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Literature summary for 5.6.1.7 extracted from

  • Mendoza, J.A.; Warren, T.; Dulin, P.
    The ATPase activity of chaperonin GroEL is highly stimulated at elevated temperatures (1996), Biochem. Biophys. Res. Commun., 229, 271-274.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
GroES inhibition between 25°C and 49°C, no inhibition at 52°C or above Escherichia coli

Localization

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

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
-
-
-

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
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
52
-
-
Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 64 ATPase activity gradually increases between 25°C and 52°C, strong decrease above Escherichia coli