3.4.22.B49: cathepsin L1
This is an abbreviated version!
For detailed information about cathepsin L1, go to the full flat file.
Word Map on EC 3.4.22.B49
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3.4.22.B49
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cathepsins
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fasciola
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hepatica
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fluke
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fasciolosis
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metacercariae
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helminth
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gigantica
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medicine
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excysted
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trematode
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excretory-secretory
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immunodiagnosis
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agriculture
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mimotopes
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diagnostics
- 3.4.22.B49
- cathepsins
- fasciola
- hepatica
- fluke
-
fasciolosis
-
metacercariae
-
helminth
- gigantica
- medicine
-
excysted
-
trematode
-
excretory-secretory
-
immunodiagnosis
- agriculture
-
mimotopes
- diagnostics
Reaction
clear preference for Arg at P1 position (Lys, Glu, Thr, and Met are less efficient). FheCL1 shows distinct preference for hydrophobic amino acids in the P2, Leu is favored. Cathepsin L1 can accommodate Pro in the P2 position, but less efficiently than cathepsin L2. FheCL1 produces clear degradation fragments from collagen =
Synonyms
cat-L1H, cathepsin L1, cathepsin L1 cysteine protease, cathepsin L1 protease, cathepsin L1 proteinase, cathepsin L1g, cathepsin L1H, CatL1, CgCTSL1, CGI_10027418, CL1, CPFhW, CTSL1, cysteine proteinase 3, Da-CTSL1, FgCatL1H, FhCL1, FheCL1, FhpCL1
ECTree
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Inhibitors
Inhibitors on EC 3.4.22.B49 - cathepsin L1
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N-benzyloxycarbonyl-FY(tert-butyl)-diazomethylketone
40.6% inhibition at 0.05 mM
N-benzyloxycarbonylphenylalanyl-t-butyl-tryrosyl diazomethylketone
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40.6% inhibition at 0.05 mM
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complete inhibition at 50 nM at a molar ratio of enzyme to inhibitor of 17:1; inhibits enzyme activity almost completely at a molar ratio of enzyme to inhibitor of 17:1
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i.e. L-trans-epoxysuccinyl-leucyamido(4-guanidino) butane, 26.6% inhibition at 0.05 mM
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cathepsin L2 is completely inactivated by 4 mM tetranitromethane, cathepsin L1 is not inactivated
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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 FhCL1
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additional information
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the enzyme's fibrinolytic activity is inhibited by plasma. Addition of GSH to plasma cannot counteract the inhibitory effect of plasma components for FhCL1
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additional information
inhibitory interactions of human family 1 and 2 cystatins with cathepsin L1 are predicted and their stability and viability are verified through protein docking and comparative molecular dynamics, overview. The key amino acid residues surfaced via interaction energy, hydrogen bonding and solvent accessible surface area analysis for each cystatin-cathepsin L1 complex influence the mode of binding and thus control the diverse inhibitory affinity of cystatins towards cysteine proteases. Docking outputs of cathepsin L1 complexes with stefin A, stefin B, cystatin C, cystatin D, cystatin F, cystatin M/E, cystatin S, cystatin SA, and cystatin SN
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additional information
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inhibitory interactions of human family 1 and 2 cystatins with cathepsin L1 are predicted and their stability and viability are verified through protein docking and comparative molecular dynamics, overview. The key amino acid residues surfaced via interaction energy, hydrogen bonding and solvent accessible surface area analysis for each cystatin-cathepsin L1 complex influence the mode of binding and thus control the diverse inhibitory affinity of cystatins towards cysteine proteases. Docking outputs of cathepsin L1 complexes with stefin A, stefin B, cystatin C, cystatin D, cystatin F, cystatin M/E, cystatin S, cystatin SA, and cystatin SN
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