3.4.22.B60: cathepsin L2
This is an abbreviated version!
For detailed information about cathepsin L2, go to the full flat file.
Word Map on EC 3.4.22.B60
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3.4.22.B60
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fasciola
-
hepatica
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proteinases
-
fluke
-
helminth
-
schistosome
-
trematode
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l-like
-
excysted
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collagenolytic
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diagnostics
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agriculture
- 3.4.22.B60
- fasciola
- hepatica
- proteinases
- fluke
-
helminth
-
schistosome
-
trematode
-
l-like
-
excysted
-
collagenolytic
- diagnostics
- agriculture
Reaction
preference for Arg in the P1 position, Pro is accepted in the P2 position =
Synonyms
cathepsin L2, cathepsin L2 protease, CatL2, CL2, FhCatL2, FhCL2, FhpCL2
ECTree
3.4.22.B60 cathepsin L2Advanced search results
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results (Substrates Products
Substrates Products on EC 3.4.22.B60 - cathepsin L2
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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
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-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
-
-
?
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-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tert-butoxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
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
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
FhCL2
-
-
?
additional information
?
-
cathepsin L1 and cathepsin L2 proteinases may be the prime mechanism by which the parasite penetrates tissue
-
-
?
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 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
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-
?
additional information
?
-
-
S2 subsite preferences are aliphatic over aromatic, L-proline. The enzyme has a preference for leucine over phenylalanine at the P2 position
-
-
?
