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Literature summary extracted from

  • Polyakova, O.; Dear, D.; Stern, I.; Martin, S.; Hirst, E.; Bawumia, S.; Nash, A.; Dodson, G.; Bronstein, I.; Bayley, P.M.
    Proteolysis of prion protein by cathepsin S generates a soluble beta-structured intermediate oligomeric form, with potential implications for neurotoxic mechanisms (2009), Eur. Biophys. J., 38, 209-218.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.22.27 dithiothreitol the presence of 0.2 mM dithiothreitol is required to maintain cathepsin activity Ovis aries

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.22.27 lysosome
-
 Ovis aries 5764
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.22.27 additional information Ovis aries proteolysis of prion protein by cathepsin S generates a soluble-structured intermediate oligomeric form, with potential implications for neurotoxic mechanisms ?
-
 ?
3.4.22.27 prion protein 94-233 + H2O Ovis aries in vitro, enzyme causes specific and limited N-terminal truncation of prion protein 94-233 prion protein 135-233 + prion protein 117-233 + prion protein 114-233 major soluble fragments, the region of prion protein between S135 and N146 is a major target for selective cleavage cathepsins S ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.27 Ovis aries
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.22.27 microglia
-
 Ovis aries
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.22.27 additional information
-
 cathepsin S, a cellular enzyme shows enhanced expression in pathogenic conditions Ovis aries

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.27 additional information proteolysis of prion protein by cathepsin S generates a soluble-structured intermediate oligomeric form, with potential implications for neurotoxic mechanisms Ovis aries ?
-
 ?
3.4.22.27 prion protein 94-233 + H2O in vitro, enzyme causes specific and limited N-terminal truncation of prion protein 94-233 Ovis aries prion protein 135-233 + prion protein 117-233 + prion protein 114-233 major soluble fragments, the region of prion protein between S135 and N146 is a major target for selective cleavage cathepsins S ?

Synonyms

EC Number Synonyms Comment Organism
3.4.22.27 cathepsin S
-
 Ovis aries

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.22.27 30
-
 assay at Ovis aries

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.22.27 additional information
-
 cathepsin S is a cysteine protease that is able to work outside the lysosome and in a wide range of pH Ovis aries

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.22.27 5.5
-
 assay at Ovis aries