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Literature summary for 3.4.23.5 extracted from
- Kinetic properties of cathepsin D and BACE 1 indicate the need to search for additional beta-secretase candidate(s) (2008), Biol. Chem., 389, 313-320.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | beta-secretase activity in brain is mainly due to cathepsin D. As cathepsin D shows poor activity towards the wild-type beta-site of the amyloid precursor protein it is necessary to continue the search for additional beta-secretase candidates | Homo sapiens |
| medicine | beta-secretase activity in brain is mainly due to cathepsin D. As cathepsin D shows poor activity towards the wild-type beta-site of the amyloid precursor protein it is necessary to continue the search for additional beta-secretase candidates | Sus scrofa |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| pepstatin A | strongly inhibits the cleavage of wild-tpye and mutated Swedish family peptide substrate bearing two mutated residues in the beta-site of the amyloid precursor protein | Homo sapiens |  |
| pepstatin A | strongly inhibits the cleavage of wild-tpye and mutated Swedish family peptide substrate bearing two mutated residues in the beta-site of the amyloid precursor protein | Sus scrofa | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.62 | - |
EEISEVNLDAEFRG | - |
Sus scrofa | |
| 1.1 | - |
EEISEVNLDAEFRG | - |
Homo sapiens | |
| 1.45 | - |
SEVNLDAEFR | - |
Sus scrofa | |
| 1.67 | - |
SEVNLDAEFR | - |
Homo sapiens | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Sus scrofa | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purified from a bovine brain homogenate | Sus scrofa |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| brain | - |
Sus scrofa | - |
| brain | by Western blot analysis it is shown that cathepsin is approximately 280fold more abundant in human brain than BACE-1 | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| EEISEVKMDAEFRG + H2O | beta-secretase activity assay: wild-type peptide substrate (14-mer) of the amyloid precursor protein. Cathepsin D shows only poor activity towards the wild-type beta-site sequence | Homo sapiens | EEISEVKM + DAEFRG | - |
? | |
| EEISEVKMDAEFRG + H2O | beta-secretase activity assay: wild-type peptide substrate (14-mer) of the amyloid precursor protein. Cathepsin D shows only poor activity towards the wild-type beta-site sequence | Sus scrofa | EEISEVKM + DAEFRG | - |
? | |
| EEISEVNLDAEFRG + H2O | beta-secretase activity assay: mutated Swedish family (SW) peptide subtrate (14-mer) with the two mutated residues flanking the beta-site of the amyloid precursor protein | Homo sapiens | EEISEVNL + DAEFRG | - |
? | |
| EEISEVNLDAEFRG + H2O | beta-secretase activity assay: mutated Swedish family (SW) peptide subtrate (14-mer) with the two mutated residues flanking the beta-site of the amyloid precursor protein | Sus scrofa | EEISEVNL + DAEFRG | - |
? | |
| SEVKMDAEFR + H2O | beta-secretase activity assay: wild-type peptide substrate (10-mer) of the beta-site of the amyloid precursor protein. Cathepsin D shows only poor activity towards the wild-type beta-site sequence | Homo sapiens | SEVKM + DAEFR | - |
? | |
| SEVKMDAEFR + H2O | beta-secretase activity assay: wild-type peptide substrate (10-mer) of the beta-site of the amyloid precursor protein. Cathepsin D shows only poor activity towards the wild-type beta-site sequence | Sus scrofa | SEVKM + DAEFR | - |
? | |
| SEVNLDAEFR + H2O | beta-secretase activity assay: mutated Swedish family (SW) peptide subtrate (10-mer) with the two mutated residues flanking the beta-site of the amyloid precursor protein | Homo sapiens | SEVNL + DAEFR | - |
? | |
| SEVNLDAEFR + H2O | beta-secretase activity assay: mutated Swedish family (SW) peptide subtrate (10-mer) with the two mutated residues flanking the beta-site of the amyloid precursor protein | Sus scrofa | SEVNL + DAEFR | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cathepsin D | - |
Homo sapiens |
| cathepsin D | - |
Sus scrofa |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.5 | - |
EEISEVNLDAEFRG | - |
Sus scrofa | |
| 8.8 | - |
SEVNLDAEFR | - |
Homo sapiens | |
| 29 | - |
SEVNLDAEFR | - |
Sus scrofa | |
| 31.4 | - |
EEISEVNLDAEFRG | - |
Homo sapiens | |
| 56.1 | - |
EEISEVNLDAEFRG | - |
Sus scrofa | |
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