Literature summary for 3.6.4.B10 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.

Search for more literature for 3.6.4.B10

Cloned(Commentary)

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

Organism

Organism	UniProt	Comment	Textmining
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
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
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

Subunits	Comment	Organism
More	the cooperativity of alpha- and beta-subunits is investigated	Aeropyrum pernix

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)