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Literature summary for 5.6.1.7 extracted from

  • Mizobata, T.; Kawata, Y.
    The versatile mutational repertoire of Escherichia coli GroEL, a multidomain chaperonin nanomachine (2018), Biophys. Rev., 10, 631-640 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
C138W at 37°C, the mutant enzyme is indistinguishable in all aspects from the wild type, however, at 25°C, steric hindrances cause the chaperonin to be arrested in a ternary complex form, with both unfolded protein and GroES bound to the same ring of the enzyme. An increase in temperature to more than 30°C is sufficient to restart both target protein refolding and ATPase activity in the mutant enzyme Escherichia coli
D398A ATP-hydrolysis deficient mutant Escherichia coli
G192W the mutant enzyme is capable of binding to GroES in the absence of ATP binding 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
-
-
-

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 * 57000, calculated from amino acid sequence Escherichia coli

Synonyms

Synonyms Comment Organism
chaperonin
-
Escherichia coli
GroEl
-
Escherichia coli