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Information on EC 3.4.22.B49 - cathepsin L1
for references in articles please use BRENDA:EC3.4.22.B49preliminary BRENDA-supplied EC number
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3.4.22.B49 cathepsin L1Specify your search results
Word Map
- 3.4.22.B49
- cathepsins
- fasciola
- hepatica
- fluke
-
fasciolosis
-
metacercariae
-
helminth
- gigantica
- medicine
-
excysted
-
trematode
-
excretory-secretory
-
immunodiagnosis
- agriculture
-
mimotopes
- diagnostics
The enzyme appears in viruses and cellular organisms
Reaction Schemes
clear preference for Arg at P1 position (Lys, Glu, Thr, and Met are less efficient). FheCL1 shows distinct preference for hydrophobic amino acids in the P2, Leu is favored. Cathepsin L1 can accommodate Pro in the P2 position, but less efficiently than cathepsin L2. FheCL1 produces clear degradation fragments from collagen
Synonyms
cathepsin l1, ctsl1, fhcl1, fhecl1, catl1, fgcatl1h, cgctsl1, cpfhw, cathepsin l1h, da-ctsl1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cathepsin L1
cathepsin L1 proteinase
-
-
-
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CatL1
CL1
FhCL1
FheCL1
cathepsin L1
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-
-
-
CL1
-
-
-
-
FheCL1
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
clear preference for Arg at P1 position (Lys, Glu, Thr, and Met are less efficient). FheCL1 shows distinct preference for hydrophobic amino acids in the P2, Leu is favored. Cathepsin L1 can accommodate Pro in the P2 position, but less efficiently than cathepsin L2. FheCL1 produces clear degradation fragments from collagen
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY
60616-82-2
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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
acetyl-FR-7-amido-4-trifluoromethyl coumarin + H2O
acetyl-FR + 7-amino-4-trifluoromethyl coumarin
-
-
-
?
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
-
cathepsin L1
-
-
?
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
-
cathepsin L1
-
-
?
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
cathepsin L1
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
FheCL1
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-L-phenylalanyl-L-arginine 4-methylcoumarinyl-7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Pro-L-Arg + 7-amino-4-methylcoumarin
FheCL1
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
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cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
benzyloxycarbonyl-Phe-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Phe-Arg + 4-nitroaniline
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-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-7-amido-4-trifluoromethylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-trifluoromethylcoumarin
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best substrate
-
-
?
benzyloxycarbonyl-Phe-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
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renatured CPFhW
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-
?
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Collagen + H2O
?
whereas FheCL1 produces clear degradation fragments, FheCL2 degrades the collagen completely, particularly at pH 4.0, indicating that only the latter cleaves efficiently within the helical structures
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-
?
Fibrinogen + H2O
?
enzyme FhCL3 is capable of degradation of the fibrinogen alpha-chain, beta-chain, and gamma-chain
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-
?
H-Leu-Val-Tyr-4-methylcoumarinyl-7-amide + H2O
H-Leu-Val-Tyr + 7-amino-4-methylcoumarin
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cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
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-
?
H-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
H-Leu-Val-Tyr + 7-amino-4-methylcoumarin
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-
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?
human IgG + H2O
?
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both cathepsins L produce similar degradation patterns and cleave all human IgG subclasses at the hinge region, yielding at pH 7.3 and 37°C Fab and Fc fragments in the case of IgG1 and IgG3 or Fab(2) and Fc in IgG2 and IgG4. Both liver fluke cathepsins L cleave the peptide bonds 237His-Thr, 237Glu-Cys, 233Gly-Asp, and 241Ser-Cys of the gamma1, gamma2, gamma3, and gamma4 H chains, respectively. Therefore, the enzymes are interacting with the following P3-P'3 sequences, Lys-Thr-His-Thr-Cys-Pro, Cys-Val-Glu-Asp-Pro-Pro, Pro-Leu-Gly-Asp-Thr-Thr, and Cys-Pro-Ser-Cys-Pro-Ala. The specificity of the liver fluke cathepsins L for peptide bonds in proteins is less defined. The P1 position, for instance, can be occupied by hydrophobic, hydrophilic, acidic, or basic residues. The P3 and P2 positions are occupied by hydrophobic amino acids with the exception of the gamma1 sequence which contains a basic lysine and a hydrophilic threonine, respectively. In addition the specificity between the enzyme and its substrate would depend on which of the amino acids of the substrate can be really exposed to the active site
-
-
?
Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Leu-Val-Tyr + 7-amino-4-methylcoumarin
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cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
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-
?
N-benzyloxycarbonyl-FR-4-nitroanilide + H2O
N-benzyloxycarbonyl-FR + 4-nitroaniline
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-
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?
N-benzyloxycarbonyl-FR-7-amido-4-trifluoromethylcoumarin + H2O
N-benzyloxycarbonyl-FR + 7-amino-4-trifluoromethylcoumarin
best substrate
-
-
?
N-benzyloxycarbonyl-GPR-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-GPR + 7-amino-4-methylcoumarin
-
-
-
?
N-benzyloxycarbonyl-VVR-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-VVR + 7-amino-4-methylcoumarin
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?
procathepsin L1 + H2O
?
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procathepsin L1 autocatalytically processes and activates to its mature enzyme (FheCL1) over a wide pH range 4.0-7.3. Activation is more rapid at low pH. Maturation initiates with cleavages of a small proportion of molecules within the central region of the prosegment, possibly by intramolecular events. Activation to fully mature enzymes is achieved by a precise intermolecular cleavage at a Leu12-Ser11-/-His10 sequence within the nonconserved C-terminal region of the prosegment. Active site variant FheproCL1C26G and a double variant FheproCL1L12P/C26G cannot autocatalytically process. The former is susceptible to trans-processing at a Leu12-Ser11-/-His10 sequence by preactivated FheCL1, but the latter is not
-
-
?
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide + H2O
succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
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cathepsin L1
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?
succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
tosyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
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-
-
-
?
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
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cathepsin L1
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?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
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-
-
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?
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
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-
-
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?
t-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
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cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
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-
?
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tert-butoxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
FheCL1
-
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
cathepsin L1
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-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
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cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide + H2O
tosyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
cathepsin L1
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Lys + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-Gly-Pro-Lys-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Lys + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
Z-Phe-Arg-OMe + SerNH2
Z-Phe-Arg-Ser-NH2 + methanol
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peptide synthesis
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
FheCL1
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
FheCL1
-
-
?
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
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
Hemoglobin + H2O
?
-
Fasciola hepatica secretes cathepsin L cysteine proteases to invade its host, migrate through tissues and digest hemoglobin, its main source of amino acids. FheCL1 can degrade hemoglobin to small peptides, predominantly of 414 residues, but cannot release free amino acids. It is suggested that hemoglobin degradation is not completed in the gut lumen but the resulting peptides are absorbed by the gut epithelial cells for further processing by intracellular di- and amino-peptidases to free amino acids that are distributed through the parasite tissue for protein anabolism. The action of FheCL1 is enhanced by glutathione, the major reducing agent found in red blood cells
-
-
?
Hemoglobin + H2O
?
FhCL1 cleaves substrates with hydrophobic residues (Phe and Leu) in the P2 position with catalytic rates (kcat/Km) that are 25- and eightfold greater, respectively, than FhCL2. In comparison to human cathepsin L, which can accommodate a wide range of amino acids in the S2 subsite, the S2 subsite of FhCL1 is restricted. Hydrophobic residues are most susceptible to cleavage, in the order Leu > Val > Ala > Phe. Together, these four residues make up about 42% of the hemoglobin molecule and, therefore, it seems that FhCL1 has been specifically adapted to degrade the host substrate, which it exploits as nutrient. Substrates with proline in the P2 position, which are good substrates for FhCL2 are poorly cleaved by FhCL1 (and not at all by human cathepsin L)
-
-
?
Hemoglobin + H2O
?
-
FheCL1 can degrade hemoglobin to small peptides, predominantly of 414 residues, but cannot release free amino acids. FheCL1 can not cleave its natural substrate hemoglobin in the pH range pH 5.5 and pH 7.0. Digestion occurs only at or below pH 4.5, which coincides with pH-induced dissociation of the hemoglobin tetramer. The acidic pH of the parasite relaxes the hemoglobin structure, making it susceptible to proteolysis by FheCL1. The P1 position could be occupied by many amino acids but most preferentially Leu. FheCL1 preferentially cleaves bonds where the P2 position is occupied with hydrophobic residues (in order of decreasing efficiency: Leu, Val, Ala, Phe) and is observed for the digestion of both hemoglobin-alpha and hemoglobin-beta
-
-
?
Hemoglobin + H2O
?
-
enzyme does not cleave its natural substrate hemoglobin in the pH range pH 5.5 and pH 7.0. Digestion occurs only at pH 4.5, which coincides with pH-induced dissociation of the hemoglobin tetramer
degradation to small peptides of 4-14 residues, no release of free amino acids
-
?
Hemoglobin + H2O
?
purified recombinant CL1 is not able to hydrolyze hemoglobin
-
-
?
ovalbumin + H2O
?
-
FheCL1 can degrade ovalbumin from pH 3.5 to pH 8.0
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
FheCL1
-
-
?
additional information
?
-
-
benzyloxycarbonyl-Gly-Pro-Atg-7-amido-4-methylcoumarin and benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin are not hydrolyzed
-
-
?
additional information
?
-
-
does not hydrolyze Arg-4-nitroanilide, N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide, benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin, and benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
substrate specificity supports the hypothesis that Diaprepes abbreviatus CTSL1 is a unique basic cathepsin L and protease inhibitor studies also suggest unique activity, unlike other characterized acidic cathepsin Ls. No activity with N-succinyl-AAPF-4-nitroanilide and HR-4-nitroanilide
-
-
?
additional information
?
-
-
substrate specificity supports the hypothesis that Diaprepes abbreviatus CTSL1 is a unique basic cathepsin L and protease inhibitor studies also suggest unique activity, unlike other characterized acidic cathepsin Ls. No activity with N-succinyl-AAPF-4-nitroanilide and HR-4-nitroanilide
-
-
?
additional information
?
-
-
the enzyme mediates kinin release from high molecular weight kininigen
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-
?
additional information
?
-
-
the enzyme facilitates the penetration of the parasite though the tissue of its host, and also participates in functions such as feeding and immune evasion
-
-
?
additional information
?
-
-
cathepsin L1 and cathepsin L2 proteinases may be the prime mechanism by which the parasite penetrates tissue
-
-
?
additional information
?
-
-
renatured enzyme shows no activity with benzyloxycarbonyl-Phe-Arg-beta-naphthylamide
-
-
?
additional information
?
-
wild-type FheCL1 shows clear preference for Arg at P1. Other residues accommodated in this position including Lys, Glu, Thr, and Met are all cleaved at similar relative rates to that observed for human cathepsin L and cathepsin K. Similar results are obtained for the variants FheCL1 L67Y and FheCL1 L205A. FheCL1 shows distinct preference for hydrophobic amino acids in the P2, Leu is favored. FheCL1 and FheCL2 are similar to cathepsin K with regard to their preference for a P2 Leu over Phe (human cathepsin L has a preference for P2 Phe over Leu). Both enzymes can accommodate Pro in the P2 position, but this is more readily accepted by FheCL2 compared with FheCL1. Neither enzyme, however, cleaves substrates with this residue in the P2 position as readily as human cathepsin K
-
-
?
additional information
?
-
-
wild-type FheCL1 shows clear preference for Arg at P1. Other residues accommodated in this position including Lys, Glu, Thr, and Met are all cleaved at similar relative rates to that observed for human cathepsin L and cathepsin K. Similar results are obtained for the variants FheCL1 L67Y and FheCL1 L205A. FheCL1 shows distinct preference for hydrophobic amino acids in the P2, Leu is favored. FheCL1 and FheCL2 are similar to cathepsin K with regard to their preference for a P2 Leu over Phe (human cathepsin L has a preference for P2 Phe over Leu). Both enzymes can accommodate Pro in the P2 position, but this is more readily accepted by FheCL2 compared with FheCL1. Neither enzyme, however, cleaves substrates with this residue in the P2 position as readily as human cathepsin K
-
-
?
additional information
?
-
-
enzyme preferentially cleaves bonds where the P2 position is occupied with hydrophobic residues, this preference follows the order Leu>Val>Ala>Phe, and is observed for the digestion of both hemoglobin-alpha and hemoglobin-beta
-
-
?
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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
Hemoglobin + H2O
?
-
Fasciola hepatica secretes cathepsin L cysteine proteases to invade its host, migrate through tissues and digest hemoglobin, its main source of amino acids. FheCL1 can degrade hemoglobin to small peptides, predominantly of 414 residues, but cannot release free amino acids. It is suggested that hemoglobin degradation is not completed in the gut lumen but the resulting peptides are absorbed by the gut epithelial cells for further processing by intracellular di- and amino-peptidases to free amino acids that are distributed through the parasite tissue for protein anabolism. The action of FheCL1 is enhanced by glutathione, the major reducing agent found in red blood cells
-
-
?
Hemoglobin + H2O
?
-
enzyme does not cleave its natural substrate hemoglobin in the pH range pH 5.5 and pH 7.0. Digestion occurs only at pH 4.5, which coincides with pH-induced dissociation of the hemoglobin tetramer
degradation to small peptides of 4-14 residues, no release of free amino acids
-
?
Hemoglobin + H2O
?
purified recombinant CL1 is not able to hydrolyze hemoglobin
-
-
?
additional information
?
-
-
the enzyme facilitates the penetration of the parasite though the tissue of its host, and also participates in functions such as feeding and immune evasion
-
-
?
additional information
?
-
-
cathepsin L1 and cathepsin L2 proteinases may be the prime mechanism by which the parasite penetrates tissue
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-benzyloxycarbonyl-FY(tert-butyl)-diazomethylketone
40.6% inhibition at 0.05 mM
N-benzyloxycarbonylphenylalanyl-t-butyl-tryrosyl diazomethylketone
-
40.6% inhibition at 0.05 mM
Aprotinin
-
complete inhibition at 50 nM at a molar ratio of enzyme to inhibitor of 17:1; inhibits enzyme activity almost completely at a molar ratio of enzyme to inhibitor of 17:1
E-64
-
i.e. L-trans-epoxysuccinyl-leucyamido(4-guanidino) butane, 26.6% inhibition at 0.05 mM
additional information
-
cathepsin L2 is completely inactivated by 4 mM tetranitromethane, cathepsin L1 is not inactivated
-
additional information
the enzyme's fibrinolytic activity is inhibited by plasma. Addition of GSH to plasma cannot counteract the inhibitory effect of plasma components for FhCL1
-
additional information
-
the enzyme's fibrinolytic activity is inhibited by plasma. Addition of GSH to plasma cannot counteract the inhibitory effect of plasma components for FhCL1
-
additional information
inhibitory interactions of human family 1 and 2 cystatins with cathepsin L1 are predicted and their stability and viability are verified through protein docking and comparative molecular dynamics, overview. The key amino acid residues surfaced via interaction energy, hydrogen bonding and solvent accessible surface area analysis for each cystatin-cathepsin L1 complex influence the mode of binding and thus control the diverse inhibitory affinity of cystatins towards cysteine proteases. Docking outputs of cathepsin L1 complexes with stefin A, stefin B, cystatin C, cystatin D, cystatin F, cystatin M/E, cystatin S, cystatin SA, and cystatin SN
-
additional information
-
inhibitory interactions of human family 1 and 2 cystatins with cathepsin L1 are predicted and their stability and viability are verified through protein docking and comparative molecular dynamics, overview. The key amino acid residues surfaced via interaction energy, hydrogen bonding and solvent accessible surface area analysis for each cystatin-cathepsin L1 complex influence the mode of binding and thus control the diverse inhibitory affinity of cystatins towards cysteine proteases. Docking outputs of cathepsin L1 complexes with stefin A, stefin B, cystatin C, cystatin D, cystatin F, cystatin M/E, cystatin S, cystatin SA, and cystatin SN
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTT
-
the action of FheCL1 is enhanced by glutathione, the major reducing agent found in red blood cells. In the presence of DTT, GSH and L-cysteine FheCL1 exhibited similar activation curves with maximal enzyme activity observed in the presence of each reducing agent at a concentration of 0.1 to 1.0 mM
L-Cys
-
the action of FheCL1 is enhanced by glutathione, the major reducing agent found in red blood cells. In the presence of DTT, GSH and L-cysteine FheCL1 exhibited similar activation curves with maximal enzyme activity observed in the presence of each reducing agent at a concentration of 0.1 to 1.0 mM
dithiothreitol
-
the cathepsins L needed the presence of dithiothreitol to digest IgG1, IgG2, and IgG4 whereas IgG3 was identically cleaved under both reducing and nonreducing conditions
glutathione
-
the action of FheCL1 is enhanced by glutathione, the major reducing agent found in red blood cells. In the presence of DTT, GSH and L-cysteine FheCL1 exhibited similar activation curves with maximal enzyme activity observed in the presence of each reducing agent at a concentration of 0.1 to 1.0 mM
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Endometritis
Endometrial expression of various genes (ISGs, PPARs, RXRs and MUC1) on day 16 post-ovulation in repeat breeder cows, with or without subclinical endometritis.
Endometritis
mRNA Expressions of Candidate Genes in Gestational Day 16 Conceptus and Corresponding Endometrium in Repeat Breeder Dairy Cows with Suboptimal Uterine Environment Following Transfer of Different Quality Day 7 Embryos.
Fascioliasis
Design and synthesis of a new peptide derived from Fasciola gigantica cathepsin L1 with potential application in serodiagnosis of fascioliasis.
Fascioliasis
Immunodiagnosis of Fasciola hepatica infection (fascioliasis) in a human population in the Bolivian Altiplano using purified cathepsin L cysteine proteinase.
Fascioliasis
Potent epitopes derived from Fasciola gigantica cathepsin L1 in peptide-based immunoassay for the serodiagnosis of human fascioliasis.
Fascioliasis
Serodiagnosis of human fascioliasis by a cystatin capture enzyme-linked immunosorbent assay with recombinant Fasciola gigantica cathepsin L antigen.
Fascioliasis
Short report: Immunodiagnosis of human fascioliasis using recombinant Fasciola hepatica cathepsin L1 cysteine proteinase.
Glioma
Viability screen on pediatric low grade glioma cell lines unveils a novel anti-cancer drug of the steroid biosynthesis inhibitor family.
Infections
Cathepsin L1 mimotopes with adjuvant Quil A induces a Th1/Th2 immune response and confers significant protection against Fasciola hepatica infection in goats.
Infections
Differences in the antibody response to adult Fasciola hepatica excretory/secretory products in experimentally and naturally infected cattle and sheep.
Infections
Early and Late Peritoneal and Hepatic Changes in Goats Immunized with Recombinant Cathepsin L1 and Infected with Fasciola hepatica.
Infections
Expression of free radicals by peritoneal cells of sheep during the early stages of Fasciola hepatica infection.
Infections
Humoral immune response in goats immunised with cathepsin L1, peroxiredoxin and Sm14 antigen and experimentally challenged with Fasciola hepatica.
Infections
Identification of protective peptides of Fasciola hepatica-derived cathepsin L1 (FhCL1) in vaccinated sheep by a linear B-cell epitope mapping approach.
Infections
Identification of reference genes for real-time PCR cytokine gene expression studies in sheep experimentally infected with Fasciola hepatica.
Infections
Immunodiagnosis of Fasciola gigantica Infection Using Monoclonal Antibody-Based Sandwich ELISA and Immunochromatographic Assay for Detection of Circulating Cathepsin L1 Protease.
Infections
Protection of cattle against a natural infection of Fasciola hepatica by vaccination with recombinant cathepsin L1 (rFhCL1).
Infections
Th1/Th2 balance in the liver and hepatic lymph nodes of vaccinated and unvaccinated sheep during acute stages of infection with Fasciola hepatica.
Infections
The combined recombinant cathepsin L1H and cathepsin B3 vaccine against Fasciola gigantica infection.
Insulin Resistance
Cathepsin gene expression in abdominal subcutaneous adipose tissue of obese/overweight humans.
Lymphoma
[Mechanism of renal injury and apoptosis in rats with nephrotic syndrome induced by mercury].
Neoplasm Metastasis
The lnc-CTSLP8 upregulates CTSL1 as a competitive endogenous RNA and promotes ovarian cancer metastasis.
Neoplasms
Biomarkers of blood cadmium and incidence of cardiovascular events in non-smokers: results from a population-based proteomics study.
Neoplasms
Candidate serological biomarkers for cancer identified from the secretomes of 23 cancer cell lines and the human protein atlas.
Neoplasms
The Biomarkers NT-proBNP and CA-125 are Elevated in Patients with Idiopathic Atrial Fibrillation.
Neoplasms
Using multimarker screening to identify biomarkers associated with cardiovascular death in patients with atrial fibrillation.
Ovarian Neoplasms
The lnc-CTSLP8 upregulates CTSL1 as a competitive endogenous RNA and promotes ovarian cancer metastasis.
Schistosomiasis
Computer-Aided Drug Design for the Identification of Novel Antischistosomal Compounds.
Starvation
Molecular cloning and mRNA expression of the liver-specific cathepsin L1 gene of the olive flounder, Paralichthys olivaceus.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0093
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0204
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0656
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0147
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0054
H-Leu-Val-Tyr-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0653
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0385
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0347
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.0436
t-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.0347
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0436
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.1069
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.38
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
2.75
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
4.35
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
8.16
benzyloxycarbonyl-L-Phel-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
19.21
benzyloxycarbonyl-L-Phel-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
24.18
benzyloxycarbonyl-L-Phel-L-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
48.41
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
137
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
191.2
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
0.0036
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.0044
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
0.003
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.0147
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.0242
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5