Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ATP | ATP binding to nucleotide-binding domain 1 serves as a central regulatory switch for the chaperone, it triggers binding of polypeptides and stimulates ATP hydrolysis in the C-terminal nucleotide-binding domain 2 by more than 2 orders of magnitude | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
E285Q | impaired hydrolysis of ATP at nucleotide-binding domain 1 | Saccharomyces cerevisiae |
E285Q/E687Q | impaired hydrolysis of ATP at nucleotide-binding domains 1 and 2 | Saccharomyces cerevisiae |
E687Q | impaired hydrolysis of ATP at nucleotide-binding domain 2 | Saccharomyces cerevisiae |
K218T | impaired binding and hydrolysis of ATP at nucleotide-binding domain 1 | Saccharomyces cerevisiae |
K620T | impaired binding and hydrolysis of ATP at nucleotide-binding domain 2 | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
isoform Hsp104 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Hsp104 actively unfolds its substrates during processing | Saccharomyces cerevisiae | ? | - |
? |