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Literature summary for 3.4.21.25 extracted from
- Isolation and characterization of a possible native cucumisin from developing melon fruits and its limited autolysis to cucumisin (1989), Agric. Biol. Chem., 53, 1009-1017.
No PubMed abstract available
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| diisopropyl fluorophosphate | completely inactivated at 0.5 mM for 10 min | Cucumis melo |  |
| HgCl2 | 10% inhibition by 0.5 mM | Cucumis melo | |
| additional information | no effect: iodoacetate, EDTA, PCMB, beta-mercaptoethanol, cysteine, N-tosyl-L-phenylalanine chloromethyl ketone and PCMB; no effect of plant proteinous inhibitors of serine proteinases | Cucumis melo | |
| PMSF | slightly inactivated by 0.1 mM, 11% inhibition by 0.5 mM, 23% inhibition by 1 mM | Cucumis melo | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | not affected by CaCl2, CdCl2, MnSO4, CoSO4 and ZnSO4 | Cucumis melo |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 54000 | - |
native enzyme, a large precursor has a MW of 67000 Da, consists of a 14000 Da C-terminal polypeptide and the active 54000 Da protease domain, which arises by limited autolysis, SDS-PAGE | Cucumis melo |
| 67000 | - |
native cucumisin, consists of a 14000 Da C-terminal polypeptide and the active 54000 Da protease domain, which arises by limited autolysis, 62000 Da by gel filtration, SDS-PAGE | Cucumis melo |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Protein + H2O | Cucumis melo | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cucumis melo | - |
L. var Prince | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Cucumis melo |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| fruit | - |
Cucumis melo | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| casein + H2O | - |
Cucumis melo | ? | - |
? | |
| Protein + H2O | - |
Cucumis melo | ? | - |
? | |
| protein + H2O | - |
Cucumis melo | hydrolyzed protein | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
both, the 67000 Da and the 54000 Da enzyme | Cucumis melo |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
the 54000 Da enzyme stable up to | Cucumis melo |
| 70 | - |
the 67000 Da enzyme was stable up to | Cucumis melo |
| 90 | - |
both, the 67000 Da and the 54000 Da enzyme were completely inactivated after 10 min above | Cucumis melo |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 10.5 | - |
both, the 67000 Da and the 54000 Da enzyme | Cucumis melo |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
the 67000 Da native enzyme is more stable at acidic pH than the 54000 Da proteinase | Cucumis melo |
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