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Literature summary for 3.6.4.10 extracted from

  • Bartolini, M.; Wainer, I.W.; Bertucci, C.; Andrisano, V.
    The rapid and direct determination of ATPase activity by ion exchange chromatography and the application to the activity of heat shock protein-90 (2013), J. Pharm. Biomed. Anal., 73, 77-81.
    View publication on PubMedView publication on EuropePMC

Application

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

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Homo sapiens
-
ADP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation Hsp90alpha Homo sapiens
-
additional information Hsp90s are overexpressed in cancer cells Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
heat shock protein 90-alpha
-
Homo sapiens
heat shock protein-90
-
Homo sapiens
Hsp90alpha
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Homo sapiens

General Information

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