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Literature summary for 3.6.4.10 extracted from
- Importance of Hsp70 ATPase domain in yeast prion propagation (2007), Genetics, 175, 621-630.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | identification of 25 mutations within the two major cytosolic Hsp70-SSa molecular chaperones that impair the propagation of the [PSI+] prion. All but one mutation are located within the ATPase domain, and only mutation SSA2-A176T has major effects on growth rate | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Saccharomyces cerevisiae | regulation of Hsp70 Ssa chaperone ATP hydrolysis is involved in prion propagation | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
isoform Hsp70 | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | regulation of Hsp70 Ssa chaperone ATP hydrolysis is involved in prion propagation | Saccharomyces cerevisiae | ? | - |
? | |
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