Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.6.4.10 extracted from

  • Lotz, G.P.; Lin, H.; Harst, A.; Obermann, W.M.
    Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone (2003), J. Biol. Chem., 278, 17228-17235.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
activator of Hsp90 ATPase Aha1, 5fold activation of intrinsic ATPase activity Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E381K no loss of ATPase activity at the non permissive temperature of 37°C Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Saccharomyces cerevisiae 5829
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant yHsp90 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Saccharomyces cerevisiae ADP + phosphate
-
?

Synonyms

Synonyms Comment Organism
yHsp90
-
Saccharomyces cerevisiae

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 37 2fold increase of ATPase activity at 37°C Saccharomyces cerevisiae