EC Number   |
General Information |
Reference |
|---|
   3.4.22.B49 | evolution |
adult flukes produce three different clades of cathepsin Ls: FhCL1, FhCL2, and FhCL5 |
754983 |
| 3.4.22.B49 | more |
cathepsin L1 is a lysosomal cysteine protease with a papain-like structure. The CTSL1 homologue CgCTSL1 is identified from Crassostrea gigas as a protein containing a typical single Pept_C1 domain with three conserved catalytically essential residues (Gln25, His135 and Asn178) |
753379 |
| 3.4.22.B49 | more |
peptides QWKRMYNKEYNGADDEHRRNIWEENV and DKIDWRESGYVTELKDQGNC from the sequence of cathepsin L1 from Fasciola gigantica and the three-dimensional structure of cathepsin L1 from Fasciola hepatica, UniProt ID Q24940 and PDB ID 2o6x, are used for modelling of diagnostic peptides binding to cathepsinL1 antigen in fasciolosis, overview |
753520 |
| 3.4.22.B49 | more |
three-dimensional structure modeling of the protein sequence shows that the mature Da-CTSL1 protein folds into an expected cathepsin L structure producing a substrate binding pocket with appropriate positioning of conserved amino acid residues. The C-terminal catalytic domain possesses the two catalytically active Cys120 and His255 amino acid residues located in a pocket at the center of the predicted mature protein catalytic groove. Both domains are organized in such a way that the propeptide (PP) becomes inserted into the groove and completely masks the catalytic pocket of the active domain, inhibiting the proteinase activity of Da-CTSL1. The three-dimensional model also predicts that a network of fourteen hydrogen bonds involving D231, T233, L253, N254, E255, and E300 residues, allows the PP to anchor at the Da-CTSL1 catalytic groove. Residues R71, L76, S77, S78, S79, and K80 of PP participate in this H-bonding network |
754348 |
| 3.4.22.B49 | 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 andFhCL3 demonstrate only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain compared to FhCL1 |
754672 |
| 3.4.22.B49 | physiological function |
cathepsin L1 (CTSL1) is implicated in multiple processes of immune response against pathogen infection based on the proteolytic activity |
753379 |
| 3.4.22.B49 | physiological function |
Fasciola gigantica cathepsin L1H (FgCatL1H) is the isotype expressed in the early stages for migration and invasion |
754982 |
