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

BRENDA support

Literature summary for 5.6.1.7 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
Search for more literature for 5.6.1.7

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
Superose 6 column chromatography Thermoplasma acidophilum

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
heterohexadecamer
-
 Thermoplasma acidophilum

Synonyms

Synonyms Comment Organism
chaperonin
-
 Thermoplasma acidophilum
thermosome
-
 Thermoplasma acidophilum