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Literature summary for 5.6.1.7 extracted from

  • Noi, K.; Hirai, H.; Hongo, K.; Mizobata, T.; Kawata, Y.
    A potentially versatile nucleotide hydrolysis activity of group II chaperonin monomers from Thermoplasma acidophilum (2009), Biochemistry, 48, 9405-9415.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermoplasma acidophilum

Protein Variants

Protein Variants Comment Organism
D391A ATP, ADP, and AMP hydrolysis activities decreased significantly compared to wild type, with the exception of the ATP hydrolysis in presence of Co2+ Thermoplasma acidophilum
D394A ATP, ADP, and AMP hydrolysis activities decreased significantly compared to wild type Thermoplasma acidophilum
D62A ATP, ADP, and AMP hydrolysis activities decreased significantly compared to wild type Thermoplasma acidophilum
D67A ATP, ADP, and AMP hydrolysis activities decreased significantly compared to wild type, with the exception of the ATP hydrolysis in presence of Co2+ Thermoplasma acidophilum

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
Thermoplasma acidophilum

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ Ta-cpn beta1 shows ATPase activity in the presence of Co2+. A weak ATPase activity is observed in the presence of Mn2+ or Mg2+ Thermoplasma acidophilum
Co2+ Ta-cpn R1 hydrolyzes ATP in the presence of Co2+, Mn2+, or Mg2+. ATPase activity of the monomeric enzyme is the highest in the presence of Co2+ Thermoplasma acidophilum
Mg2+ Ta-cpn beta1 shows ATPase activity in the presence of Co2+. A weak ATPase activity is observed in the presence of Mn2+ or Mg2+ Thermoplasma acidophilum
Mg2+ Ta-cpn R1 hydrolyzes ATP in the presence of Co2+, Mn2+, or Mg2+ Thermoplasma acidophilum
Mn2+ Ta-cpn beta1 shows ATPase activity in the presence of Co2+. A weak ATPase activity is observed in the presence of Mn2+ or Mg2+ Thermoplasma acidophilum
Mn2+ Ta-cpn R1 hydrolyzes ATP in the presence of Co2+, Mn2+, or Mg2+ Thermoplasma acidophilum

Organism

Organism UniProt Comment Textmining
Thermoplasma acidophilum P48424 chaperonin alpha-subunit
-
Thermoplasma acidophilum P48425 chaperonin beta-subunit
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermoplasma acidophilum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + H2O + a folded polypeptide ADPase activity in presence of Co2+, almost no hydrolysis in presence of Mn2+ or Mg2+, monomeric enzyme form Thermoplasma acidophilum AMP + phosphate + an unfolded polypeptide
-
?
ADP + H2O + a folded polypeptide ADPase activity in presence of Co2+, Mn2+ or Mg2+, monomeric enzyme form Thermoplasma acidophilum AMP + phosphate + an unfolded polypeptide
-
?
AMP + H2O AMPase activity in presence of Co2+, almost no hydrolysis in presence of Mn2+ or Mg2+, monomeric enzyme form Thermoplasma acidophilum adenosine + phosphate
-
?
AMP + H2O AMPase activity in presence of Co2+, Mn2+ or Mg2+, monomeric enzyme form Thermoplasma acidophilum adenosine + phosphate
-
?
ATP + H2O + a folded polypeptide
-
Thermoplasma acidophilum ADP + phosphate + an unfolded polypeptide
-
?
CTP + H2O + a folded polypeptid
-
Thermoplasma acidophilum CDP + phosphate + an unfolded polypeptide
-
?
CTP + H2O + a folded polypeptide
-
Thermoplasma acidophilum CDP + phosphate + an unfolded polypeptide
-
?
GTP + H2O + a folded polypeptide
-
Thermoplasma acidophilum GDP + phosphate + an unfolded polypeptide
-
?
IDP + H2O + a folded polypeptide
-
Thermoplasma acidophilum IMP + phosphate + an unfolded polypeptide
-
?
ITP + H2O + a folded polypeptide
-
Thermoplasma acidophilum IDP + phosphate + an unfolded polypeptide
-
?
UTP + H2O + a folded polypeptide
-
Thermoplasma acidophilum UDP + phosphate + an unfolded polypeptide
-
?

Synonyms

Synonyms Comment Organism
Ta-cpn alpha1 monomeric enzyme form Thermoplasma acidophilum
Ta-cpn beta1 monomeric enzyme form Thermoplasma acidophilum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
Thermoplasma acidophilum