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Literature summary for 3.6.4.B10 extracted from

  • Yan, Z.; Fujiwara, S.; Kohda, K.; Takagi, M.; Imanaka, T.
    In vitro stabilization and in vivo solubilization of foreign proteins by the beta subunit of a chaperonin from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1 (1997), Appl. Environ. Microbiol., 63, 785-789.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.B10

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Thermococcus kodakarensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59140
-
 x * 59140, calculatzed from sequence Thermococcus kodakarensis
60000
-
 x * 60000, SDS-PAGE Thermococcus kodakarensis

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q52500
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermococcus kodakarensis

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O = ADP + phosphate enzymes exists as a homooligomer in a double-ring structure, which captures non-native proteins in a central cavity to promote correct folding in an ATP-dependent manner Thermococcus kodakarensis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O the enzyme prevents thermal denaturation and enhances thermostability of Saccharomyces cerevisiae alcohol dehydrogenase. CpkB requires ATP for its chaperonin function at a low CpkB concentration. CpkB functions without ATP when present in excess. CpkB is useful for solubilizing insoluble proteins in vivo Thermococcus kodakarensis ADP + phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 60000, SDS-PAGE Thermococcus kodakarensis
? x * 59140, calculatzed from sequence Thermococcus kodakarensis

Synonyms

Synonyms Comment Organism
CpkB beta subunit of a molecular chaperonin Thermococcus kodakarensis