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Literature summary extracted from

  • Nowak, J.; Tsai, H.
    Purification and properties of three endopeptidases from baker's yeast (1989), Can. J. Microbiol., 35, 295-303.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.48 Urea stimulates Saccharomyces cerevisiae
3.4.23.25 Urea stimulates Saccharomyces cerevisiae

General Stability

EC Number General Stability Organism
3.4.21.48 freezing and thawing has no effect Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.48 PCMB
-
 Saccharomyces cerevisiae
3.4.21.48 PMSF
-
 Saccharomyces cerevisiae
3.4.21.48 Trypsin inhibitor inhibitor isolated from potato tuber Saccharomyces cerevisiae
3.4.23.25 1,2-epoxy-3-(4-nitrophenoxy)propane
-
 Saccharomyces cerevisiae
3.4.23.25 Diazoacetyl-DL-norleucine methyl ester
-
 Saccharomyces cerevisiae
3.4.23.25 pepstatin
-
 Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.48 34000
-
 gel filtration Saccharomyces cerevisiae
3.4.23.25 42000
-
 enzyme form A', gel filtration Saccharomyces cerevisiae
3.4.23.25 45000
-
 1 * 45000, Saccharomyces cerevisiae, enzyme form A, SDS-PAGE Saccharomyces cerevisiae
3.4.23.25 49000
-
 enzyme form A, gel filtration Saccharomyces cerevisiae
3.4.23.25 54000
-
 1 * 54000, Saccharomyces cerevisiae, enzyme form A, SDS-PAGE Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.48 Saccharomyces cerevisiae
-
 Saccharomyces cerevisiae
-
3.4.23.25 Saccharomyces cerevisiae
-
 2 molecular forms: MW 45000 (A') and 54000 (A)
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.48
-
 Saccharomyces cerevisiae
3.4.23.25
-
 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
3.4.23.25 additional information
-
-
 Saccharomyces cerevisiae

Storage Stability

EC Number Storage Stability Organism
3.4.21.48 -20°C, stable for several months Saccharomyces cerevisiae
3.4.23.25 -20°C or 0°C, 0.05 M potassium phosphate buffer, pH 6.7, stable for many months Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.48 additional information milk-clotting activity Saccharomyces cerevisiae ?
-
 ?
3.4.21.48 nitrated casein + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
3.4.23.25 casein + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
3.4.23.25 Hemoglobin + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
3.4.23.25 Oxidized B-chain of insulin + H2O at pH 3.0 or at pH 4.7 in the presence of 4 M urea, the enzyme preferentially cleaves peptide bonds of the X-Tyr and X-Phe types, the peptide bonds Leu15-Tyr16, Phe24-Phe25 and Phe25-Tyr26 are hydrolyzed simultaneously Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.48 monomer
-
 Saccharomyces cerevisiae
3.4.23.25 monomer 1 * 54000, Saccharomyces cerevisiae, enzyme form A, SDS-PAGE Saccharomyces cerevisiae
3.4.23.25 monomer 1 * 45000, Saccharomyces cerevisiae, enzyme form A', SDS-PAGE Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.48 6.5 7.5 hydrolysis of nitrated casein, in presence of 4 M urea Saccharomyces cerevisiae
3.4.21.48 6.5 9.8 hydrolysis of nitrated casein, in absence of urea Saccharomyces cerevisiae
3.4.23.25 additional information
-
 the pH-optimum for hydrolysis of protein substrates can be shifted to about 5 with 4-6 M urea Saccharomyces cerevisiae
3.4.23.25 2.4 2.8 and 5.5-6.0, casein Saccharomyces cerevisiae
3.4.23.25 2.7 3.2 hemoglobin Saccharomyces cerevisiae
3.4.23.25 5.5 6 and 2.4-2.8, casein Saccharomyces cerevisiae

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.23.25 3.6 6.8 37°C, optimal pH for stability Saccharomyces cerevisiae