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Literature summary extracted from

  • Shoemark, D.K.; Sessions, R.B.; Brancaccio, A.; Bigotti, M.G.
    Intraring allostery controls the function and assembly of a hetero-oligomeric class II chaperonin (2018), FASEB J., 32, 2223-2234 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.6.1.7 expressed in Escherichia coli BL21(DE3) Codon Plus-RIL cells Thermoplasma acidophilum

Protein Variants

EC Number Protein Variants Comment Organism
5.6.1.7 D93K the mutation of the beta subunit blocks ATP hydrolysis. The mutant has 43% of wild type protein refolding activity Thermoplasma acidophilum
5.6.1.7 D94A the mutation of the alpha subunit blocks ATP hydrolysis. The mutant has 32% of wild type protein refolding activity Thermoplasma acidophilum
5.6.1.7 D94K the mutation of the alpha subunit blocks ATP hydrolysis. The mutant has 31% of wild type protein refolding activity Thermoplasma acidophilum
5.6.1.7 T157A the mutation of the alpha subunit blocks ATP binding. The mutant has 30.5% of wild type protein refolding activity Thermoplasma acidophilum
5.6.1.7 T158A the mutation of the beta subunit blocks ATP binding. The mutant has 62.6% of wild type protein refolding activity Thermoplasma acidophilum
5.6.1.7 T96V the mutation of the beta subunit blocks ATP binding. The mutant has 44% of wild type protein refolding activity Thermoplasma acidophilum
5.6.1.7 T97V the mutation of the alpha subunit blocks ATP binding. The mutant has no activity Thermoplasma acidophilum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.6.1.7 0.015
-
 ATP wild type enzyme, with rhamnose dehydrogenase as protein substrate, at pH 7.5 and 55°C Thermoplasma acidophilum
5.6.1.7 0.082
-
 ATP mutant enzyme D94A, with rhamnose dehydrogenase as protein substrate, at pH 7.5 and 55°C Thermoplasma acidophilum
5.6.1.7 0.285
-
 ATP mutant enzyme D93K, with rhamnose dehydrogenase as protein substrate, at pH 7.5 and 55°C Thermoplasma acidophilum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.6.1.7 K+ 50 mM used in assay conditions Thermoplasma acidophilum
5.6.1.7 Mg2+ 20 mM used in assay conditions Thermoplasma acidophilum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.6.1.7 ATP + H2O + a folded polypeptide Thermoplasma acidophilum
-
 ADP + phosphate + an unfolded polypeptide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.6.1.7 Thermoplasma acidophilum P48424 subunit alpha
-
5.6.1.7 Thermoplasma acidophilum P48425 subunit beta
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.1.7 Superose 6 column chromatography Thermoplasma acidophilum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.1.7 ATP + H2O + a folded polypeptide
-
 Thermoplasma acidophilum ADP + phosphate + an unfolded polypeptide
-
 ?
5.6.1.7 ATP + H2O + folded aldohexose dehydrogenase
-
 Thermoplasma acidophilum ADP + phosphate + unfolded aldohexose dehydrogenase
-
 ?
5.6.1.7 ATP + H2O + folded rhamnose dehydrogenase
-
 Thermoplasma acidophilum ADP + phosphate + unfolded rhamnose dehydrogenase
-
 ?

Subunits

EC Number Subunits Comment Organism
5.6.1.7 heterohexadecamer
-
 Thermoplasma acidophilum

Synonyms

EC Number Synonyms Comment Organism
5.6.1.7 chaperonin
-
 Thermoplasma acidophilum
5.6.1.7 thermosome
-
 Thermoplasma acidophilum