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Literature summary for 3.4.23.5 extracted from
- CmCatD, a cathepsin D-like protease has a potential role in insect defense against a phytocystatin (2009), J. Insect Physiol., 55, 678-685.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| the propeptide is expressed in Escherichia coli BL21(DE3) cells | Callosobruchus maculatus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | not inhibited by E-64, leupeptin, and phenylmethylsulfonyl fluoride | Callosobruchus maculatus | |
| pepstatin A | - |
Callosobruchus maculatus |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 43000 | - |
recombinant proprotein, SDS-PAGE | Callosobruchus maculatus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Callosobruchus maculatus | CatD can trans-process CPA16 | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Callosobruchus maculatus | C7AAS7 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni2+-Sepharose column chromatography | Callosobruchus maculatus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| midgut | midgut from the 4th instar larva | Callosobruchus maculatus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Hemoglobin + H2O | - |
Callosobruchus maculatus | ? | - |
? | |
| additional information | CatD can trans-process CPA16 | Callosobruchus maculatus | ? | - |
? | |
| proteinaceous cysteine protease inhibitor from soybean sCN + H2O | - |
Callosobruchus maculatus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CatD | - |
Callosobruchus maculatus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4 | - |
maximal hydrolysis of hemoglobin is detected at pH 4.0 | Callosobruchus maculatus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 5.5 | autoprocessing of CatD becomes less efficient and eventually diminished at pH values 5.0 and above. At pH 5.5, while autoprocessing is inactive, mature CmCatD exhibits approximately 50% of its maximal enzymatic activity | Callosobruchus maculatus |
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Release 2023.1 (January 2023)
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