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Literature summary extracted from

  • Lenney, J.F.; Dalbec, J.M.
    Purification and properties of two proteinases from Saccharomyces cerevisiae (1967), Arch. Biochem. Biophys., 120, 42-48.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.4.21.48 0.5% gelatin stabilizes Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.48 Ag+
-
 Saccharomyces cerevisiae
3.4.21.48 Cu2+
-
 Saccharomyces cerevisiae
3.4.21.48 Hg2+ fully reversed by Cys Saccharomyces cerevisiae
3.4.21.48 PCMB inhibition is partly reversed by Cys Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.48 additional information 80% or more of the proteinase in the yeast cell is in the zymogen form and seems to be particle-bound Saccharomyces cerevisiae
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.48 73000
-
 gel filtration Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.48 Saccharomyces cerevisiae
-
 Saccharomyces cerevisiae
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.48
-
 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.21.48 additional information
-
-
 Saccharomyces cerevisiae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.48 additional information
-
-
 Saccharomyces cerevisiae