Protein Variants | Comment | Organism |
---|---|---|
A107N | the mutation increases ATPase activity about 5fold compared to the wild type | Saccharomyces cerevisiae |
F349A | inactive | Saccharomyces cerevisiae |
T101I | the mutation substantially reduces ATPase activity | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | 10 mM used in assay conditions | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Saccharomyces cerevisiae | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P02829 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Saccharomyces cerevisiae | ADP + phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
90-kDa heat shock protein | - |
Saccharomyces cerevisiae |
Hsp90 | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
metabolism | the Hsp90 chaperone is a central node of protein homeostasis activating a large number of diverse client proteins. Hsp90 functions as a molecular clamp that closes and opens in response to the binding and hydrolysis of ATP | Saccharomyces cerevisiae |