Literature summary extracted from

Shin, E.J.; Lee, J.W.; Kim, J.H.; Jeon, S.J.; Kim, Y.H.; Nam, S.W.
Overexpression, purification, and characterization of beta-subunit group II chaperonin from hyperthermophilic Aeropyrum pernix K1 (2010), J. Microbiol. Biotechnol., 20, 542-549.

Application

EC Number	Application	Comment	Organism
3.6.4.B10	synthesis	ApCpnB has both foldase and holdase activities and can be used as a powerful molecular machinery for the production of recombinant proteins as soluble and active forms in Escherichia coli	Aeropyrum pernix K1

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
3.6.4.B10	subcloned into vector pET21a. The constructed pET21a-ApCpnB is transformed into Escherichia coli BL21 Codonplus (DE3)	Aeropyrum pernix K1

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
3.6.4.B10	61200	-	x * 61200, SDS-PAGE	Aeropyrum pernix K1

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.6.4.B10	Aeropyrum pernix K1	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
3.6.4.B10	recombinant enzyme	Aeropyrum pernix K1

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.6.4.B10	ATP + H2O	in the presence of ATP, ApCpnB effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Specifically, the activity of malate dehydrogenase (MDH) at 85°C is greatly stabilized by the addition of ApCpnB and ATP	Aeropyrum pernix K1	ADP + phosphate	-	?

Subunits

EC Number	Subunits	Comment	Organism
3.6.4.B10	?	x * 61200, SDS-PAGE	Aeropyrum pernix K1

Synonyms

EC Number	Synonyms	Comment	Organism
3.6.4.B10	ApCpnB	-	Aeropyrum pernix K1
3.6.4.B10	chaperonin B	-	Aeropyrum pernix K1

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Release 2023.1 (January 2023)