Any feedback?
Literature summary extracted from
- Fibrinogen and fibrin are novel substrates for Fasciola hepatica cathepsin L peptidases (2018), Mol. Biochem. Parasitol., 221, 10-13 .
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.22.B49 | 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 | Fasciola hepatica | |
| 3.4.22.B60 | 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
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.22.B49 | extracellular | the enzyme is secreted | Fasciola hepatica | - |
- |
| 3.4.22.B60 | extracellular | the enzyme is secreted | Fasciola hepatica | - |
- |
| 3.4.22.B62 | extracellular | the enzyme is secreted | Fasciola hepatica | - |
- |
| 3.4.22.B62 | extracellular | the enzyme is secreted | Schistosoma mansoni | - |
- |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.22.B49 | Fasciola hepatica | H8WG11 | - |
- |
| 3.4.22.B60 | Fasciola hepatica | A0A220T1Z2 | procathepsin L2 | - |
| 3.4.22.B62 | Fasciola hepatica | B3TM67 | - |
- |
| 3.4.22.B62 | Schistosoma mansoni | B4XC67 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.22.B49 | Fibrin + H2O | - |
Fasciola hepatica | ? | - |
? |  |
| 3.4.22.B49 | Fibrinogen + H2O | enzyme FhCL3 is capable of degradation of the fibrinogen alpha-chain, beta-chain, and gamma-chain | Fasciola hepatica | ? | - |
? | |
| 3.4.22.B60 | Fibrin + H2O | - |
Fasciola hepatica | ? | - |
? | |
| 3.4.22.B60 | Fibrinogen + H2O | FhCL2 demonstrates only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain | Fasciola hepatica | ? | - |
? | |
| 3.4.22.B62 | Collagen + H2O | - |
Fasciola hepatica | ? | - |
? | |
| 3.4.22.B62 | Fibrinogen + H2O | FhCL3 demonstrates only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain | Fasciola hepatica | ? | - |
? | |
| 3.4.22.B62 | additional information | no activity with fibrinogen or fibrin | Schistosoma mansoni | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.22.B49 | FhCL1 | - |
Fasciola hepatica |
| 3.4.22.B60 | FhCL2 | - |
Fasciola hepatica |
| 3.4.22.B62 | FhCL3 | - |
Fasciola hepatica |
| 3.4.22.B62 | SmCL3 | - |
Schistosoma mansoni |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 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 | Fasciola hepatica |
| 3.4.22.B60 | 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 |
| 3.4.22.B62 | 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 degrade 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 | Fasciola hepatica |
| 3.4.22.B62 | physiological function | schistosomal cathepsin peptidases are not able to cleave fibrinogen or fibrin, which is in line with the presence of other anticoagulant and fibrinolytic strategies adopted by schistosomes. This allows schistosomes to counteract fibrin formation at their surface, allowing blood-feeding and survival of the parasite within its host | Schistosoma mansoni |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
