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Literature summary for 5.6.1.7 extracted from

  • Melkani, G.C.; Zardeneta, G.; Mendoza, J.A.
    The ATPase activity of GroEL is supported at high temperatures by divalent cations that stabilize its structure (2003), BioMetals, 16, 479-484.
    View publication on PubMed
Search for more literature for 5.6.1.7

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ 2 mM, 41% of activity with Mg2+ Escherichia coli
K+ required for activity, maximal activity at 2 mM Escherichia coli
Mg2+ required for activity, maximal activity at 2 mM Escherichia coli
Mn2+ 2 mM, 64% of activity with Mg2+ Escherichia coli
NH4+ can fully substitute for K+ Escherichia coli
Ni2+ 2 mM, 29% of activity with Mg2+ Escherichia coli
Rb+ can fully substitute for K+ 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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 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
49
-
 in the presence of 2 mM K+ and Mg2+ Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 60 approx. 50% of maximal activity at 30°C, approx. 90% of maximal activity at 55°C, almost no activity at 60°C Escherichia coli