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Literature summary for 3.4.22.1 extracted from

  • Alli, A.A.; Song, J.Z.; Al-Khalili, O.; Bao, H.F.; Ma, H.P.; Alli, A.A.; Eaton, D.C.
    Cathepsin B is secreted apically from Xenopus 2F3 cells and cleaves the epithelial sodium channel (ENaC) to increase its activity (2012), J. Biol. Chem., 287, 30073-30083.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.1

Inhibitors

Inhibitors Comment Organism Structure
L-3-trans-(propylcarbamoyl)-oxirane-2-carbonyl-L-isoleucyl-L-proline inhibition of cathepsin B decreases the number of active alpha ENaCs in 2F3 cells Xenopus laevis

Organism

Organism UniProt Comment Textmining
Xenopus laevis
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
epithelial sodium channel alpha subunit + H2O in vitro cleavage studies show that the full-length ENaC alpha subunit fusion protein is cleaved by active cathepsin B but not the full-length beta or gamma subunit fusion proteins Xenopus laevis ?
-
 ?

Synonyms

Synonyms Comment Organism
cathepsin B
-
 Xenopus laevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Xenopus laevis