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Literature summary for 3.4.22.1 extracted from

  • Malagon, D.; Díaz-Lopez, M.; Benítez, R.; Adroher, F.
    Cathepsin B- and L-like cysteine protease activities during the in vitro development of Hysterothylacium aduncum (Nematoda: Anisakidae), a worldwide fish parasite (2010), Parasitol. Int., 59, 89-92.
    View publication on PubMed
Search for more literature for 3.4.22.1

Inhibitors

Inhibitors Comment Organism Structure
E-64 i.e. L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane, irreversible inhibitor Hysterothylacium aduncum

Organism

Organism UniProt Comment Textmining
Hysterothylacium aduncum
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
larva
-
 Hysterothylacium aduncum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity with benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin Hysterothylacium aduncum ?
-
 ?
Nalpha-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
-
 Hysterothylacium aduncum Nalpha-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.5
-
 Hysterothylacium aduncum

pH Range

pH Minimum pH Maximum Comment Organism
5 8
-
 Hysterothylacium aduncum

Expression

Organism Comment Expression
Hysterothylacium aduncum cathepsin B activity decreassd after developmental stage M4, returning to its initial level down
Hysterothylacium aduncum the start of cultivation during in vitro development leads to 1.8fold increased activity up

General Information

General Information Comment Organism
physiological function cathepsin B is involved in cuticle renewal Hysterothylacium aduncum