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Literature summary for 5.6.1.7 extracted from

  • Guagliardi, A.; Cerchia, L.; Bartolucci, S.; Rossi, M.
    The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro (1994), Protein Sci., 3, 1436-1443.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.7

Metals/Ions

Metals/Ions Comment Organism Structure
K+ required for hydrolysis Saccharolobus solfataricus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
 x * 57000, SDS-PAGE Saccharolobus solfataricus
920000
-
 gel filtration Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide
-
 Saccharolobus solfataricus ADP + phosphate + an unfolded polypeptide
-
 ?
additional information chaperonin completely inhibits spontaneous refoldings of several denatured proteins and suppresses aggregation upon dilution of the denaturant, refoldings resume upon ATP hydrolysis, with yields of active molecules and rates of folding notably higher than in spontaneous processes. Chaperonin prevents the irreversible inactivations at 90°C of several thermophilic enzymes by the binding of the denaturation intermediate, the timecourses of inactivations are unaffected and most activity is regained upon hydrolysis of ATP. Chaperonin completely prevents the formation of aggregates during thermal inactivation of chicken egg white lysozyme at 70°C, without affecting the rate of activity loss. ATP hydrolysis results in the recovery of most lytic activity Saccharolobus solfataricus ?
-
 ?

Subunits

Subunits Comment Organism
? x * 57000, SDS-PAGE Saccharolobus solfataricus
More enzyme undergoes a dramatic conformational rearrangement in the presence of ATP/Mg, and hydrolysis of ATP is not required for the conformational change. The ATP/Mg-induced conformation of the chaperonin is fully unable to bind the protein substrate Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
-
 Saccharolobus solfataricus