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Literature summary for 3.6.4.10 extracted from

  • Graf, C.; Stankiewicz, M.; Kramer, G.; Mayer, M.P.
    Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine (2009), EMBO J., 28, 602-613.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
E12C C for fluorescent labelling Escherichia coli
E12C/C-terminal truncation containing residue 1-496, monomeric Escherichia coli
E12C/E34A mutant hydrolyses ATP about 10-times more slowly than wild-type protein, C for fluorescent labelling Escherichia coli
E34A mutant hydrolyses ATP about 10-times more slowly than wild-type protein Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.25
-
ATP at 30°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homodimer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
chaperone hsp90
-
Escherichia coli
HtpG
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.011
-
ATP at 30°C Escherichia coli