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Literature summary for 3.6.4.10 extracted from
- Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides (2005), J. Biol. Chem., 280, 38170-38176.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K218T | mutation results in complete loss of polypeptide binding | Saccharomyces cerevisiae |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 611000 | - |
sedimentation equilibrium analysis | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Hsp104 mediates the solubilization of aggregated proteins in an ATP-dependent process assisted by the Hsp70/40 system. The affinity of Hsp104 toward polypeptides is regulated by nucleotides. In the presence of ATP or adenosine-5 -O -(3-thiotriphosphate), the chaperone forms complexes with reduced,carboxymethylated alpha-lactalbumin (RCMLa), a permanently unfolded model substrate. No binding is observed in the presence of ADP. The occupation of the N-terminally located nucleotide-binding domain with ATP seems to be crucial for substrate interaction. When ATP binding to this domain is impaired by mutation,Hsp104 loses its ability to interact with RCMLa. Upon association with a polypeptide,a conformational change occurs within Hsp104 that strongly reduces the dynamics of nucleotide exchange and commits the bound polypeptide to ATP hydrolysis | Saccharomyces cerevisiae | ADP + phosphate | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | - |
Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Hsp104 | - |
Saccharomyces cerevisiae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0194 | - |
ATP | wild-type enzyme | Saccharomyces cerevisiae | |
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Release 2023.1 (January 2023)
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