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Literature summary for 3.6.4.10 extracted from

  • Schulze, A.; Beliu, G.; Helmerich, D.; Schubert, J.; Pearl, L.; Prodromou, C.; Neuweiler, H.
    Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism (2016), Nat. Chem. Biol., 12, 628-635 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.10

Protein Variants

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

Metals/Ions Comment Organism Structure
Mg2+ 10 mM used in assay conditions Saccharomyces cerevisiae

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 P02829
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
90-kDa heat shock protein
-
 Saccharomyces cerevisiae
Hsp90
-
 Saccharomyces cerevisiae

General Information

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