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Literature summary for 3.6.4.10 extracted from

  • Needham, P.G.; Masison, D.C.
    Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities (2008), Arch. Biochem. Biophys., 478, 167-174.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.10

Protein Variants

Protein Variants Comment Organism
A17V nucleotide-binding domain mutant Saccharomyces cerevisiae
L483W substrate-binding domain mutant Saccharomyces cerevisiae
R34K nucleotide-binding domain mutant Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 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
Hsp70 chaperone Ssa1
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information ATPase activities are stimulated by unfolded carboxy-methyl lactalbumin and the hydrophobic peptide A7 (stimulation factor 1.2-3.9) Saccharomyces cerevisiae
0.00062
-
 ATP mutant A17V Saccharomyces cerevisiae
0.00073
-
 ATP mutant R34K Saccharomyces cerevisiae
0.00078
-
 ATP wild type Saccharomyces cerevisiae
0.0073
-
 ATP mutant L483W Saccharomyces cerevisiae