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Literature summary extracted from

  • Robinson, M.W.; Dalton, J.P.; Donnelly, S.
    Helminth pathogen cathepsin proteases (2008), Trends Biochem. Sci., 33, 601-608.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.B49 Fasciola hepatica Q24940
-
-
3.4.22.B60 Fasciola hepatica Q24940
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.B49 Hemoglobin + H2O FhCL1 cleaves substrates with hydrophobic residues (Phe and Leu) in the P2 position with catalytic rates (kcat/Km) that are 25- and eightfold greater, respectively, than FhCL2. In comparison to human cathepsin L, which can accommodate a wide range of amino acids in the S2 subsite, the S2 subsite of FhCL1 is restricted. Hydrophobic residues are most susceptible to cleavage, in the order Leu > Val > Ala > Phe. Together, these four residues make up about 42% of the hemoglobin molecule and, therefore, it seems that FhCL1 has been specifically adapted to degrade the host substrate, which it exploits as nutrient. Substrates with proline in the P2 position, which are good substrates for FhCL2 are poorly cleaved by FhCL1 (and not at all by human cathepsin L) Fasciola hepatica ?
-
 ?
3.4.22.B60 Collagen + H2O FhCL2 cleaves substrates with a bulky proline in the P2 position as the native collagen, which contains a repeat motif of Gly-Pro-Xaa (in which Xaa is any amino acid). By contrast these substrates are poorly cleaved by FhCL1 and not at all by human cathepsin L Fasciola hepatica ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.22.B49 FhCL1
-
 Fasciola hepatica
3.4.22.B60 FhCL2
-
 Fasciola hepatica