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Literature summary for 3.4.23.5 extracted from
- Purification and characterization of a cathepsin D protease from bovine chromaffin granule (1992), Biochemistry, 31, 4223-4231.
General Stability
| General Stability | Organism |
|---|---|
| stable against repetitive freezing and thawing | Bos taurus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| pepstatin | pepstatin A | Bos taurus |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| chromaffin granule | - |
Bos taurus | 42583 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 45000 | 55000 | two enzyme forms exist: a single 47000 Da polypeptide and a complex of 30000 Da subunit plus a 16500 Da subunit, gel filtration | Bos taurus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Bos taurus | possible participation of the enzyme in cleaving some peptide precursors | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| side-chain modification | glycoprotein | Bos taurus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Bos taurus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Bos taurus |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -70°C, stable | Bos taurus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | cleaves at paired basic residues and at hydrophobic residues | Bos taurus | ? | - |
? | |
| additional information | possible participation of the enzyme in cleaving some peptide precursors | Bos taurus | ? | - |
? | |
| neuropeptide K + H2O | cleaved at a Lys-Arg basic residue site | Bos taurus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | two enzyme forms exist: a single 47000 Da polypeptide and a complex of 30000 Da subunit plus a 16500 Da subunit, SDS-PAGE | Bos taurus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 5.5 | - |
Bos taurus |
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Release 2023.1 (January 2023)
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