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Literature summary extracted from

  • Lee, J.W.; Kim, S.W.; Kim, J.H.; Jeon, S.J.; Kwon, H.J.; Kim, B.W.; Nam, S.W.
    Functional characterization of the alpha- and beta-subunits of a group II chaperonin from Aeropyrum pernix K1 (2013), J. Microbiol. Biotechnol., 23, 818-825.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.4.B10 expression of ApCpnA (subunit alpha) and ApCpnB (subunit beta) in Escherichia coli Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) cells Aeropyrum pernix
3.6.4.B10 gene thsA, recombinant expression of alpha-subunit in Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) Aeropyrum pernix
3.6.4.B10 gene thsB, recombinant expression of beta-subunit in Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) Aeropyrum pernix

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.4.B10 K+ activates Aeropyrum pernix
3.6.4.B10 K+ ATPase activity of the two chaperonin subunits is dependent on the salt concentration. Among the ions examined, K+ are the most effective at enhancing the ATP hydrolysis activity of ApCpnA and ApCpnB. Activity is maximal at 200 mM K+ Aeropyrum pernix
3.6.4.B10 Mg2+ required Aeropyrum pernix
3.6.4.B10 Mn2+ activates Aeropyrum pernix
3.6.4.B10 additional information the ATPase activity of the two chaperonin subunits is dependent on the salt concentration. Potassium ions are the most effective at enhancing the ATP hydrolysis activity of ApCpnA and ApCpnB, activity is maximal at 200 mM K+ Aeropyrum pernix
3.6.4.B10 Na+ activates Aeropyrum pernix
3.6.4.B10 NH4+ activates Aeropyrum pernix

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.4.B10 60700
-
 x * 60700 (subunit alpha) + x * 61200 (subunit beta), SDS-PAGE Aeropyrum pernix
3.6.4.B10 60700
-
 x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE Aeropyrum pernix
3.6.4.B10 61200
-
 x * 60700 (subunit alpha) + x * 61200 (subunit beta), SDS-PAGE Aeropyrum pernix
3.6.4.B10 61200
-
 x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE Aeropyrum pernix

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.4.B10 ATP + H2O Aeropyrum pernix
-
 ADP + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.B10 Aeropyrum pernix Q9YA66 beta-subunit ApCpnB; gene thsB
-
3.6.4.B10 Aeropyrum pernix Q9YDK6 alpha-subunit ApCpnA; gene thsA
-
3.6.4.B10 Aeropyrum pernix Q9YDK6 and Q9YA66 Q9YDK6: alpha-subunit, Q9YA66: beta-subunit
-
3.6.4.B10 Aeropyrum pernix DSM 11879 Q9YDK6 and Q9YA66 Q9YDK6: alpha-subunit, Q9YA66: beta-subunit
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.4.B10 recombinant alpha-subunit from Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) by heat shock treatment and anion exchange chromatography Aeropyrum pernix
3.6.4.B10 recombinant beta-subunit from Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) by heat shock treatment and anion exchange chromatography Aeropyrum pernix
3.6.4.B10 recombinant subunit alpha and subunit beta Aeropyrum pernix

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.B10 ATP + H2O
-
 Aeropyrum pernix ADP + phosphate
-
 ?
3.6.4.B10 ATP + H2O addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP Aeropyrum pernix ADP + phosphate
-
 ?
3.6.4.B10 ATP + H2O addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP Aeropyrum pernix DSM 11879 ADP + phosphate
-
 ?
3.6.4.B10 CTP + H2O
-
 Aeropyrum pernix CDP + phosphate
-
 ?
3.6.4.B10 CTP + H2O addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP Aeropyrum pernix CDP + phosphate
-
 ?
3.6.4.B10 CTP + H2O addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP Aeropyrum pernix DSM 11879 CDP + phosphate
-
 ?
3.6.4.B10 GTP + H2O
-
 Aeropyrum pernix GDP + phosphate
-
 ?
3.6.4.B10 GTP + H2O addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP Aeropyrum pernix GDP + phosphate
-
 ?
3.6.4.B10 GTP + H2O addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP Aeropyrum pernix DSM 11879 GDP + phosphate
-
 ?
3.6.4.B10 additional information subunits ApCpnA and ApCpnB are able to hydrolyze not only ATP, but also CTP, GTP, and UTP, albeit with different efficacies. Addition of subunits ApCpnA and ApCpnB effectively protects porcine heart citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. In particular, the addition of ATP or CTP to subunits ApCpnA and ApCpnB results in the most effective prevention of thermal aggregation and inactivation of the substrate proteins Aeropyrum pernix ?
-
 ?
3.6.4.B10 UTP + H2O
-
 Aeropyrum pernix UDP + phosphate
-
 ?
3.6.4.B10 UTP + H2O addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP Aeropyrum pernix UDP + phosphate
-
 ?
3.6.4.B10 UTP + H2O addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP Aeropyrum pernix DSM 11879 UDP + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.4.B10 ? x * 60700 (subunit alpha) + x * 61200 (subunit beta), SDS-PAGE Aeropyrum pernix
3.6.4.B10 More x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE Aeropyrum pernix

Synonyms

EC Number Synonyms Comment Organism
3.6.4.B10 group II chaperonin
-
 Aeropyrum pernix
3.6.4.B10 thermosome
-
 Aeropyrum pernix

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.4.B10 80
-
-
 Aeropyrum pernix
3.6.4.B10 80
-
 recombinant enzyme Aeropyrum pernix

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.6.4.B10 70 85 70°C: about 60% of maximal actiovity, 85°C: about 40% of maximal activity Aeropyrum pernix

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.4.B10 5
-
 ATPase assay at Aeropyrum pernix
3.6.4.B10 7.5 8 thermal protection assay at Aeropyrum pernix

General Information

EC Number General Information Comment Organism
3.6.4.B10 additional information group II chaperonins exist as an 8- or 9-membered rotationally symmetrical double-ring in a toridal structure composed of homologous subunits of about 60 kDa. Each ring has a large central cavity in which a non-native protein can undergo productive folding in an ATP-dependent manner. A unique structural feature, termed the helical protrusion, acts as a built-in lid to seal off the central cavity of group II chaperonins during folding. Opening and closing of the folding chamber is controlled by a conformational cycle driven by ATP binding and hydrolysis. All chaperonins share a similar subunit architecture consisting of three distinct domains as follows: an ATP-binding equatorial domain, a distal apical domain harboring the polypeptide-binding sites, and an intermediate hinge domain Aeropyrum pernix
3.6.4.B10 physiological function chaperonins are ubiquitous chaperones that are required for correct protein folding, assembly, and degradation Aeropyrum pernix