Application | Comment | Organism |
---|---|---|
drug development | human heat shock protein 90 is a target in cancer drug discovery, inhibition of ATP hydrolysis is a validated avenue for the development of anticancer therapies | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Homo sapiens | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | Hsp90alpha | Homo sapiens | - |
additional information | Hsp90s are overexpressed in cancer cells | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Homo sapiens | ADP + phosphate | - |
? | |
additional information | development and optimization of an ion exchange liquid chromatography method for the determination of ATP, ADP and AMP, for the direct separation, identification and determination of the adenosine nucleotides using a small disk shaped monolithic ethylenediamine column, specifically aimed at the determination of the ATP-ase activity of human heat shock protein 90, Hsp90, detailed overview | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
heat shock protein 90-alpha | - |
Homo sapiens |
heat shock protein-90 | - |
Homo sapiens |
Hsp90alpha | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | Hsp90 is part of a family of molecular chaperones that play a crucial role in the normal folding, intracellular disposition, and proteolytic turnover of a vast array of factors involved in cell regulation. The Hsp90 protein folding activity is ATP-dependent and ATP hydrolysis is a key aspect in the Hsp90 chaperone function. Increase of Hsp90 expression and activity has been linked with the protection of oncoproteins from physiological clearance | Homo sapiens |