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Information on EC 3.4.22.B60 - cathepsin L2 and Organism(s) Fasciola hepatica and UniProt Accession Q24940
for references in articles please use BRENDA:EC3.4.22.B60preliminary BRENDA-supplied EC number
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3.4.22.B60 cathepsin L2Specify your search results
Word Map
- 3.4.22.B60
- fasciola
- hepatica
- proteinases
- fluke
-
helminth
-
schistosome
-
trematode
-
l-like
-
excysted
-
collagenolytic
- diagnostics
- agriculture
The taxonomic range for the selected organisms is: Fasciola hepatica
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cathepsin l2, fhcl2, fhcatl2, cathepsin l2 protease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cathepsin L2
FhCL2
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
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Pro-L-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tert-butoxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
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
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methyl coumarin
-
cathepsin L2
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Collagen type I + H2O
?
-
cathepsin L2 cleaves collagen type I at 43 sites within the alpha1 chain and 26 sites within the alpha2 chain
-
-
?
collagen type II + H2O
?
-
cathepsin L2 exhibits collagenase activity by cleaving at multiple sites within the alpha1 and alpha2 triple helix regions (Col domains)
-
-
?
Fibrinogen + H2O
?
FhCL2 demonstrates only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain
-
-
?
human IgG + H2O
?
-
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-4-methylcoumarinyl-7-amide + H2O
Leu-Val-Tyr + 7-amino-4-methylcoumarin
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
procathepsin L2 + H2O
?
-
procathepsin L2 autocatalytically processes and activates to its mature enzyme (FheCL2). FheCL2, which, unlike FheCL1, can readily accept proline in the S2 subsite of its active site, can trans-process the double variant FheproCL1Pro-12/Gly26 by cleavage at the Pro-12-Ser-11-/-His-10 sequence
-
-
?
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide + H2O
succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
cathepsin L2
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
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 L2
-
-
?
tosyl-Gly-Phe-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Phe-Arg + 7-amino-4-methylcoumarin
-
cathepsin L2
-
-
?
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-methyl coumarin
-
cathepsin L2
-
-
?
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
-
-
?
Z-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Z-Gly-Pro + Gly-Gly + L-Pro-L-Ala
-
-
-
-
?
Collagen + H2O
?
FhCL2 cleaves substrates with a bulky proline in the P2 position as the native collagen, which contains a repeat motif of Gly-Pro-Xaa (in which Xaa is any amino acid). By contrast these substrates are poorly cleaved by FhCL1 and not at all by human cathepsin L
-
-
?
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
-
-
?
Fibrin + H2O
?
-
cathepsin L proteinase cleaves fibrinogen and produces a novel type of fibrin clot
-
-
?
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
-
-
?
additional information
?
-
FheCL1 and FheCL2 exhibit similar preferences for amino acids at P1. Both enzymes have a clear preference for Arg at P1 position, but other residues accommodate in this position include Lys, Glu, Thr, and Met. These are all cleaved at similar relative rates to that observed for human cathepsin L and cathepsin K. FheCL1 and FheCL2 are similar to cathepsin K with regard to their preference for a P2 position Leu over Phe (human cathepsin L has a preference for P2 position 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
?
-
-
FheCL1 and FheCL2 exhibit similar preferences for amino acids at P1. Both enzymes have a clear preference for Arg at P1 position, but other residues accommodate in this position include Lys, Glu, Thr, and Met. These are all cleaved at similar relative rates to that observed for human cathepsin L and cathepsin K. FheCL1 and FheCL2 are similar to cathepsin K with regard to their preference for a P2 position Leu over Phe (human cathepsin L has a preference for P2 position 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
?
-
cathepsin L1 and cathepsin L2 proteinases may be the prime mechanism by which the parasite penetrates tissue
-
-
?
additional information
?
-
-
cathepsin L2 readily cleaves substrates with Pro in the P2 position and peptide substrates mimicking the repeating Gly-Pro-Xaa motifs
-
-
?
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
?
-
S2 subsite preferences are aliphatic over aromatic, L-proline. The enzyme has a preference for leucine over phenylalanine at the P2 position
-
-
?
additional information
?
-
-
S2 subsite preferences are aliphatic over aromatic, L-proline. The enzyme has a preference for leucine over phenylalanine at the P2 position
-
-
?
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
Collagen type I + H2O
?
-
cathepsin L2 cleaves collagen type I at 43 sites within the alpha1 chain and 26 sites within the alpha2 chain
-
-
?
collagen type II + H2O
?
-
cathepsin L2 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
-
-
-
-
?
additional information
?
-
-
cathepsin L2 readily cleaves substrates with Pro in the P2 position and peptide substrates mimicking the repeating Gly-Pro-Xaa motifs
-
-
?
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tetranitromethane
cathepsin L2 is completely inactivated by 4 mM tetranitromethane, cathepsin L1 is not inactivated
additional information
-
fibrin clot formation by cathepsin L is not inhibited by the thrombin inhibitor hirudin or by the anti-polymerant H-Gly-Pro-Arg-Pro-OH
-
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 FhCL2
-
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 FhCL2
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0014
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
FheCL2
0.04
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide
FheCL2
0.084
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
FheCL2
0.0337
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
FheCL2
0.0012
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0141
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0091
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.004
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0094
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
0.0022
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
0.01139
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
0.0038
Leu-Val-Tyr-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0412
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0232
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0073
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0248
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0171
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0355
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0129
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
0.0139
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
0.00213
Z-Leu-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.0078
Z-Phe-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.00153
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
0.0036
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
0.016
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.0399
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
0.0752
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.084
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.62
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
FheCL2
2.64
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
FheCL2
2.48
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
FheCL2
0.06
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.09
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.02
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.56
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.55
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
0.07
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
0.23
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
0.21
Leu-Val-Tyr-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.14
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.08
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
3.75
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
1.19
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
1.93
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
1.37
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.18
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
0.26
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
0.95
Z-Leu-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.09
Z-Phe-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.014
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
58.03
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
30.71
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
20.19
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
13.75
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
18.56
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
444.1
Z-Leu-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
11.09
Z-Phe-Arg-NHMe
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
9.238
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000046
cathepsin K inhibitor II
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
0.00000532
Z-Phe-Ala-CHN2
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
adult flukes produce three different clades of cathepsin Ls: FhCL1, FhCL2, and FhCL5
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 degraded 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 and FhCL3 demonstrate only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain compared to FhCL1
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
FhCL2 is expressed as 37000 Da zymogen that autocatalytically processes at pH 4.5 to produce a 24500 Da mature enzyme
proteolytic modification
proteolytic modification
-
procathepsin L2 autocatalytically processes and activates to its mature enzyme (FheCL2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
screening of cathepsin L1/cathepsin L2 mimotopes and use of an M13 phage random 12-mers peptide library to evaluate their immunogenicity in sheep
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant solubilized and refolded His-tagged enzyme from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene FhpCL2, DNA and amino acid sequence determination and analysis, sequence comparisons of rFhpCLs, recombinant expression of His-tagged enzyme in Escherichia coli
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli inclusion bodies, solubilization by 8 M urea, followed by dilution, dialysis, and ultrafiltration
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
screening of cathepsin L1/cathepsin L2 mimotopes and use of an M13 phage random 12-mers peptide library to evaluate their immunogenicity in sheep. Immunization of sheep with clones showing positive reactivity to rabbit cathepsin L1/L2 antiserum results in decrease in worm burdens after challenge. A significant reduction in worm size and burden is observed for those sheep immunized with clone 1. Animals receiving clone 20, show a significant reduction in egg output. Immunization induces a reduction of egg viability ranging from 58% to 82%. Vaccinated animals produce clone-specific antibodies which are boosted after challenge with metacercariae of Fasciola hepatica
diagnostics
analysis of the diagnostic values of the three different clades of cathepsin Ls, FhCL1, FhCL2, and FhCL5, from adult flukes in an ELISA, test of sera from sheep and cattle naturally infected with Fasciola hepatica, assessment of cross-reactive antibodies, overview. For sheep sera, the sensitivity is 100% for the three rFhpCLs, while for cattle sera, the highest sensitivity is obtained using rFhpCL2 (97%), being equal for both rFhpCL1 and rFhpCL5 (87.9%), after adjusting cut-offs for maximum specificity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dowd, A.J.; Smith, A.M.; McGonigle, S.; Dalton, J.P.
Purification and characterization of a second cathepsin L proteinase secreted by parasitic trematode Fasciola hepatica
Eur. J. Biochem.
223
91-98
1994
Fasciola hepatica (P80342)
Stack, C.M.; Donnelly, S.; Lowther, J.; Xu, W.; Collins, P.R.; Brinen, L.S.; Dalton, J.P.
The major secreted cathepsin L1 protease of the liver fluke, Fasciola hepatica: a Leu-12 to Pro-12 replacement in the nonconserved C-terminal region of the prosegment prevents complete enzyme autoactivation and allows definition of the molecular events in
J. Biol. Chem.
282
16532-16543
2007
Fasciola hepatica
Stack, C.M.; Caffrey, C.R.; Donnelly, S.M.; Seshaadri, A.; Lowther, J.; Tort, J.F.; Collins, P.R.; Robinson, M.W.; Xu, W.; McKerrow, J.H.; Craik, C.S.; Geiger, S.R.; Marion, R.; Brinen, L.S.; Dalton, J.P.
Structural and functional relationships in the virulence-associated cathepsin L proteases of the parasitic liver fluke, Fasciola hepatica
J. Biol. Chem.
283
9896-9908
2008
Fasciola hepatica (Q24940), Fasciola hepatica
Dowd, A.J.; McGonigle, S.; Dalton, J.P.
Fasciola hepatica cathepsin L proteinase cleaves fibrinogen and produces a novel type of fibrin clot
Eur. J. Biochem.
232
241-246
1995
Fasciola hepatica
Berasain, P.; Carmona, C.; Frangione, B.; Dalton, J.P.; Goni, F.
Fasciola hepatica: parasite-secreted proteinases degrade all human IgG subclasses: determination of the specific cleavage sites and identification of the immunoglobulin fragments produced
Exp. Parasitol.
94
99-110
2000
Fasciola hepatica
Smooker, P.M.; Whisstock, J.C.; Irving, J.A.
Siyaguna, S.; Spithill, T.W.: Pike, R.N.: A single amino acid substitution affects substrate specificity in cysteine proteinases from Fasciola hepatica
Protein Sci.
9
2567-2572
2000
Fasciola hepatica
Robinson, M.W.; Dalton, J.P.; Donnelly, S.
Helminth pathogen cathepsin proteases
Trends Biochem. Sci.
33
601-608
2008
Fasciola hepatica (Q24940)
Robinson, M.W.; Tort, J.F.; Lowther, J.; Donnelly, S.M.; Wong, E.; Xu, W.; Stack, C.M.; Padula, M.; Herbert, B.; Dalton, J.P.
Proteomics and phylogenetic analysis of the cathepsin L protease family of the helminth pathogen Fasciola hepatica: expansion of a repertoire of virulence-associated factors
Mol. Cell. Proteomics
7
1111-1123
2008
Fasciola hepatica (Q7JNQ8)
Villa-Mancera, A.; Quiroz-Romero, H.; Correa, D.; Ibarra, F.; Reyes-Perez, M.; Reyes-Vivas, H.; Lopez-Velazquez, G.; Gazarian, K.; Gazarian, T.; Alonso, R.A.
Induction of immunity in sheep to Fasciola hepatica with mimotopes of cathepsin L selected from a phage display library
Parasitology
135
1437-1445
2008
Fasciola hepatica
Norbury, L.J.; Beckham, S.; Pike, R.N.; Grams, R.; Spithill, T.W.; Fecondo, J.V.; Smooker, P.M.
Adult and juvenile Fasciola cathepsin L proteases: different enzymes for different roles
Biochimie
93
604-611
2011
Fasciola hepatica (Q7JNQ8), Fasciola hepatica
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
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 (A0A220T1Z2), Fasciola hepatica
Martinez-Sernandez, V.; Perteguer, M.J.; Hernandez-Gonzalez, A.; Mezo, M.; Gonzalez-Warleta, M.; Orbegozo-Medina, R.A.; Romaris, F.; Paniagua, E.; Garate, T.; Ubeira, F.M.
Comparison of recombinant cathepsins L1, L2, and L5 as ELISA targets for serodiagnosis of bovine and ovine fascioliasis
Parasitol. Res.
117
1521-1534
2018
Fasciola hepatica (A0A220T1Z2), Fasciola hepatica
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