Information on EC 3.4.22.B60 - cathepsin L2

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.22.B60
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
cathepsin L2
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preference for Arg in the P1 position, Pro is accepted in the P2 position
show the reaction diagram
-
-
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
cathepsin L2
-
-
?
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
cathepsin L2
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
cathepsin L2
-
-
?
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
FhCL2
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
FhCL2
-
-
?
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Pro-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
FhCL2
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
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
show the reaction diagram
-
cathepsin L2
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Boc-AGPR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Boc-VLK-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Boc-VPR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
Collagen type I + H2O
?
show the reaction diagram
-
cathepsin L2 cleaves collagen type I at 43 sites within the alpha1 chain and 26 sites within the alpha2 chain
-
-
?
collagen type II + H2O
?
show the reaction diagram
-
cathepsin L2 exhibits collagenase activity by cleaving at multiple sites within the alpha1 and alpha2 triple helix regions (Col domains)
-
-
?
Fibrin + H2O
?
show the reaction diagram
-
cathepsin L proteinase cleaves fibrinogen and produces a novel type of fibrin clot
-
-
?
human IgG + H2O
?
show the reaction diagram
-
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
show the reaction diagram
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
procathepsin L2 + H2O
?
show the reaction diagram
-
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
show the reaction diagram
cathepsin L2
-
-
?
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
cathepsin L2
-
-
?
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tert-butoxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
FhCL2
-
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
cathepsin L2
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
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
show the reaction diagram
cathepsin L2
-
-
?
tosyl-Gly-Phe-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
cathepsin L2
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methyl coumarin
show the reaction diagram
-
cathepsin L2
-
-
?
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-GPK-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
tosyl-GPR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Z-Gly-Pro + Gly-Gly + L-Pro-L-Ala
show the reaction diagram
-
-
-
-
?
Z-Gly-Pro-Leu-Gly-Pro + H2O
Z-Gly-Pro + L-Leu + Gly + L-Pro
show the reaction diagram
-
-
-
-
?
Z-Leu-Arg-NHMe + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Phe-Arg-NHMe + H2O
?
show the reaction diagram
-
-
-
-
?
Z-VVR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Boc-AGPR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Boc-VLK-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Boc-VPR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen type I + H2O
?
show the reaction diagram
-
cathepsin L2 cleaves collagen type I at 43 sites within the alpha1 chain and 26 sites within the alpha2 chain
-
-
?
collagen type II + H2O
?
show the reaction diagram
-
cathepsin L2 exhibits collagenase activity by cleaving at multiple sites within the alpha1 and alpha2 triple helix regions (Col domains)
-
-
?
tosyl-GPK-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
tosyl-GPR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Z-Gly-Pro + Gly-Gly + L-Pro-L-Ala
show the reaction diagram
-
-
-
-
?
Z-Gly-Pro-Leu-Gly-Pro + H2O
Z-Gly-Pro + L-Leu + Gly + L-Pro
show the reaction diagram
-
-
-
-
?
Z-Leu-Arg-NHMe + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Phe-Arg-NHMe + H2O
?
show the reaction diagram
-
-
-
-
?
Z-VVR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzyloxycarbonyl-Phe-Ala-diazomethyl ketone
-
FheCL2
cathepsin K inhibitor II
-
Tetranitromethane
cathepsin L2 is completely inactivated by 4 mM tetranitromethane, cathepsin L1 is not inactivated
Z-Phe-Ala-CHN2
-
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
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
0.0014
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
0.0036 - 0.0044
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
0.004
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide
pH 7.0, 37°C, cathepsin L2
0.0155 - 0.0399
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
0.0752 - 0.084
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
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
0.0337
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
-
FheCL2
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
0.0327
tosyl-Gly-Phe-Arg-7-amido-4-methylcoumarin
-
FhCatL2
0.0153 - 0.0171
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
0.0483
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
FhCatL2
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide
Fasciola hepatica
P80342
pH 7.0, 37°C, cathepsin L2
0.09
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide
Fasciola hepatica
P80342
pH 7.0, 37°C, cathepsin L2
0.02
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide
Fasciola hepatica
P80342
pH 7.0, 37°C, cathepsin L2
1.62
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
Fasciola hepatica
-
FheCL2
1.7
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide
Fasciola hepatica
-
FheCL2
2.64
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
Fasciola hepatica
-
FheCL2
1.6 - 3.2
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
0.56
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide
Fasciola hepatica
P80342
pH 7.0, 37°C, cathepsin L2
0.4 - 50
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
1.9 - 2.6
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
0.55
Boc-AGPR-7-amido-4-methylcoumarin
Fasciola hepatica
-
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
Fasciola hepatica
-
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
Fasciola hepatica
-
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
Fasciola hepatica
P80342
pH 7.0, 37°C, cathepsin L2
0.14
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide
Fasciola hepatica
P80342
pH 7.0, 37°C, cathepsin L2
0.08
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide
Fasciola hepatica
P80342
pH 7.0, 37°C, cathepsin L2
2.48
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
Fasciola hepatica
-
FheCL2
3.75
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide
Fasciola hepatica
P80342
pH 7.0, 37°C, cathepsin L2
1.19
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide
Fasciola hepatica
P80342
pH 7.0, 37°C, cathepsin L2
26.3
tosyl-Gly-Phe-Arg-7-amido-4-methylcoumarin
Fasciola hepatica
-
FhCatL2
1.17 - 1.93
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
440
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
Fasciola hepatica
-
FhCatL2
1.37
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide
Fasciola hepatica
P80342
pH 7.0, 37°C, cathepsin L2
0.18
tosyl-GPK-7-amido-4-methylcoumarin
Fasciola hepatica
-
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
Fasciola hepatica
-
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
Fasciola hepatica
-
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
Fasciola hepatica
-
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
Fasciola hepatica
-
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 hide
LITERATURE
IMAGE
58.03
Boc-AGPR-7-amido-4-methylcoumarin
Fasciola hepatica
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
19614
30.71
Boc-VLK-7-amido-4-methylcoumarin
Fasciola hepatica
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
19609
20.19
Boc-VPR-7-amido-4-methylcoumarin
Fasciola hepatica
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
19613
13.75
tosyl-GPK-7-amido-4-methylcoumarin
Fasciola hepatica
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
19612
18.56
tosyl-GPR-7-amido-4-methylcoumarin
Fasciola hepatica
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
19611
444.1
Z-Leu-Arg-NHMe
Fasciola hepatica
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
19607
11.09
Z-Phe-Arg-NHMe
Fasciola hepatica
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
19608
9.238
Z-VVR-7-amido-4-methylcoumarin
Fasciola hepatica
-
in 100 mM sodium phosphate buffer (pH 6.0) containing 1 mM dithiothreitol and 1 mM EDTA, at 37°C
19610
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00167
benzyloxycarbonyl-Phe-Ala-diazomethyl ketone
-
FheCL2
0.00000046 - 0.000023
cathepsin K inhibitor II
-
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 hide
LITERATURE
16.2
-
substrate: tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
liver migrating juvenile and mature bile duct parasites
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
secreted by adult flukes
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24500
-
x * 24500, mature enzyme, SDS-PAGE
26000
-
x * 26000, mature enzyme, SDS-PAGE
29500
x * 29500, SDS-Page
37000
-
x * 37000, proenzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
10% v/v, no inactivation of cathepsin L1 or cathepsin L2
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
combined purification of cathepsin L1 and cathepsin L2
-
Ni-NTA-agarose column chromatography
-
recombinant zymogen of cathepsin L2
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia angusta
-
expression in Saccharomyces cerevisiae
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recombinantly expressed in Pichia pastoris
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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screening of cathepsin L1/cathepsin L2 mimotopes and use of an M13 phage random 12-mers peptide library to evaluate their immunogenicity in sheep
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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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