EC Number   |
Natural Substrates |
|---|
   3.4.22.B49 | Collagen type I + H2O |
- |
| 3.4.22.B49 | Collagen type III + H2O |
- |
| 3.4.22.B49 | collagen type IV + H2O |
- |
| 3.4.22.B49 | Fibronectin + H2O |
- |
| 3.4.22.B49 | Gelatin + H2O |
- |
| 3.4.22.B49 | Hemoglobin + H2O |
- |
| 3.4.22.B49 | Hemoglobin + H2O |
Fasciola hepatica secretes cathepsin L cysteine proteases to invade its host, migrate through tissues and digest hemoglobin, its main source of amino acids. FheCL1 can degrade hemoglobin to small peptides, predominantly of 414 residues, but cannot release free amino acids. It is suggested that hemoglobin degradation is not completed in the gut lumen but the resulting peptides are absorbed by the gut epithelial cells for further processing by intracellular di- and amino-peptidases to free amino acids that are distributed through the parasite tissue for protein anabolism. The action of FheCL1 is enhanced by glutathione, the major reducing agent found in red blood cells |
| 3.4.22.B49 | Hemoglobin + H2O |
enzyme does not cleave its natural substrate hemoglobin in the pH range pH 5.5 and pH 7.0. Digestion occurs only at pH 4.5, which coincides with pH-induced dissociation of the hemoglobin tetramer |
| 3.4.22.B49 | Hemoglobin + H2O |
purified recombinant CL1 is not able to hydrolyze hemoglobin |
| 3.4.22.B49 | more |
the enzyme facilitates the penetration of the parasite though the tissue of its host, and also participates in functions such as feeding and immune evasion |
