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Literature summary for 3.6.4.10 extracted from

  • Silberg, J.J.; Vickery, L.E.
    Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli (2000), J. Biol. Chem., 275, 7779-7786.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Hsc20 cochaperone to Hsc66 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0127
-
ATP Hsc66 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
Hsc66 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + ATP Escherichia coli Hsc66 ATP + ADP
-
r
ATP + H2O Escherichia coli ATP hydrolysis catalyzed by Hsc66 ADP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Hsc66 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O = ADP + phosphate highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + ATP Hsc66 Escherichia coli ATP + ADP
-
r
ATP + H2O ATP hydrolysis catalyzed by Hsc66 Escherichia coli ADP + phosphate
-
?
ATP + H2O ATP hydrolysis catalyzed by Hsc66 Escherichia coli ADP + phosphate
-
r

Synonyms

Synonyms Comment Organism
DnaK
-
Escherichia coli
Hsc66
-
Escherichia coli