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benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-AGPR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-VLK-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-VPR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
FhCL3 demonstrates only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain
-
-
?
human immumglobulin G + H2O
?
partial cleavage
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + interleukin-1beta propeptide
-
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
?
-
restricted substrate specificity with 70fold preference for tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin over benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin and benzyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
tosyl-GPK-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
tosyl-GPR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
type II collagen + H2O
?
-
cathepsin L3 exhibits collagenase activity by cleaving at multiple sites within the alpha1 and alpha2 triple helix regions (Col domains)
-
-
?
Z-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Z-Gly-Pro + Gly + Gly + L-Pro-L-Ala
-
-
-
-
?
Z-Gly-Pro-Leu-Gly-Pro + H2O
Z-Gly-Pro + L-Leu + Gly + L-Pro
-
-
-
-
?
Z-Leu-Arg-NHMe + H2O
?
-
-
-
-
?
Z-Phe-Arg-NHMe + H2O
?
-
-
-
-
?
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
Z-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-VVR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
additional information
?
-
Collagen + H2O
?
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
FhCL3 efficiently cleaves type I collagen over different pH and temperature conditions
-
-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + 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
-
-
-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
70fold preference for tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin over typical cathepsin substrates with hydrophobic or aliphatic residues in the S2 position
-
-
?
Type I collagen + H2O
?
-
CL3 exhibits the ability to degrade type I collagen efficiently at pH 5.5, 6.3 and 7.0
-
-
?
Type I collagen + H2O
?
-
cathepsin CL3 cleaves at 24 sites within the alpha1 chain and 24 sites within the alpha2 chain of collagen type I
-
-
?
Type I collagen + H2O
?
-
the enzyme with collagenolytic activity favours Pro at P2 and shows a distinctive specificity at the S3 pocket, accommodating preferentially the small Gly residue
-
-
?
additional information
?
-
-
cathepsin L3 is a main component of the juvenile secretory products and may participate in the tissue invasion process
-
-
?
additional information
?
-
-
no cleavage of immunoglobulin
-
-
?
additional information
?
-
-
tosyl-Gly-Pro-7-amino-4-methylcoumarin is the preferred substrate in newly excysted juveniles, it is suggested that this activity may be due to cathepsin L3
-
-
?
additional information
?
-
-
does not cleave immunoglobulin
-
-
?
additional information
?
-
-
cathepsin L3 has preference for proline in the selective P2 position
-
-
?
additional information
?
-
-
the cathepsin L zymogen is autocatalytically activated and processed to mature enzyme by incubation for 2 h at 37°C in 0.1 M sodium citrate buffer (pH 5.0) containing 2 mM dithiothreitol and 2.5 mM EDTA
-
-
?
additional information
?
-
-
cathepsin L3 readily cleaves substrates with Pro in the P2 position and peptide substrates mimicking the repeating Gly-Pro-Xaa motifs that occur within the primary sequence of collagen
-
-
?
additional information
?
-
no activity with fibrinogen or fibrin
-
-
?
additional information
?
-
-
no activity with fibrinogen or fibrin
-
-
?
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(2E)-2-[(2,3-dimethyl-1,4-dioxidoquinoxalin-6-yl)methylidene]-N-(2-phenylethyl)hydrazinecarboxamide
32% inhibiton at 0.01 mM
(2E)-2-[(2-amino-3-cyano-1,4-dioxidoquinoxalin-6-yl)methylidene]-N-(2-phenylethyl)hydrazinecarboxamide
61% inhibiton at 0.01 mM
(2E)-2-[(2-amino-3-cyano-1,4-dioxidoquinoxalin-6-yl)methylidene]-N-(prop-2-en-1-yl)hydrazinecarbothioamide
39% inhibiton at 0.01 mM
(2E)-2-[(2-amino-3-cyano-1,4-dioxidoquinoxalin-6-yl)methylidene]-N-butylhydrazinecarboxamide
27% inhibiton at 0.01 mM
(2E)-N'-(2-[(naphthalen-1-ylmethyl)sulfanyl]acetyl)-3-phenylprop-2-enehydrazide
-
(2Z)-2-[(2E)-[(2,3-dimethyl-1,4-dioxidoquinoxalin-6-yl)methylidene]hydrazinylidene]-3-(prop-2-en-1-yl)-1,3-thiazolidin-4-one
22% inhibiton at 0.01 mM
(6,7-difluoro-3-methyl-1,4-dioxidoquinoxalin-2-yl)(phenyl)methanone
17% inhibiton at 0.01 mM
2-([4-benzyl-5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl)-1-(1,2,3,4-tetrahydroquinolin-1-yl)ethan-1-one
-
2-methylquinoxaline 1,4-dioxide
8% inhibiton at 0.01 mM
3-amino-7-([ethyl[(2Z)-3-phenylprop-2-en-1-yl]amino]methyl)quinoxaline-2-carbonitrile 1,4-dioxide
45% inhibiton at 0.01 mM
3-methyl-N-phenyl-7-([4-[(2E)-3-phenylprop-2-en-1-yl]piperazin-1-yl]methyl)quinoxaline-2-carboxamide 1,4-dioxide
49% inhibiton at 0.01 mM
3-methyl-N-phenylquinoxaline-2-carboxamide 1,4-dioxide
40% inhibiton at 0.01 mM
4-(2,5-dimethyl-1H-pyrrol-1-yl)-N'-(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)benzohydrazide
-
4-[4-(benzyloxy)phenyl]-3-([(4-methylphenyl)methyl]sulfanyl)-4,5-dihydro-1H-1,2,4-triazol-5-one
-
6,7-dichloro-2-methyl-3-(phenylsulfanyl)quinoxaline 1,4-dioxide
22% inhibiton at 0.01 mM
6-[(E)-[(2Z)-[4-(4-chlorophenyl)-3-(prop-2-en-1-yl)-1,3-thiazol-2(3H)-ylidene]hydrazinylidene]methyl]-2,3-dimethylquinoxaline 1,4-dioxide
2% inhibiton at 0.01 mM
6-[(E)-[(2Z)-[4-oxo-3-(prop-2-en-1-yl)-1,3-thiazolidin-2-ylidene]hydrazinylidene]methyl]-N,3-diphenylquinoxaline-2-carboxamide 1,4-dioxide
81% inhibiton at 0.01 mM
7-[ethyl[(2E)-3-phenylprop-2-en-1-yl]amino]-3-methyl-N-phenylquinoxaline-2-carboxamide 1,4-dioxide
54% inhibiton at 0.01 mM
cathepsin K inhibitor II
-
i.e. Z-LNHNHCONHNHLF-Boc
ethyl 3-methyl-7-[(E)-[2-(prop-2-en-1-ylcarbamothioyl)hydrazinylidene]methyl]quinoxaline-2-carboxylate 1,4-dioxide
58% inhibiton at 0.01 mM
ethyl 3-methylquinoxaline-2-carboxylate 1,4-dioxide
5% inhibiton at 0.01 mM
ethyl 3-phenyl-7-([4-[(2E)-3-phenylprop-2-en-1-yl]piperazin-1-yl]methyl)quinoxaline-2-carboxylate 1,4-dioxide
61% inhibiton at 0.01 mM
ethyl 3-phenyl-7-[(E)-[2-(prop-2-en-1-ylcarbamothioyl)hydrazinylidene]methyl]quinoxaline-2-carboxylate 1,4-dioxide
86% inhibiton at 0.01 mM
ethyl 6,7-dichloro-3-phenylquinoxaline-2-carboxylate 1,4-dioxide
35% inhibiton at 0.01 mM
methyl (2E)-2-[(2,3-dimethyl-1,4-dioxidoquinoxalin-6-yl)methylidene]hydrazinecarboxylate
3% inhibiton at 0.01 mM
methyl (2E)-2-[(2-amino-3-cyano-1,4-dioxidoquinoxalin-6-yl)methylidene]hydrazinecarboxylate
27% inhibiton at 0.01 mM
N,3-diphenyl-6-[(E)-[2-(prop-2-en-1-ylcarbamothioyl)hydrazinylidene]methyl]quinoxaline-2-carboxamide 1,4-dioxide
79% inhibiton at 0.01 mM
N1-[3,5-bis(trifluoromethyl)phenyl]-N2-(1-ethynylcyclohexyl)benzene-1,2-dicarboxamide
-
[1,4-dioxido-3-(trifluoromethyl)quinoxalin-2-yl](phenyl)methanone
22% inhibiton at 0.01 mM
[6,7-difluoro-1,4-dioxido-3-(trifluoromethyl)quinoxalin-2-yl](phenyl)methanone
38% inhibiton at 0.01 mM
additional information
cathepsin L inhibitors with activity against the liver fluke identified from a focus library of quinoxaline 1,4-di-N-oxide derivatives, library screening, overview. Analysis of me-ligand interactions in silico by molecular docking and molecular dynamic (MD) simulations. The compounds readily kill newly excysted juveniles of Fasciola hepaticaa in vitro and have low cytotoxicityin a Hep-G2 cell line and bovine spermatozoa. No inhibition by quinoxaline-2-carbaldehyde 1,4-dioxide, 3-aminoquinoxaline-2-carbonitrile 1,4-dioxide, 3-amino-6,7-dichloroquinoxaline-2-carbonitrile 1,4-dioxide, and 3-methyl-N-phenyl-7-[(E)-[2-(prop-2-en-1-ylcarbamothioyl)hydrazinylidene]methyl]quinoxaline-2-carboxamide 1,4-dioxide
-
additional information
virtual inhibitor screening is carried out by docking inhibitors obtained from the MYBRIDGE-HitFinder database to FhCL3 and human cathepsin L substrate-binding sites. On the basis of dock-scores, five compounds are predicted as selective inhibitors of FhCL3, molecular dynamic simulations. The active site-binding compounds prevent substrate processing by competitive inhibition. Structure-based drug design strategy, overview. Calculation of inhibition kinetics and thermodynamics
-
additional information
-
virtual inhibitor screening is carried out by docking inhibitors obtained from the MYBRIDGE-HitFinder database to FhCL3 and human cathepsin L substrate-binding sites. On the basis of dock-scores, five compounds are predicted as selective inhibitors of FhCL3, molecular dynamic simulations. The active site-binding compounds prevent substrate processing by competitive inhibition. Structure-based drug design strategy, overview. Calculation of inhibition kinetics and thermodynamics
-
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0.02353
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
in 50 mM sodium phosphate, pH 6.5, 1 mM dithiothreitol, 1 mM EDTA, at 24°C
0.0157
benzyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
in 50 mM sodium phosphate, pH 6.5, 1 mM dithiothreitol, 1 mM EDTA, at 24°C
0.0235
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
0.0157
benzyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
-
0.0096
Boc-AGPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.00613
Boc-VLK-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0211
Boc-VPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0041
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
-
in 50 mM sodium phosphate, pH 6.5, 1 mM dithiothreitol, 1 mM EDTA, at 24°C
0.0041 - 0.0067
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
0.0098
tosyl-GPK-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0106
tosyl-GPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.048
Z-Leu-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.02005
Z-Phe-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0157 - 0.0448
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
0.0117
Z-VVR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0041
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
-
0.0041
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
0.0052
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
mutant enzyme W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
0.0067
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
mutant enzyme H61N/W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
0.0157
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
0.0287
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
-
mutant enzyme H61N/W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
0.0448
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
-
mutant enzyme W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
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0.39
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
in 50 mM sodium phosphate, pH 6.5, 1 mM dithiothreitol, 1 mM EDTA, at 24°C
0.33
benzyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
in 50 mM sodium phosphate, pH 6.5, 1 mM dithiothreitol, 1 mM EDTA, at 24°C
0.39
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
0.33
benzyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
-
0.58
Boc-AGPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.01
Boc-VLK-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.033
Boc-VPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
6
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
-
in 50 mM sodium phosphate, pH 6.5, 1 mM dithiothreitol, 1 mM EDTA, at 24°C
0.0053 - 6
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
0.15
tosyl-GPK-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
1.015
tosyl-GPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
1.2
Z-Leu-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.02
Z-Phe-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.03 - 0.33
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
0.043
Z-VVR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0053
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
mutant enzyme W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
0.0072
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
mutant enzyme H61N/W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
6
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
-
6
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
0.03
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
-
mutant enzyme H61N/W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
0.03
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
-
mutant enzyme W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
0.33
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
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16.78
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
in 50 mM sodium phosphate, pH 6.5, 1 mM dithiothreitol, 1 mM EDTA, at 24°C
20.76
benzyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
in 50 mM sodium phosphate, pH 6.5, 1 mM dithiothreitol, 1 mM EDTA, at 24°C
60.76
Boc-AGPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
1.748
Boc-VLK-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
1.564
Boc-VPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
1464
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
-
in 50 mM sodium phosphate, pH 6.5, 1 mM dithiothreitol, 1 mM EDTA, at 24°C
1.017 - 1464
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
36.42
tosyl-GPK-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
95.77
tosyl-GPR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
25
Z-Leu-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.9993
Z-Phe-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.59 - 20.76
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
3.697
Z-VVR-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
1.017
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
mutant enzyme W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
1.072
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
mutant enzyme H61N/W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
1464
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
0.59
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
-
mutant enzyme W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
1.037
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
-
mutant enzyme H61N/W67L, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
20.76
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, 1 mM dithiothreitol and 1 mM EDTA at 25°C
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physiological function
the dormant larvae of Fasciola hepatica express a specific cathepsin L protease, CL3, stored as an inactive zymogen that is rapidly secreted and activated following emergence from their cysts to become infective larvae
physiological function
-
the enzyme enables the parasite penetrate the intestinal wall
physiological function
although no direct anticoagulant effect of the peptidases is observed, cathepsin peptidases from Fasciola are able to degrade purified fibrinogen, with FhCL1 having the highest fibrinogenolytic activity. FhCL1 and FhCL2 also both efficiently degrade fibrin, but FhCL3 does not. FhCL1 has a larger fibrinogenolytic activity than FhCL2 and FhCL3 and is capable of degradation of the fibrinogen alpha-chain, beta-chain, and gamma-chain. FhCL2 andFhCL3 demonstrate only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain compared to FhCL1
physiological function
in the case of the helminth trematode Fasciola hepatica, the secretion of different cathepsin L cysteine peptidases (FhCL) is crucial for the parasite survival. Among these enzymes, cathepsin L3 (FhCL3) is expressed mainly in the juvenile or invasive stage. The ability of FhCL3 to digest collagen is critical for intestinal tissue invasion during juvenile larvae migration. FhCL3 induces a non-canonical inflammasome activation in dendritic cells (DCs) of C57BL/6 mice, leading to interleukin (IL)-1beta and IL-18 production without a previous microbial priming. This activation is depending on the cysteine protease activity of FhCL3 and the NLRP3 receptor, but independent of caspase activation. FhCL3 is internalized by DCs, promoting pro-IL-1beta cleavage to its mature and biologically active form IL-1beta, which is released to the extracellular environment. The FhCL3-induced NLRP3 inflammasome activation conditions DCs to promote a singular adaptive immune response, characterized by increased production of IFN-gamma and IL-13. Due to the poor colocalization of FhCL3 with endosomes or lysosomes, the mechanism of endocytosis could be different from that used by FhCL1. The lack of involvement of NF-kkappaB in FhCL3-induced DCs activation, suggests that other/s transcription factor might be involved in the synthesis of pro-IL-1beta
physiological function
schistosomal cathepsin peptidases are not able to cleave fibrinogen or fibrin, which is in line with the presence of other anticoagulant and fibrinolytic strategies adopted by schistosomes. This allows schistosomes to counteract fibrin formation at their surface, allowing blood-feeding and survival of the parasite within its host
additional information
homology modeling of FhCL3 using the three dimensional structure of proFhCL1 C25G, PDB ID 2O6X, as a template
additional information
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homology modeling of FhCL3 using the three dimensional structure of proFhCL1 C25G, PDB ID 2O6X, as a template
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Harmsen, M.M.; Cornelissen, J.B.; Buijs, H.E.; Boersma, W.J.; Jeurissen, S.H.; van Milligen, F.J.
Identification of a novel Fasciola hepatica cathepsin L protease containing protective epitopes within the propeptide
Int. J. Parasitol.
34
675-682
2004
Fasciola hepatica (Q9GRW4), Fasciola hepatica (Q9GRW6)
brenda
Tkalcevic, J.; Ashman, K.; Meeusen, E.
Fasciola hepatica: rapid identification of newly excysted juvenile proteins
Biochem. Biophys. Res. Commun.
213
169-174
1995
Fasciola hepatica (P80532)
brenda
Cancela, M.; Acosta, D.; Rinaldi, G.; Silva, E.; Duran, R.; Roche, L.; Zaha, A.; Carmona, C.; Tort, J.F.
A distinctive repertoire of cathepsins is expressed by juvenile invasive Fasciola hepatica
Biochimie
90
1461-1475
2008
Fasciola hepatica
brenda
Corvo, I.; Cancela, M.; Cappetta, M.; Pi-Denis, N.; Tort, J.F.; Roche, L.
The major cathepsin L secreted by the invasive juvenile Fasciola hepatica prefers proline in the S2 subsite and can cleave collagen
Mol. Biochem. Parasitol.
167
41-47
2009
Fasciola hepatica
brenda
Reszka, N.; Cornelissen, J.B.; Harmsen, M.M.; Bienkowska-Szewczyk, K.; de Bree, J.; Boersma, W.J.; Rijsewijk, F.A.
Fasciola hepatica procathepsin L3 protein expressed by a baculovirus recombinant can partly protect rats against fasciolosis
Vaccine
23
2987-2993
2005
Fasciola hepatica (Q9GRW6), Fasciola hepatica
brenda
Robinson, M.W.; Menon, R.; Donnelly, S.M.; Dalton, J.P.; Ranganathan, S.
An integrated transcriptomics and proteomics analysis of the secretome of the helminth pathogen Fasciola hepatica: proteins associated with invasion and infection of the mammalian host
Mol. Cell. Proteomics
8
1891-1907
2009
Fasciola hepatica (B3TM67), Fasciola hepatica (B3TM68)
brenda
Robinson, M.W.; Corvo, I.; Jones, P.M.; George, A.M.; Padula, M.P.; To, J.; Cancela, M.; Rinaldi, G.; Tort, J.F.; Roche, L.; Dalton, J.P.
Collagenolytic activities of the major secreted cathepsin L peptidases involved in the virulence of the helminth pathogen, Fasciola hepatica
PLoS Negl. Trop. Dis.
5
e1012
2011
Fasciola hepatica
brenda
Zawistowska-Deniziak, A.; Wasyl, K.; Norbury, L.J.; Wesolowska, A.; Bien, J.; Grodzik, M.; Wisniewski, M.; Baska, P.; Wedrychowicz, H.
Characterization and differential expression of cathepsin L3 alleles from Fasciola hepatica
Mol. Biochem. Parasitol.
190
27-37
2013
Fasciola hepatica (B9VXS1), Fasciola hepatica (B9VXS2), Fasciola hepatica
brenda
Corvo, I.; ODonoghue, A.J.; Pastro, L.; Pi-Denis, N.; Eroy-Reveles, A.; Roche, L.; McKerrow, J.H.; Dalton, J.P.; Craik, C.S.; Caffrey, C.R.; Tort, J.F.
Dissecting the active site of the collagenolytic cathepsin L3 protease of the invasive stage of Fasciola hepatica
PLoS Negl. Trop. Dis.
7
e2269
2013
Fasciola hepatica
brenda
Celias, D.P.; Corvo, I.; Silvane, L.; Tort, J.F.; Chiapello, L.S.; Fresno, M.; Arranz, A.; Motran, C.C.; Cervi, L.
Cathepsin L3 from Fasciola hepatica induces NLRP3 inflammasome alternative activation in murine dendritic cells
Front. Immunol.
10
552
2019
Fasciola hepatica (B3TM67), Fasciola hepatica
brenda
Mebius, M.M.; Op Heij, J.M.J.; Tielens, A.G.M.; de Groot, P.G.; Urbanus, R.T.; van Hellemond, J.J.
Fibrinogen and fibrin are novel substrates for Fasciola hepatica cathepsin L peptidases
Mol. Biochem. Parasitol.
221
10-13
2018
Fasciola hepatica (B3TM67), Fasciola hepatica, Schistosoma mansoni (B4XC67), Schistosoma mansoni
brenda
Ferraro, F.; Merlino, A.; Gil, J.; Cerecetto, H.; Corvo, I.; Cabrera, M.
Cathepsin L inhibitors with activity against the liver fluke identified from a focus library of quinoxaline 1,4-di-N-oxide derivatives
Molecules
24
2348
2019
Fasciola hepatica (B3TM67)
brenda
Hernandez Alvarez, L.; Naranjo Feliciano, D.; Hernandez Gonzalez, J.E.; de Oliveira Soares, R.O.; Barreto Gomes, D.E.; Pascutti, P.G.
Insights into the Interactions of Fasciola hepatica cathepsin L3 with a substrate and potential novel inhibitors through in silico approaches
PLoS Negl. Trop. Dis.
9
e0003759
2015
Fasciola hepatica (Q9GRW6), Fasciola hepatica
brenda