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Literature summary for 3.4.23.18 extracted from
- Purification and characterization of the two molecular forms of membrane acid protease from Aspergillus oryzae (1978), Eur. J. Biochem., 84, 347-353.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| cholesterol | activation, acetone-washed membrane-bound enzyme | Aspergillus oryzae |  |
| Diglycerides | activation, acetone-washed membrane-bound enzyme | Aspergillus oryzae | |
| monoglycerides | activation, acetone-washed membrane-bound enzyme | Aspergillus oryzae | |
| additional information | no activation of membrane-bound enzyme by triglycerides or 1,3-dipalmitin | Aspergillus oryzae | |
| Phospholipids | activation, acetone-washed membrane-bound enzyme | Aspergillus oryzae | |
| Triton X-100 | activation, acetone-washed membrane-bound enzyme | Aspergillus oryzae | |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | diisopropyl phosphofluoridate; monoiodoacetate, 1,10-phenanthroline, 6-aminohexanoate; PCMB | Aspergillus oryzae | |
| N-bromosuccinimide | not | Aspergillus oryzae | |
| SDS | 3.3 mM | Aspergillus oryzae | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Aspergillus oryzae | 16020 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 100000 | - |
Aspergillus oryzae, enzyme form M2, gel filtration | Aspergillus oryzae |
| 230000 | - |
Aspergillus oryzae, Triton X-100 treated enzyme, gel filtration | Aspergillus oryzae |
| 2000000 | - |
Aspergillus oryzae, enzyme form M1, gel filtration | Aspergillus oryzae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus oryzae | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | 80.5% (enzyme form M1), 52.5% (enzyme form M2) | Aspergillus oryzae |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| several isoforms (membrane-bound M1 and M2) | Aspergillus oryzae |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| mycelium | - |
Aspergillus oryzae | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 143 | - |
enzyme form M1, in the presence of Triton X-100 | Aspergillus oryzae |
| 867 | - |
enzyme form M2, in the presence of Triton X-100 | Aspergillus oryzae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Cytochrome c + H2O | - |
Aspergillus oryzae | ? | - |
? | |
| Hemoglobin + H2O | urea-denatured hemoglobin | Aspergillus oryzae | ? | - |
? | |
| Trypsinogen + H2O | - |
Aspergillus oryzae | ? | - |
? | |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
10 min, in 50 mM sodium acetate buffer, pH 5 | Aspergillus oryzae |
| 55 | - |
isozyme M1 retains more than 95% of its original activity, M2 is completely inactivated | Aspergillus oryzae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 3.2 | - |
cytochrome c | Aspergillus oryzae |
| 4.5 | - |
urea-denatured hemoglobin | Aspergillus oryzae |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 6 | stable in this range, complete inactivation below 2 and above 7 | Aspergillus oryzae |
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