, respectively
CA-074
i.e. N-(L-3-trans-propylcarbamoyl-oxirane-2-carbonyl)-L-isoleucyl-L-proline, about 25% residual activity at 0.02 mM; i.e. N-(L-3-trans-propylcarbamoyl-oxirane-2-carbonyl)-L-isoleucyl-L-proline, about 75% residual activity at 0.02 mM
CAA0225
-
i.e. (2S,3S)-oxirane-2,3-dicarboxylic acid 2-[((S)-1-benzylcarbamoyl-2-phenyl-ethyl)-amide]3-[[2-(4-hydroxy-phenyl)-ethyl]-amide], a cathepsin L-specific inhibitor
Chloroquine
-
chloroquine inhibits the infection with live Nipah virus and Hendra virus at a concentration of 1 microM in vitro. The mechanism for the antiviral action likely is the inhibition of cathepsin L, which is essential for the processing of the viral fusion glycoprotein and the maturation of newly budding virions
CID 23631927
-
38% inhibition at 0.025 mM, sub-nanomolar slow-binding, reversible inhibitor of human cathepsin L with cathepsin L/B selectivity of above 700fold that blocks SARS-CoV and Ebola pseudotype virus entry in human cells
Cu2+