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Literature summary extracted from

  • Kim, J.H.; Lee, J.W.; Shin, E.J.; Nam, S.W.
    Cooperativity of alpha- and beta-subunits of group II chaperonin from the hyperthermophilic archaeum Aeropyrum pernix K1 (2011), J. Microbiol. Biotechnol., 21, 212-217.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.4.B10 ApCpnA and ApCpnB chaperonin genes are overexpressed in Escherichia coli Rosetta and Codonplus (DE3), respectively Aeropyrum pernix

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.B10 Aeropyrum pernix Q9YDK6 and Q9YA66 Q9YDK6: alpha-subunit, Q9YA66: beta-subunit
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3.6.4.B10 Aeropyrum pernix DSM 11879 Q9YDK6 and Q9YA66 Q9YDK6: alpha-subunit, Q9YA66: beta-subunit
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Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.4.B10 each of the recombinant alpha- and beta- subunits is purified to 92% and 94% by using anion exchange chromatography Aeropyrum pernix

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.B10 ATP + H2O the enzyme protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively, and malate dehydrogenase from thermal inactivation at 80°C and 85°C. In the presence of ATP, the protective effects of alpha- and beta-subunits on citrate synthase from thermal aggregation and inactivation, and alcohol dehydrogenase from thermal aggregation, are more enhanced, whereas cooperation between chaperonins and ATP in protection activity on alcohol dehydrogenase and malate dehydrogenase (at 85°C) from thermal inactivation is not observed. Specifically, the presence of both alpha- and beta- subunits can effectively protect malate dehydrogenase from thermal inactivation at 80°C in an ATP-dependent manner Aeropyrum pernix ADP + phosphate
-
 ?
3.6.4.B10 ATP + H2O the enzyme protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively, and malate dehydrogenase from thermal inactivation at 80°C and 85°C. In the presence of ATP, the protective effects of alpha- and beta-subunits on citrate synthase from thermal aggregation and inactivation, and alcohol dehydrogenase from thermal aggregation, are more enhanced, whereas cooperation between chaperonins and ATP in protection activity on alcohol dehydrogenase and malate dehydrogenase (at 85°C) from thermal inactivation is not observed. Specifically, the presence of both alpha- and beta- subunits can effectively protect malate dehydrogenase from thermal inactivation at 80°C in an ATP-dependent manner Aeropyrum pernix DSM 11879 ADP + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.4.B10 More the cooperativity of alpha- and beta-subunits is investigated Aeropyrum pernix