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Literature summary for 3.6.4.10 extracted from

  • Lissin, N.M.; Venyaminov, S.Y.; Girshovich, A.S.
    (Mg-ATP)-dependent self-assembly of molecular chaperone GroEL (1990), Nature, 348, 339-342.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
GroES required for the functioning of the Escherichia coli heat shock protein, also stimulates the reassembly Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57260
-
-
Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
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.
ATP + H2O
-
Escherichia coli ADP + phosphate
-
?

Subunits

Subunits Comment Organism
oligomer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
heat shock protein GroEl
-
Escherichia coli
molecular chaperone GroEl
-
Escherichia coli