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Literature summary for 3.4.22.27 extracted from

  • Wiederanders, B.
    The function of propeptide domains of cysteine proteinases (2000), Adv. Exp. Med. Biol., 477, 261-270.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DELTAW52-N63 mutant procathepsin S is expressed in HEK 293 cells as a stable protein. However it is not processed to mature cathepsin S as is the wild-type procathepsin S Homo sapiens

Protein Variants

Protein Variants Comment Organism
DELTAW52-N63 the mutant procathepsin S is expressed in HEK 293 cells as a stable protein. However it is not processed to mature cathepsin S as is the wild-type procathepsin S Homo sapiens
E44A mutant procathepsin S shows lysosomal localization Homo sapiens
N104Q no substantial maturation of the mutant has been observed Homo sapiens
W52A mutant enzyme does not show a lysosomal localization Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
cathespin S propeptide tight binding/slow reacting inhibition Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification structural stability and the folding of procathepsin S are considerably dependent on an aromatic stack built by the residue Trp28, Trp31 and Trp52 Homo sapiens
proteolytic modification the propeptide domain of procathepsin S shows chaperone function Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00000005
-
cathepsin S propeptide wild-type enzyme Homo sapiens
0.0000003
-
cathepsin S propeptide mutant enzyme E44A Homo sapiens
0.0000013
-
cathepsin S propeptide mutant enzyme R48A Homo sapiens