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Literature summary for 3.4.18.1 extracted from
- Cathepsins L and Z are critical in degrading polyglutamine-containing proteins within lysosomes (2012), J. Biol. Chem., 287, 17471-17482.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Mus musculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| biotinyl-KKQ20KK + H2O | - |
Mus musculus | ? | within the lysosome, the major endoprotease, cathepsin L, carries out an initial attack within the polyglutamine repeat, which generates new C termini, facilitating the actions of the carboxypeptidase cathepsin Z. Extracts containing both cathespin L and Z show multiple cleavages within the polyglutamine sequence of biotinyl-KKQ20KK, generating a variety of fragments, including biotinyl-KKQ4,biotinyl-KKQ8, Q12KK, andQ16KK | ? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cathepsin Z | - |
Mus musculus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | RNAi for cathepsins L and Z confirms that they are critical in degrading polyglutamine-rich proteins (expanded huntingtin exon 1) but not other types of aggregation-prone proteins | Mus musculus |
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