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Literature summary for 3.6.4.B10 extracted from
- Functional characterization of the alpha- and beta-subunits of a group II chaperonin from Aeropyrum pernix K1 (2013), J. Microbiol. Biotechnol., 23, 818-825.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of ApCpnA (subunit alpha) and ApCpnB (subunit beta) in Escherichia coli Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) cells | Aeropyrum pernix |
| gene thsA, recombinant expression of alpha-subunit in Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) | Aeropyrum pernix |
| gene thsB, recombinant expression of beta-subunit in Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) | Aeropyrum pernix |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| K+ | activates | Aeropyrum pernix |  |
| 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 | |
| Mg2+ | required | Aeropyrum pernix | |
| Mn2+ | activates | Aeropyrum pernix | |
| 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 | |
| Na+ | activates | Aeropyrum pernix | |
| NH4+ | activates | Aeropyrum pernix | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 60700 | - |
x * 60700 (subunit alpha) + x * 61200 (subunit beta), SDS-PAGE | Aeropyrum pernix |
| 60700 | - |
x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE | Aeropyrum pernix |
| 61200 | - |
x * 60700 (subunit alpha) + x * 61200 (subunit beta), SDS-PAGE | Aeropyrum pernix |
| 61200 | - |
x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE | Aeropyrum pernix |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Aeropyrum pernix | - |
ADP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aeropyrum pernix | Q9YA66 | beta-subunit ApCpnB; gene thsB | - |
| Aeropyrum pernix | Q9YDK6 | alpha-subunit ApCpnA; gene thsA | - |
| Aeropyrum pernix | Q9YDK6 and Q9YA66 | Q9YDK6: alpha-subunit, Q9YA66: beta-subunit | - |
| Aeropyrum pernix DSM 11879 | Q9YDK6 and Q9YA66 | Q9YDK6: alpha-subunit, Q9YA66: beta-subunit | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant alpha-subunit from Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) by heat shock treatment and anion exchange chromatography | Aeropyrum pernix |
| recombinant beta-subunit from Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) by heat shock treatment and anion exchange chromatography | Aeropyrum pernix |
| recombinant subunit alpha and subunit beta | Aeropyrum pernix |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Aeropyrum pernix | ADP + phosphate | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| CTP + H2O | - |
Aeropyrum pernix | CDP + phosphate | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| GTP + H2O | - |
Aeropyrum pernix | GDP + phosphate | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | ? | - |
? | |
| UTP + H2O | - |
Aeropyrum pernix | UDP + phosphate | - |
? | |
| 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 | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 60700 (subunit alpha) + x * 61200 (subunit beta), SDS-PAGE | Aeropyrum pernix |
| More | x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE | Aeropyrum pernix |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| group II chaperonin | - |
Aeropyrum pernix |
| thermosome | - |
Aeropyrum pernix |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
- |
Aeropyrum pernix |
| 80 | - |
recombinant enzyme | Aeropyrum pernix |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | 85 | 70°C: about 60% of maximal actiovity, 85°C: about 40% of maximal activity | Aeropyrum pernix |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
ATPase assay at | Aeropyrum pernix |
| 7.5 | 8 | thermal protection assay at | Aeropyrum pernix |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| physiological function | chaperonins are ubiquitous chaperones that are required for correct protein folding, assembly, and degradation | Aeropyrum pernix |
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