Literature summary for 3.4.22.B49 extracted from

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

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Organism

Organism	UniProt	Comment	Textmining
Fasciola hepatica	Q24940	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	?	-	?

Synonyms

Synonyms	Comment	Organism
FhCL1	-	Fasciola hepatica

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Release 2023.1 (January 2023)