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Literature summary for 3.4.22.27 extracted from

  • Kopitar, G.; Dolinar, M.; Strukelj, B.; Pungercar, B.; Turk, V.
    Folding and activation of human procathepsin S from inclusion bodies produced in Escherichia coli (1996), Eur. J. Biochem., 236, 558-562.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
inclusion body recombinant enzyme expressed in Escherichia coli Homo sapiens 16234
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
x * 24000, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the proenzyme is autocatalytically processed to active cathepsin S at pH 4.5 in the presence of an excess of cysteine and catalytic amounts of dextran sulfate Homo sapiens

Renatured (Commentary)

Renatured (Comment) Organism
recombinant procathepsin S from inclusion bodies produced in Escherichia coli is renatured at pH 7.6 by a two-step dilution Homo sapiens

Subunits

Subunits Comment Organism
? x * 24000, SDS-PAGE Homo sapiens
More most of the loss of procathepsin S occurs during folding, probably because of aggregation. Concentrations lower than 0.02 mg/ml of procathepsin S are necessary to minimise such aggregation Homo sapiens