Inhibitors | Comment | Organism | Structure |
---|---|---|---|
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 FhCL2 | Fasciola hepatica |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | the enzyme is secreted | Fasciola hepatica | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Fasciola hepatica | A0A220T1Z2 | procathepsin L2 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Fibrin + H2O | - |
Fasciola hepatica | ? | - |
? | |
Fibrinogen + H2O | FhCL2 demonstrates only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain | Fasciola hepatica | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
FhCL2 | - |
Fasciola hepatica |
General Information | Comment | Organism |
---|---|---|
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 and FhCL3 demonstrate only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain compared to FhCL1 | Fasciola hepatica |