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Literature summary for 3.4.22.B49 extracted from

  • Mebius, M.M.; Op Heij, J.M.J.; Tielens, A.G.M.; de Groot, P.G.; Urbanus, R.T.; van Hellemond, J.J.
    Fibrinogen and fibrin are novel substrates for Fasciola hepatica cathepsin L peptidases (2018), Mol. Biochem. Parasitol., 221, 10-13 .
    View publication on PubMed
Search for more literature for 3.4.22.B49

Inhibitors

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 FhCL1 Fasciola hepatica

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Fasciola hepatica
-
-

Organism

Organism UniProt Comment Textmining
Fasciola hepatica H8WG11
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Fibrin + H2O
-
 Fasciola hepatica ?
-
 ?
Fibrinogen + H2O enzyme FhCL3 is capable of degradation of the fibrinogen alpha-chain, beta-chain, and gamma-chain Fasciola hepatica ?
-
 ?

Synonyms

Synonyms Comment Organism
FhCL1
-
 Fasciola hepatica

General Information

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 andFhCL3 demonstrate only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain compared to FhCL1 Fasciola hepatica