3.4.22.B62: cathepsin L3
This is an abbreviated version!
For detailed information about cathepsin L3, go to the full flat file.
Word Map on EC 3.4.22.B62
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3.4.22.B62
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cathepsins
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fasciola
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hepatica
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worm
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schistosoma
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fluke
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peptidases
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schistosomiasis
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mansoni
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adjuvant-free
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japonicum
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samarium
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fasciolosis
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collagenolytic
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drug development
- 3.4.22.B62
- cathepsins
- fasciola
- hepatica
-
worm
- schistosoma
- fluke
- peptidases
- schistosomiasis
- mansoni
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adjuvant-free
- japonicum
- samarium
-
fasciolosis
-
collagenolytic
- drug development
Reaction
70fold preference for tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin over typical cathepsin substrates with hydrophobic or aliphatic residues in the S2 position. Efficiently cleaves type I collagen over different pH and temperature conditions =
Synonyms
cathepsin L clade 3, cathepsin L3, CL3, CL3-1, CL3-2, FhCL3, FheCL3, NEJ protein 8, newly excysted juvenile protein 8, SmCL3
ECTree
3.4.22.B62 cathepsin L3Advanced search results
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results (Substrates Products
Substrates Products on EC 3.4.22.B62 - cathepsin L3
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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
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
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-
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?
benzyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
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-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
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-
-
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?
benzyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
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-
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?
Fibrinogen + H2O
?
FhCL3 demonstrates only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain
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-
?
pro-interleukin-1beta + H2O
interleukin-1beta + interleukin-1beta propeptide
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-
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?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
?
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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
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-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
type II collagen + H2O
?
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cathepsin L3 exhibits collagenase activity by cleaving at multiple sites within the alpha1 and alpha2 triple helix regions (Col domains)
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?
Z-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Z-Gly-Pro + Gly + Gly + L-Pro-L-Ala
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-
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?
Z-Val-Leu-Lys-7-amido-4-methylcoumarin
Z-Val-Leu-Lys + 7-amino-4-methylcoumarin
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-
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?
Collagen + H2O
?
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FhCL3 efficiently cleaves type I collagen over different pH and temperature conditions
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-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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-
-
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?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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-
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?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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70fold preference for tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin over typical cathepsin substrates with hydrophobic or aliphatic residues in the S2 position
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-
?
Type I collagen + H2O
?
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CL3 exhibits the ability to degrade type I collagen efficiently at pH 5.5, 6.3 and 7.0
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-
?
Type I collagen + H2O
?
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cathepsin CL3 cleaves at 24 sites within the alpha1 chain and 24 sites within the alpha2 chain of collagen type I
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?
Type I collagen + H2O
?
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the enzyme with collagenolytic activity favours Pro at P2 and shows a distinctive specificity at the S3 pocket, accommodating preferentially the small Gly residue
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?
additional information
?
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cathepsin L3 is a main component of the juvenile secretory products and may participate in the tissue invasion process
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?
additional information
?
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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
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?
additional information
?
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cathepsin L3 has preference for proline in the selective P2 position
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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no activity with fibrinogen or fibrin
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?
