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Literature summary for 3.4.23.5 extracted from
- Identification and characterization of cathepsin D in a highly purified sialidase from starfish A. pectinifera (2008), J. Biochem., 143, 117-122.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| pepstatin A | - |
Patiria pectinifera |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50000 | - |
SDS-PAGE | Patiria pectinifera |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Patiria pectinifera | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purified by ammonium sulfate precipitation and octyl sepharose, Con-A sepharose, CM-sephadex columns sequentially. Finally, by preparative gel electrophoresis. On SDS-PAGE the purified preparation gives two bands 50 kDa and 47 kDa. The upper band is characterized as cathepsin D and the lower band as sialidase. The two enzymes are separated from each other by using high-performance gel-filtration chromatography | Patiria pectinifera |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1.15 | - |
after preparative PAGE (gel concentration 7%) | Patiria pectinifera |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2 + H2O | - |
Patiria pectinifera | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cathepsin D | - |
Patiria pectinifera |
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Release 2023.1 (January 2023)
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