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Literature summary for 3.4.22.1 extracted from

  • Asai, M.; Yagishita, S.; Iwata, N.; Saido, T.C.; Ishiura, S.; Maruyama, K.
    An alternative metabolic pathway of amyloid precursor protein C-terminal fragments via cathepsin B in a human neuroglioma model (2011), FASEB J., 25, 3720-3730.
    View publication on PubMed
Search for more literature for 3.4.22.1

Inhibitors

Inhibitors Comment Organism Structure
CA-074 cathepsin B inhibitor III, i.e. [L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline Homo sapiens
CA-074Me cathepsin B specific inhibitor, cathepsin B inhibitor IV, i.e. [L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline methyl ester Homo sapiens
E-64d i.e. (L-3-trans-ethoxycarbonyloxirane-2-carbonyl)-L-leucine(3-methylbutyl)amide Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
H4 neuroglioma cell
-
 Homo sapiens
-
liver
-
 Homo sapiens
-
neuroglioma cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amyloid precursor protein C-terminal fragment + H2O cathepsin B degraded C-terminal fragments regardless of phosphorylation Homo sapiens ?
-
 ?
amyloid precursor protein intracellular domain + H2O
-
 Homo sapiens ?
-
 ?

General Information

General Information Comment Organism
malfunction inhibition of cathepsin B has no inhibitory effect on Notch processing Homo sapiens
physiological function cathepsin B plays a role in the metabolism of amyloid precursor protein. Cathepsin B is a major CTF- and AICD-degrading enzyme with no effect on alpha- and beta-secretase activities Homo sapiens