Any feedback?
Literature summary for 3.4.23.25 extracted from
- Purification and properties of three endopeptidases from baker's yeast (1989), Can. J. Microbiol., 35, 295-303.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Urea | stimulates | Saccharomyces cerevisiae |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 1,2-epoxy-3-(4-nitrophenoxy)propane | - |
Saccharomyces cerevisiae | |
| Diazoacetyl-DL-norleucine methyl ester | - |
Saccharomyces cerevisiae | |
| pepstatin | - |
Saccharomyces cerevisiae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 42000 | - |
enzyme form A', gel filtration | Saccharomyces cerevisiae |
| 45000 | - |
1 * 45000, Saccharomyces cerevisiae, enzyme form A, SDS-PAGE | Saccharomyces cerevisiae |
| 49000 | - |
enzyme form A, gel filtration | Saccharomyces cerevisiae |
| 54000 | - |
1 * 54000, Saccharomyces cerevisiae, enzyme form A, SDS-PAGE | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
2 molecular forms: MW 45000 (A') and 54000 (A) | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Saccharomyces cerevisiae |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -20°C or 0°C, 0.05 M potassium phosphate buffer, pH 6.7, stable for many months | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| casein + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
| Hemoglobin + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 54000, Saccharomyces cerevisiae, enzyme form A, SDS-PAGE | Saccharomyces cerevisiae |
| monomer | 1 * 45000, Saccharomyces cerevisiae, enzyme form A', SDS-PAGE | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
the pH-optimum for hydrolysis of protein substrates can be shifted to about 5 with 4-6 M urea | Saccharomyces cerevisiae |
| 2.4 | 2.8 | and 5.5-6.0, casein | Saccharomyces cerevisiae |
| 2.7 | 3.2 | hemoglobin | Saccharomyces cerevisiae |
| 5.5 | 6 | and 2.4-2.8, casein | Saccharomyces cerevisiae |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3.6 | 6.8 | 37°C, optimal pH for stability | Saccharomyces cerevisiae |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
