Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.6.1.7 extracted from

  • Diamant, S.; Azem, A.; Weiss, C.; Gouloubinoff, P.
    Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL (1995), Biochemistry, 34, 273-277.
    View publication on PubMed
Search for more literature for 5.6.1.7

Inhibitors

Inhibitors Comment Organism Structure
MgADP 50% inhibition at 0.205 mM Escherichia coli
Mn2+ 25% reversible inhibition of Mg-ATPase activity Escherichia coli
MnADP 50% inhibition at 0.036 mM Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ half maximal ATPase activation at 2.6 mM Escherichia coli
Mn2+ half maximal ATPase activation at 2.3 mM 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
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0275
-
 ATP Mn2+ concentration variable, ATP concentration fixed, Mn-ATP complexes at 1 mM ATP and 0.8 mM Mn2+ Escherichia coli
0.0462
-
 ATP ATP concentration variable, Mn2+ concentration fixed, Mn-ATP complexes at 1 mM ATP and 0.8 mM Mn2+ Escherichia coli
0.0565
-
 ATP Mg2+ concentration variable, ATP concentration fixed, Mg-ATP complexes at 1 mM ATP and 0.8 mM Mg2+ Escherichia coli
0.1
-
 ATP ATP concentration variable, Mg2+ concentration fixed, Mg-ATP complexes at 1 mM ATP and 0.8 mM Mg2+ Escherichia coli