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BRENDA support

Literature summary for 5.6.1.7 extracted from

  • Ranson, N.A.; White, H.E.; Saibil, H.R.
    Chaperonins (1998), Biochem. J., 333, 233-242.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
GroES
-
Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Escherichia coli 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
58000
-
14 * 58000, two heptameric rings stacked back-to-back Escherichia coli
812000
-
-
Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide binding and hydrolysis of ATP sets up an alternating cycle in which each ring of the chaperonin is switched between states with strong and weak affinity for a non-native protein substrate Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide
-
Escherichia coli ADP + phosphate + an unfolded polypeptide
-
?

Subunits

Subunits Comment Organism
tetradecamer 14 * 58000, two heptameric rings stacked back-to-back Escherichia coli